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Conserved domains on  [gi|115534176|ref|NP_498263|]
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Putative aldehyde dehydrogenase family 7 member A1 homolog [Caenorhabditis elegans]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
43-519 0e+00

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


:

Pssm-ID: 143448  Cd Length: 474  Bit Score: 927.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  43 GVFHGKWAASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLV 122
Cdd:cd07130    1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 123 SLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTG 202
Cdd:cd07130   81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 203 NSVVWKPAPSTPLTAIAVTKLVEEVLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGK 282
Cdd:cd07130  161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 283 LLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIG 362
Cdd:cd07130  241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV--RIGDPLDDGTLVG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 363 PLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDsPVVLRETFAPILYVLKFSTLEEAIAINNE 442
Cdd:cd07130  319 PLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDTLEEAIAWNNE 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115534176 443 VDQGLSSSLFTTNIQNVFKWMGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRSTCTINYS 519
Cdd:cd07130  398 VPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
 
Name Accession Description Interval E-value
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
43-519 0e+00

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 927.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  43 GVFHGKWAASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLV 122
Cdd:cd07130    1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 123 SLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTG 202
Cdd:cd07130   81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 203 NSVVWKPAPSTPLTAIAVTKLVEEVLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGK 282
Cdd:cd07130  161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 283 LLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIG 362
Cdd:cd07130  241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV--RIGDPLDDGTLVG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 363 PLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDsPVVLRETFAPILYVLKFSTLEEAIAINNE 442
Cdd:cd07130  319 PLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDTLEEAIAWNNE 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115534176 443 VDQGLSSSLFTTNIQNVFKWMGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRSTCTINYS 519
Cdd:cd07130  398 VPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
28-530 0e+00

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 693.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  28 KYGFLKELGLTENNAGVF-HGKWAASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQ 106
Cdd:PLN02315   7 EYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 107 IGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNF 186
Cdd:PLN02315  87 IGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 187 PCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSS 266
Cdd:PLN02315 167 PCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSS 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 267 EIGKIVGQQVQARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQ 346
Cdd:PLN02315 247 KVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 347 FesRIGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTgLKHDSPVVLRETFAPILY 426
Cdd:PLN02315 327 V--KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLY 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 427 VLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKWMGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWR 506
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWK 483
                        490       500
                 ....*....|....*....|....
gi 115534176 507 QYMRRSTCTINYSKELPLAQGIKF 530
Cdd:PLN02315 484 QYMRRSTCTINYGNELPLAQGINF 507
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
50-513 2.52e-158

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 249650  Cd Length: 459  Bit Score: 462.00  E-value: 2.52e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176   50 AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKI 129
Cdd:pfam00171   3 DSSSETIEVINPATGEVIATVPAATAEDVDAAVAAARAAFKAWAKTPPAERAAILRKAADLLEERRDELAELETLETGKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  130 SAEGVGEVQEYVDICDYATGLSRSLEGKIFPSeRPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKP 209
Cdd:pfam00171  83 LAEARGEVPRAIDTLRYYAGLARKLEGETLPS-DPGVLAYTRREPLGVVGAITPWNFPLLLAAWKIAPALAAGNTVVLKP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  210 APSTPLTAIAVTKLVEEVLVANNVnpalCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELG 288
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGV----LNVVTGSGsEVGDALVEHPDVDKVSFTGSTEVGRRIAKAAAKNLKRVTLELG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  289 GNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQ 368
Cdd:pfam00171 238 GKNPLIVFDDADLDAAVEAAVFGAFGNAGQVCTAGSRLLVHESIYDEFVERLVEAAKSL--KVGDPLDPDTDIGPLISKA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  369 AVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLS 448
Cdd:pfam00171 316 QRERVLSYIEDAKEEGAKLLCGGEAGLEKGYFVEPTVLADVTPDMRIAQEEIFGPVLSVIPFKDEEEAIELANDTEYGLA 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115534176  449 SSLFTTNIQNVFKWMgpKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRST 513
Cdd:pfam00171 396 AGVFTNDLERALRVA--RRLEAGMVWINDYTTGDPEALPFGGFKQSGFGREGGKEGLEEYTETKT 458
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
47-519 1.35e-143

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 223944  Cd Length: 472  Bit Score: 424.79  E-value: 1.35e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKWAASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEM 126
Cdd:COG1012    7 GEWVDGASTIEVINPATGEVIATVPAATAEDVDAAVAAARAAFEAWSRLSAEERAAILRRIADLLEARAEELAALITLET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 127 GKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPsERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVV 206
Cdd:COG1012   87 GKPISEARGEIARAADFIRYYAEEARRLEGETIP-TDKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 207 WKPAPSTPLTAIAVTKLVEEVLVANNVnpalCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLL 285
Cdd:COG1012  166 LKPSEQTPLSALALAELAAEAGLPAGV----LNVVTGGGaEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANLKPVTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 286 ELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYaqFESRIGCPLDSNTIIGPLH 365
Cdd:COG1012  242 ELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARA--ASLKVGDPLDPSTDLGPLI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 366 NQQAVGKYKASVAEAVASGGKIEYGGKVLerDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQ 445
Cdd:COG1012  320 SEEQLDRVEGYIEDAVAEGARLLAGGKRP--GGYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELANDTEY 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115534176 446 GLSSSLFTTNIQNVFKWMgpKGSDCGIVNVNIPTSGAEIGGA-FGGEKETGGGRESGSDSWRQYMRRSTCTINYS 519
Cdd:COG1012  398 GLAAAIFTRDLARAFRVA--RRLEAGMVGINDYTGGADIAYLpFGGVKQSGLGREGGKYGLEEFTEVKTVTIKLG 470
SSADH TIGR01780
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ...
61-509 3.34e-81

succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 & G-242, C-293 & G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]


Pssm-ID: 188167  Cd Length: 448  Bit Score: 262.75  E-value: 3.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176   61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:TIGR01780   4 PATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEILYA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  141 VDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAV 220
Cdd:TIGR01780  84 ASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSALAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  221 TKLVEEVLVANNV-NPALCSLVcgeGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDA 299
Cdd:TIGR01780 164 ARLAEQAGIPKGVlNVITGSRA---KEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  300 DLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAE 379
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKL--KVGNGLDEGVTQGPLINEKAVEKVEKHIAD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  380 AVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNV 459
Cdd:TIGR01780 319 AVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRI 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 115534176  460 fkWMGPKGSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRESGSDSWRQYM 509
Cdd:TIGR01780 399 --WRVAEALEYGMVGINTGLISNVV-APFGGVKQSGLGREGSKYGIEEYL 445
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
50-510 1.31e-61

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 212.75  E-value: 1.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  50 AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYND--WCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMG 127
Cdd:PLN02466  69 AASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 128 KISAEGVG-EVQEYVDICDYATGLSRSLEGKIFPSERPgHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVV 206
Cdd:PLN02466 149 KPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGP-HHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIV 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 207 WKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVgQQVQAR--FGKL 283
Cdd:PLN02466 228 LKTAEQTPLSALYAAKLLHEA----GLPPGVLNVVSGFGpTAGAALASHMDVDKLAFTGSTDTGKIV-LELAAKsnLKPV 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 284 LLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLErlkKAYAQFESR-IGCPLDSNTIIG 362
Cdd:PLN02466 303 TLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVE---KAKARALKRvVGDPFKKGVEQG 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 363 PLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNE 442
Cdd:PLN02466 380 PQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANN 459
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115534176 443 VDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVN--------IPtsgaeiggaFGGEKETGGGRESGSDSWRQYMR 510
Cdd:PLN02466 460 TRYGLAAGVFTQNLDTANTLS--RALRVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
47-501 4.92e-57

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 226683 [Multi-domain]  Cd Length: 769  Bit Score: 203.40  E-value: 4.92e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKWAASGQVVQSFAPANNSPI-ANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLE 125
Cdd:COG4230  120 GAPVAGGEPRPVINPADPDDIvGTVTEATEADVEQALEAAVAAAPIWSATPPAERAAILERAADLMEAQMPQLMGLLVRE 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 126 MGKISAEGVGEVQEYVDICDYATGLSRSlegkifPSERPGHAlleqwnPLGVVGVISAFNFPCAVYGWNNALALVTGNSV 205
Cdd:COG4230  200 AGKTLSNAIAEVREAVDFLRYYAGQARD------TFGNLTHR------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 206 VWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGK-- 282
Cdd:COG4230  268 LAKPAEQTPLIAAQAVRLLHEA----GVPPGVLQLLPGRGeTVGAALTADARVAGVMFTGSTEVARLIQRQLAKRQGRpi 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 283 -LLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAqfESRIGCPLDSNTII 361
Cdd:COG4230  344 pLIAETGGQNAMIVDSSALAEQVVADVLASAFDSAGQRCSALRVLCLQEDVADRILTMLKGAMA--ELRVGNPDRLTTDV 421
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 362 GPLHNQQAvgkyKASVA---EAVASGGKIEYGGKV--LERDGNFVLPTI--VTGLKHdspvVLRETFAPILYVLKF--ST 432
Cdd:COG4230  422 GPVIDAEA----KANIEkhiQTMRSKGRLVHQAAApnSLQKGTFVAPTLieLENLDE----LQREVFGPVLHVVRYkrDE 493
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 433 LEEAIAINNEVDQGLSSSLFTTNIQNVFKWMGpkGSDCGIVNVNIPTSGAEIG-GAFGGEKETGGGRESG 501
Cdd:COG4230  494 LDEVIDQINATGYGLTLGVHTRIDETIAHVTE--RAHAGNLYVNRNIVGAVVGvQPFGGEGLSGTGPKAG 561
PaaN-DH TIGR02278
phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening ...
174-512 1.35e-24

phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardized in. This enzyme is related to aldehyde dehydrogenases and has domains which are members of the pfam00171 and pfam01575 families. This family includes paaN genes from Pseudomonas, Sinorhizobium, Rhodopseudomonas, Escherichia, Deinococcus and Corynebacterium. Another homology family (TIGR02288) includes several other species.


Pssm-ID: 131331 [Multi-domain]  Cd Length: 663  Bit Score: 106.45  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  174 PLGVVGV-ISAFNFPCavygWNN----ALALVTGNSVVWKPAPSTPLTAIAVTKLVEEvlvANNVNPALCSLVCGE-GDV 247
Cdd:TIGR02278 143 PKGGVAVqINAFNFPV----WGLlekfAPAFLAGVPTLAKPATPTAYVAEALVRTMVE---SGLLPEGSLQLICGSaGDL 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  248 GQALvkDKRvNLVSFTGSSEIGKIVGQQ--VQARFGKLLLELGGNNAIIVNEDA-----DLNMVVPATVFAAVGTAGQRC 320
Cdd:TIGR02278 216 LDHL--DHR-DVVAFTGSAATADRLRAHpnVLERGIRFNAEADSLNAAILGEDAtpdepEFDLFAQEIVRELTIKAGQKC 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  321 TTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVlERDGNF 400
Cdd:TIGR02278 293 TAIRRVIVPKALLEAVLKALQARLAKV--VLGDPREEGVDMGPLVSLEQRADVEAAVAALLAAGAEVRLGGPG-RLDGAF 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  401 VLPTIVTGLKHDSPVVLR-ETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKWMGPKGSDCGIVNVNIPT 479
Cdd:TIGR02278 370 FPPTLLLAEDPWAGAVHAtEAFGPVATFFPYGDRAEAARLAARGGGSLVATLATSDPEEARQFILGLAPYHGRLHILNRD 449
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 115534176  480 SGAEIGG--------AFGGEKETGGGRE-SGSDSWRQYMRRS 512
Cdd:TIGR02278 450 DAAESTGhgsplprlLHGGPGRAGGGEElGGLRSVKHYMQRT 491
 
Name Accession Description Interval E-value
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
43-519 0e+00

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 927.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  43 GVFHGKWAASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLV 122
Cdd:cd07130    1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 123 SLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTG 202
Cdd:cd07130   81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 203 NSVVWKPAPSTPLTAIAVTKLVEEVLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGK 282
Cdd:cd07130  161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 283 LLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIG 362
Cdd:cd07130  241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV--RIGDPLDDGTLVG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 363 PLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDsPVVLRETFAPILYVLKFSTLEEAIAINNE 442
Cdd:cd07130  319 PLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDTLEEAIAWNNE 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115534176 443 VDQGLSSSLFTTNIQNVFKWMGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRSTCTINYS 519
Cdd:cd07130  398 VPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
43-519 0e+00

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405  Cd Length: 478  Bit Score: 868.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  43 GVFHGKWAASG-QVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKL 121
Cdd:cd07086    1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 122 VSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVT 201
Cdd:cd07086   81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 202 GNSVVWKPAPSTPLTAIAVTKLVEEVLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFG 281
Cdd:cd07086  161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 282 KLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTII 361
Cdd:cd07086  241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQV--RIGDPLDEGTLV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 362 GPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLER--DGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAI 439
Cdd:cd07086  319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 440 NNEVDQGLSSSLFTTNIQNVFKWMGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRSTCTINYS 519
Cdd:cd07086  399 NNDVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
28-530 0e+00

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 693.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  28 KYGFLKELGLTENNAGVF-HGKWAASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQ 106
Cdd:PLN02315   7 EYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 107 IGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNF 186
Cdd:PLN02315  87 IGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 187 PCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSS 266
Cdd:PLN02315 167 PCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSS 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 267 EIGKIVGQQVQARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQ 346
Cdd:PLN02315 247 KVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 347 FesRIGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTgLKHDSPVVLRETFAPILY 426
Cdd:PLN02315 327 V--KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLY 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 427 VLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKWMGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWR 506
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWK 483
                        490       500
                 ....*....|....*....|....
gi 115534176 507 QYMRRSTCTINYSKELPLAQGIKF 530
Cdd:PLN02315 484 QYMRRSTCTINYGNELPLAQGINF 507
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
50-513 2.52e-158

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 249650  Cd Length: 459  Bit Score: 462.00  E-value: 2.52e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176   50 AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKI 129
Cdd:pfam00171   3 DSSSETIEVINPATGEVIATVPAATAEDVDAAVAAARAAFKAWAKTPPAERAAILRKAADLLEERRDELAELETLETGKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  130 SAEGVGEVQEYVDICDYATGLSRSLEGKIFPSeRPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKP 209
Cdd:pfam00171  83 LAEARGEVPRAIDTLRYYAGLARKLEGETLPS-DPGVLAYTRREPLGVVGAITPWNFPLLLAAWKIAPALAAGNTVVLKP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  210 APSTPLTAIAVTKLVEEVLVANNVnpalCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELG 288
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGV----LNVVTGSGsEVGDALVEHPDVDKVSFTGSTEVGRRIAKAAAKNLKRVTLELG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  289 GNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQ 368
Cdd:pfam00171 238 GKNPLIVFDDADLDAAVEAAVFGAFGNAGQVCTAGSRLLVHESIYDEFVERLVEAAKSL--KVGDPLDPDTDIGPLISKA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  369 AVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLS 448
Cdd:pfam00171 316 QRERVLSYIEDAKEEGAKLLCGGEAGLEKGYFVEPTVLADVTPDMRIAQEEIFGPVLSVIPFKDEEEAIELANDTEYGLA 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115534176  449 SSLFTTNIQNVFKWMgpKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRST 513
Cdd:pfam00171 396 AGVFTNDLERALRVA--RRLEAGMVWINDYTTGDPEALPFGGFKQSGFGREGGKEGLEEYTETKT 458
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
81-516 5.08e-155

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397  Cd Length: 432  Bit Score: 452.82  E-value: 5.08e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  81 AISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFP 160
Cdd:cd07078    3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 161 SERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVLVAnnvnPALCSL 240
Cdd:cd07078   83 SPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLP----PGVLNV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 241 VCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQR 319
Cdd:cd07078  159 VTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 320 CTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERD-G 398
Cdd:cd07078  239 CTAASRLLVHESIYDEFVERLVERVKAL--KVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkG 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 399 NFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVNIP 478
Cdd:cd07078  317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDY 394
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 115534176 479 TSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRSTCTI 516
Cdd:cd07078  395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
47-519 1.35e-143

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 223944  Cd Length: 472  Bit Score: 424.79  E-value: 1.35e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKWAASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEM 126
Cdd:COG1012    7 GEWVDGASTIEVINPATGEVIATVPAATAEDVDAAVAAARAAFEAWSRLSAEERAAILRRIADLLEARAEELAALITLET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 127 GKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPsERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVV 206
Cdd:COG1012   87 GKPISEARGEIARAADFIRYYAEEARRLEGETIP-TDKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 207 WKPAPSTPLTAIAVTKLVEEVLVANNVnpalCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLL 285
Cdd:COG1012  166 LKPSEQTPLSALALAELAAEAGLPAGV----LNVVTGGGaEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANLKPVTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 286 ELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYaqFESRIGCPLDSNTIIGPLH 365
Cdd:COG1012  242 ELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARA--ASLKVGDPLDPSTDLGPLI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 366 NQQAVGKYKASVAEAVASGGKIEYGGKVLerDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQ 445
Cdd:COG1012  320 SEEQLDRVEGYIEDAVAEGARLLAGGKRP--GGYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELANDTEY 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115534176 446 GLSSSLFTTNIQNVFKWMgpKGSDCGIVNVNIPTSGAEIGGA-FGGEKETGGGRESGSDSWRQYMRRSTCTINYS 519
Cdd:COG1012  398 GLAAAIFTRDLARAFRVA--RRLEAGMVGINDYTGGADIAYLpFGGVKQSGLGREGGKYGLEEFTEVKTVTIKLG 470
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
47-519 1.74e-130

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449  Cd Length: 478  Bit Score: 391.71  E-value: 1.74e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKW--AASGQVVQSFAPANNSP-IANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVS 123
Cdd:cd07131    5 GEWvdSASGETFDSRNPADLEEvVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 124 LEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGN 203
Cdd:cd07131   85 REMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 204 SVVWKPAPSTPLTAiavTKLVEeVLVANNVNPALCSLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVqARFGK 282
Cdd:cd07131  165 TVVFKPAEDTPACA---LKLVE-LFAEAGLPPGVVNVVHGRGEeVGEALVEHPDVDVVSFTGSTEVGERIGETC-ARPNK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 283 LL-LELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTII 361
Cdd:cd07131  240 RVaLEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRL--RVGDGLDEETDM 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 362 GPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERD----GNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAI 437
Cdd:cd07131  318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 438 AINNEVDQGLSSSLFTTNIQNVFKWMGpkgsDC--GIVNVNIPTSGAEIGGAFGGEKETGGG-RESGSDSWRQYMRRSTC 514
Cdd:cd07131  398 EIANDTEYGLSSAIYTEDVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473

                 ....*
gi 115534176 515 TINYS 519
Cdd:cd07131  474 YVDYS 478
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
43-503 3.85e-124

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415  Cd Length: 473  Bit Score: 375.05  E-value: 3.85e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  43 GVFHGKWAASGQVVQSFAPAN-NSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKL 121
Cdd:cd07097    3 NYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 122 VSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVT 201
Cdd:cd07097   83 LTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 202 GNSVVWKPAPSTPLTAIAVTKLVEEV-LVANNVNpalcsLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQAR 279
Cdd:cd07097  163 GNTVVFKPAELTPASAWALVEILEEAgLPAGVFN-----LVMGSGsEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 280 FGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNT 359
Cdd:cd07097  238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKAL--KVGDALDEGV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 360 IIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERD--GNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAI 437
Cdd:cd07097  316 DIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115534176 438 AINNEVDQGLSSSLFTTNIQ--NVFKwmgpKGSDCGIVNVNIPTSGAEIGGAFGGEKETG-GGRESGSD 503
Cdd:cd07097  396 AIANDTEFGLSAGIVTTSLKhaTHFK----RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEA 460
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
85-516 3.19e-122

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395  Cd Length: 367  Bit Score: 366.17  E-value: 3.19e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  85 AKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERP 164
Cdd:cd06534    3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 165 GHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVLVAnnvnPALCSLVCGE 244
Cdd:cd06534   83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLP----PGVVNVVPGG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 245 GD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTT 323
Cdd:cd06534  159 GDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 324 RRLIVHDKVYDQVLERLKkayaqfesrigcpldsntiigplhnqqavgkykasvaeavasggkieyggkvlerdgnfvlp 403
Cdd:cd06534  239 SRLLVHESIYDEFVEKLV-------------------------------------------------------------- 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 404 TIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVNIPTSGAE 483
Cdd:cd06534  257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA--ERLRAGTVYINDSSIGVG 334
                        410       420       430
                 ....*....|....*....|....*....|...
gi 115534176 484 IGGAFGGEKETGGGRESGSDSWRQYMRRSTCTI 516
Cdd:cd06534  335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
47-513 8.91e-113

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407  Cd Length: 468  Bit Score: 345.40  E-value: 8.91e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKW--AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSL 124
Cdd:cd07088    4 GEFvpSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 125 EMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNS 204
Cdd:cd07088   84 EQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 205 VVWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKL 283
Cdd:cd07088  164 IVIKPSEETPLNALEFAELVDEA----GLPAGVLNIVTGRGsVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 284 LLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQfeSRIGCPLDSNTIIGP 363
Cdd:cd07088  240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKA--VKVGDPFDAATDMGP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 364 LHNQQAVGKYKASVAEAVASGGKIEYGGKVLERD-GNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNE 442
Cdd:cd07088  318 LVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115534176 443 VDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVNiPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRST 513
Cdd:cd07088  398 SEYGLTSYIYTENLNTAMRAT--NELEFGETYIN-RENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKV 465
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
61-509 2.58e-112

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421  Cd Length: 451  Bit Score: 343.65  E-value: 2.58e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:cd07103    4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 141 VDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAV 220
Cdd:cd07103   84 ASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALAL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 221 TKLVEEV-LVANNVNpalcsLVCGE-GDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNED 298
Cdd:cd07103  164 AELAEEAgLPAGVLN-----VVTGSpAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 299 ADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVA 378
Cdd:cd07103  239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKL--KVGNGLDEGTDMGPLINERAVEKVEALVE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 379 EAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQN 458
Cdd:cd07103  317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 115534176 459 VFKWMgpKGSDCGIVNVNIPT-SGAEIggAFGGEKETGGGRESGSDSWRQYM 509
Cdd:cd07103  397 AWRVA--EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
77-508 3.83e-103

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422  Cd Length: 431  Bit Score: 319.48  E-value: 3.83e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  77 DYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEG 156
Cdd:cd07104    1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 157 KIFPSERPGhalleQWN-----PLGVVGVISAFNFPC-----AVygwnnALALVTGNSVVWKPAPSTPLT-AIAVTKLVE 225
Cdd:cd07104   81 EILPSDVPG-----KESmvrrvPLGVVGVISPFNFPLilamrSV-----APALALGNAVVLKPDSRTPVTgGLLIAEIFE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 226 E------VLvanNVnpalcsLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDA 299
Cdd:cd07104  151 EaglpkgVL---NV------VPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDA 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 300 DLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAE 379
Cdd:cd07104  222 DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKAL--PVGDPRDPDTVIGPLINERQVDRVHAIVED 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 380 AVASGGKIEYGGKvleRDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNV 459
Cdd:cd07104  300 AVAAGARLLTGGT---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERA 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 115534176 460 FKwMGpKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWRQY 508
Cdd:cd07104  377 MA-FA-ERLETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
58-504 3.53e-99

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468  Cd Length: 451  Bit Score: 309.65  E-value: 3.53e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  58 SFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEV 137
Cdd:cd07150    3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 138 QEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTA 217
Cdd:cd07150   83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 218 IAVTKLVEEVLVANNVnpaLCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNE 297
Cdd:cd07150  163 LKIAEIMEEAGLPKGV---FNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 298 DADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFESriGCPLDSNTIIGPLHNQQAVGKYKASV 377
Cdd:cd07150  240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKV--GDPRDPDTVIGPLISPRQVERIKRQV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 378 AEAVASGGKIEYGGKvleRDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQ 457
Cdd:cd07150  318 EDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 115534176 458 NVFKWMgpKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDS 504
Cdd:cd07150  395 RAFKLA--ERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWS 439
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
47-518 1.05e-98

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 310.31  E-value: 1.05e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKWAASGQVVQSFAPANNSPI-ANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLE 125
Cdd:cd07124   39 GKEVRTEEKIESRNPADPSEVlGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 126 MGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLeQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSV 205
Cdd:cd07124  119 VGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRY-VYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 206 VWKPAPSTPLTAIAVTKLVEEV-LVANNVNpalcsLVCGEGD-VGQALVKDKRVNLVSFTGSSEIG------KIVGQQVQ 277
Cdd:cd07124  198 VLKPAEDTPVIAAKLVEILEEAgLPPGVVN-----FLPGPGEeVGDYLVEHPDVRFIAFTGSREVGlriyerAAKVQPGQ 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 278 ARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAqfESRIGCPLDS 357
Cdd:cd07124  273 KWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTK--ALKVGDPEDP 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 358 NTIIGPLHNQQAVGKYKASVAEAVaSGGKIEYGGKVLERD--GNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEE 435
Cdd:cd07124  351 EVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 436 AIAINNEVDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKETG-GGRESGSDSWRQYMRRST 513
Cdd:cd07124  430 ALEIANDTEYGLTGGVFSRSPEHLERAR--REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507

                 ....*
gi 115534176 514 CTINY 518
Cdd:cd07124  508 VTENF 512
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
61-501 7.04e-98

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424  Cd Length: 446  Bit Score: 305.99  E-value: 7.04e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:cd07106    4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 141 VDICDYATGLSrsLEGKIFPSERPGHALLeQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAV 220
Cdd:cd07106   84 VAWLRYTASLD--LPDEVIEDDDTRRVEL-RRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 221 TKLVEEVLVANNVNpalcsLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDAD 300
Cdd:cd07106  161 GELAQEVLPPGVLN-----VVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 301 LNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAEA 380
Cdd:cd07106  236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAA--VVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 381 VASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVF 460
Cdd:cd07106  314 KAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAE 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 115534176 461 KwMGPKgSDCGIVNVNiptSGAEIGGA--FGGEKETGGGRESG 501
Cdd:cd07106  394 A-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFG 431
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
58-510 9.93e-97

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432  Cd Length: 457  Bit Score: 303.70  E-value: 9.93e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  58 SFAPANNSPIANVQNGNVQDYEIAISEAKKAYND--WCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVG 135
Cdd:cd07114    1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 136 EVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPL 215
Cdd:cd07114   81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 216 TAIAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAII 294
Cdd:cd07114  161 STLELAKLAEEA----GFPPGVVNVVTGFGpETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 295 VNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYK 374
Cdd:cd07114  237 VFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAI--RVGDPLDPETQMGPLATERQLEKVE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 375 ASVAEAVASGGKIEYGGKVLE----RDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSS 450
Cdd:cd07114  315 RYVARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115534176 451 LFTTNIQNVFKWMgpKGSDCGIVNVNI-----PTSgaeiggAFGGEKETGGGRESGSDSWRQYMR 510
Cdd:cd07114  395 IWTRDLARAHRVA--RAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
59-499 1.49e-96

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467  Cd Length: 453  Bit Score: 302.98  E-value: 1.49e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  59 FAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQ 138
Cdd:cd07149    4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 139 EYVDICDYATGLSRSLEGKIFPSE-------RPGHALLEqwnPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAP 211
Cdd:cd07149   84 RAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 212 STPLTAIAVTKLVEEVlvanNVNPALCSLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARfgKLLLELGGN 290
Cdd:cd07149  161 QTPLSALKLAELLLEA----GLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLELGSN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 291 NAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAV 370
Cdd:cd07149  235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKL--VVGDPLDEDTDVGPMISEAEA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 371 GKYKASVAEAVASGGKIEYGGKvleRDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSS 450
Cdd:cd07149  313 ERIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 115534176 451 LFTTNIQNVFKWMgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKETGGGRE 499
Cdd:cd07149  390 VFTNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
58-509 2.12e-94

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412  Cd Length: 455  Bit Score: 297.55  E-value: 2.12e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  58 SFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGK-ISAEGVGE 136
Cdd:cd07093    1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKpITLARTRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 137 V----QEYVDICDYATGLsrslEGKIFPSErPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPS 212
Cdd:cd07093   81 IpraaANFRFFADYILQL----DGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 213 TPLTAIAVTKLVEEV-LVANNVNpalcsLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGN 290
Cdd:cd07093  156 TPLTAWLLAELANEAgLPPGVVN-----VVHGFGpEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGK 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 291 NAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAV 370
Cdd:cd07093  231 NPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKAL--KVGDPLDPDTEVGPLISKEHL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 371 GKYKASVAEAVASGGKIEYGGKVLE----RDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQG 446
Cdd:cd07093  309 EKVLGYVELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYG 388
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115534176 447 LSSSLFTTNIQNVFKwMGpKGSDCGIVNVN------IPTsgaeiggAFGGEKETGGGRESGSDSWRQYM 509
Cdd:cd07093  389 LAAYVWTRDLGRAHR-VA-RRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYSLEFYT 448
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
61-500 1.67e-92

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463  Cd Length: 456  Bit Score: 292.33  E-value: 1.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:cd07145    6 PANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 141 VDICDYATGLSRSLEGKIFPSE----RPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLT 216
Cdd:cd07145   86 IRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 217 AIAVTKLVEEVlvanNVNPALCSLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIV 295
Cdd:cd07145  166 AIELAKILEEA----GLPPGVINVVTGYGSeVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 296 NEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKA 375
Cdd:cd07145  242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKL--KVGDPLDESTDLGPLISPEAVERMEN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 376 SVAEAVASGGKIEYGGKVLErdGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTN 455
Cdd:cd07145  320 LVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 115534176 456 IQNVFKWmgPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRES 500
Cdd:cd07145  398 INRALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
81-499 4.53e-89

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418  Cd Length: 429  Bit Score: 282.81  E-value: 4.53e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  81 AISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICD-YATGLSRSLEGKIF 159
Cdd:cd07100    4 ALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAFLADEPI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 160 PSErPGHALLeQWNPLGVVGVISAFNFP---CAVYGwnnALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVLVANNVnpa 236
Cdd:cd07100   84 ETD-AGKAYV-RYEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGV--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 237 LCSLVCGEGDVGQaLVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTA 316
Cdd:cd07100  156 FQNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 317 GQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLER 396
Cdd:cd07100  235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAAL--KVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 397 DGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQnvfkwmgpKGS------DC 470
Cdd:cd07100  313 PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLE--------RAErvarrlEA 384
                        410       420       430
                 ....*....|....*....|....*....|
gi 115534176 471 GIVNVNIPT-SGAEIggAFGGEKETGGGRE 499
Cdd:cd07100  385 GMVFINGMVkSDPRL--PFGGVKRSGYGRE 412
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
11-509 1.94e-88

succinic semialdehyde dehydrogenase


Pssm-ID: 215157  Cd Length: 498  Bit Score: 283.12  E-value: 1.94e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  11 AATLQTRMASQLLINDskygfLKELGLTENnAGVFHGKWAAS--GQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKA 88
Cdd:PLN02278   1 PSTRASSMDAQSALVK-----LRNAGLLRT-QGLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  89 YNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHAL 168
Cdd:PLN02278  75 FPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 169 LEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEG-DV 247
Cdd:PLN02278 155 LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQA----GIPPGVLNVVMGDApEI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 248 GQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLI 327
Cdd:PLN02278 231 GDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRIL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 328 VHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVT 407
Cdd:PLN02278 311 VQEGIYDKFAEAFSKAVQKL--VVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLG 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 408 GLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVfkWMGPKGSDCGIVNVN---IPTSGAei 484
Cdd:PLN02278 389 DVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRA--WRVSEALEYGIVGVNeglISTEVA-- 464
                        490       500
                 ....*....|....*....|....*
gi 115534176 485 ggAFGGEKETGGGRESGSDSWRQYM 509
Cdd:PLN02278 465 --PFGGVKQSGLGREGSKYGIDEYL 487
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
61-508 2.67e-87

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433  Cd Length: 453  Bit Score: 278.94  E-value: 2.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGK-ISAEGVGEVQE 139
Cdd:cd07115    4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKpIRAARRLDVPR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 140 YVDICDYATGLSRSLEGKIFPSeRPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIA 219
Cdd:cd07115   84 AADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 220 VTKLVEEVlvanNVNPALCSLVCGEGDV-GQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNED 298
Cdd:cd07115  163 IAELMAEA----GFPAGVLNVVTGFGEVaGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 299 ADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVA 378
Cdd:cd07115  239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSL--RPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 379 EAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQN 458
Cdd:cd07115  317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 115534176 459 VFKWmgPKGSDCGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDSWRQY 508
Cdd:cd07115  397 AHRV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
61-499 7.20e-87

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 277.70  E-value: 7.20e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGK-ISAEGVGEVQE 139
Cdd:cd07108    4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNaLRTQARPEAAV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 140 YVDICDYATGLSRSLEGKIFPSeRPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIA 219
Cdd:cd07108   84 LADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 220 VTKLVEEVLVANNVNpalcsLVCGEGDV-GQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNED 298
Cdd:cd07108  163 LAEILAQVLPAGVLN-----VITGYGEEcGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 299 ADLNMVVPATVFAAVGT-AGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASV 377
Cdd:cd07108  238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKL--KIGDPLDEATDIGAIISEKQFAKVCGYI 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 378 AEAVA-SGGKIEYGGK----VLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLF 452
Cdd:cd07108  316 DLGLStSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 115534176 453 TTNIQNVFKwmGPKGSDCGIVNVNiPTSGAEIGGAFGGEKETGGGRE 499
Cdd:cd07108  396 TRDLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGRE 439
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
47-509 1.29e-84

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 272.65  E-value: 1.29e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKW--AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYN--DWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLV 122
Cdd:cd07119    4 GEWveAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARLE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 123 SLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQwNPLGVVGVISAFNFPCAVYGWNNALALVTG 202
Cdd:cd07119   84 TLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVR-EPVGVCGLITPWNYPLLQAAWKLAPALAAG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 203 NSVVWKPAPSTPLTAIAVTKLVEEV-LVANNVNpalcsLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARF 280
Cdd:cd07119  163 NTVVIKPSEVTPLTTIALFELIEEAgLPAGVVN-----LVTGSGAtVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 281 GKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTI 360
Cdd:cd07119  238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKI--KLGNGLDADTE 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 361 IGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERD----GNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEA 436
Cdd:cd07119  316 MGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEA 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115534176 437 IAINNEVDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVN---IPTSGAEiggaFGGEKETGGGRESGSDSWRQYM 509
Cdd:cd07119  396 IRLANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
61-516 7.98e-84

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464  Cd Length: 451  Bit Score: 269.61  E-value: 7.98e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISeakKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:cd07146    6 PYTGEVVGTVPAGTEEALREALA---LAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 141 VDICDYATGLSRSLEGKIFPSERPGHA----LLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLT 216
Cdd:cd07146   83 ADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 217 AIAVTklveEVLVANNVNPALCSLVCGE-GDVGQALVKDKRVNLVSFTGSSEIGKIVGQQvqARFGKLLLELGGNNAIIV 295
Cdd:cd07146  163 AIYLA----DLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAAT--AGYKRQLLELGGNDPLIV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 296 NEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKA 375
Cdd:cd07146  237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAAL--VVGDPMDPATDMGTVIDEEAAIQIEN 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 376 SVAEAVASGGKIEYGGkvlERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTN 455
Cdd:cd07146  315 RVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115534176 456 IQNVFKWMgpKGSDCGIVNVN------IPTSgaeiggAFGGEKETG-GGRESGSDSWRQYMRRSTCTI 516
Cdd:cd07146  392 LDTIKRLV--ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
61-510 3.82e-83

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417  Cd Length: 453  Bit Score: 267.94  E-value: 3.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:cd07099    3 PATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 141 VDICDYATGLSrsleGKIFPSER-------PGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPST 213
Cdd:cd07099   83 LEAIDWAARNA----PRVLAPRKvptgllmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 214 PLTAIAVTKLVEEVlvanNVNPALCSLVCGEGDVGQALVkDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAI 293
Cdd:cd07099  159 PLVGELLAEAWAAA----GPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPM 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 294 IVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKY 373
Cdd:cd07099  234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARAL--RPGADDIGDADIGPMTTARQLDIV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 374 KASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFT 453
Cdd:cd07099  312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115534176 454 TNIQnvfkwmgpKGS------DCGIVNVNIPTSGAEIGGA-FGGEKETGGGRESGSDSWRQYMR 510
Cdd:cd07099  392 RDLA--------RAEaiarrlEAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
47-501 5.58e-83

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469  Cd Length: 465  Bit Score: 268.02  E-value: 5.58e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKW--AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSL 124
Cdd:cd07151    1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 125 EMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNS 204
Cdd:cd07151   81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 205 VVWKPAPSTPLTA-IAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGK 282
Cdd:cd07151  161 VVLKPASDTPITGgLLLAKIFEEA----GLPKGVLNVVVGAGsEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 283 LLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIG 362
Cdd:cd07151  237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKAL--PYGDPSDPDTVVG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 363 PLHNQQAVGKYKASVAEAVASGGKIEYGGKVlerDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNE 442
Cdd:cd07151  315 PLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 115534176 443 VDQGLSSSLFTTNIQNVFKWmgPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESG 501
Cdd:cd07151  392 TEYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
39-516 8.66e-83

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 267.54  E-value: 8.66e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  39 ENNAGVF-HGKW--AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYND--WCEVPAPRRGEIVRQIGDKLRT 113
Cdd:cd07091    1 EQPTGLFiNNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 114 QLQNLGKLVSLEMGK-ISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQwNPLGVVGVISAFNFPCAVYG 192
Cdd:cd07091   81 DRDELAALESLDNGKpLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 193 WNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVLVAnnvnPALCSLVCGEGDV-GQALVKDKRVNLVSFTGSSEIGKI 271
Cdd:cd07091  160 WKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFP----PGVVNIVPGFGPTaGAAISSHMDVDKIAFTGSTAVGRT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 272 VGQQV-QARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKkayAQFESR 350
Cdd:cd07091  236 IMEAAaKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFK---ARAEKR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 351 -IGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLK 429
Cdd:cd07091  313 vVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILK 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 430 FSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVN--------IPtsgaeiggaFGGEKETGGGRESG 501
Cdd:cd07091  393 FKTEDEVIERANDTEYGLAAGVFTKDINKALRVS--RALKAGTVWVNtynvfdaaVP---------FGGFKQSGFGRELG 461
                        490
                 ....*....|....*
gi 115534176 502 SDSWRQYMRRSTCTI 516
Cdd:cd07091  462 EEGLEEYTQVKAVTI 476
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
61-516 1.04e-82

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436  Cd Length: 454  Bit Score: 266.90  E-value: 1.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYND--WCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQ 138
Cdd:cd07118    4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 139 EYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAI 218
Cdd:cd07118   84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 219 AVTKLVEEVLVANNVnpalCSLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNE 297
Cdd:cd07118  164 MLAELLIEAGLPAGV----VNIVTGYGAtVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 298 DADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASV 377
Cdd:cd07118  240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKV--RVGDPLDPETKVGAIINEAQLAKITDYV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 378 AEAVASGGKIEYGGKVLE-RDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNI 456
Cdd:cd07118  318 DAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115534176 457 QNVFKwmGPKGSDCGIVNVN-IPTSGAEIggAFGGEKETGGGRESGSDSWRQYMRRSTCTI 516
Cdd:cd07118  398 DTALT--VARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
60-518 2.21e-82

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425  Cd Length: 456  Bit Score: 266.16  E-value: 2.21e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  60 APANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQE 139
Cdd:cd07107    3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 140 YVDICDYATGLSRSLEGKIFPSErPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIA 219
Cdd:cd07107   83 AAALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 220 VTKLVEEVLVANNVNpalcsLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNED 298
Cdd:cd07107  162 LAELAREVLPPGVFN-----ILPGDGAtAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 299 ADLNMVVPATVFAA-VGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASV 377
Cdd:cd07107  237 ADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAI--KVGDPTDPATTMGPLVSRQQYDRVMHYI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 378 AEAVASGGKIEYGGKVLE----RDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFT 453
Cdd:cd07107  315 DSAKREGARLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115534176 454 TNIQNVFKWMgpKGSDCGIVNVNiPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRSTCTINY 518
Cdd:cd07107  395 NDISQAHRTA--RRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
67-509 8.58e-82

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470  Cd Length: 443  Bit Score: 264.16  E-value: 8.58e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  67 IANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICDY 146
Cdd:cd07152    4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 147 ATGLSRSLEGKIFPSErPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAVtklVEE 226
Cdd:cd07152   84 AAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV---IAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 227 VLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDADLNMVVP 306
Cdd:cd07152  160 LFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAAS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 307 ATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGK 386
Cdd:cd07152  240 NGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHL--PVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 387 IEYGGkvlERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKwMGPK 466
Cdd:cd07152  318 LEAGG---TYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA-LADR 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 115534176 467 gSDCGIVNVNIPTSGAEIGGAFGGEKETG-GGRESGSDSWRQYM 509
Cdd:cd07152  394 -LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
SSADH TIGR01780
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ...
61-509 3.34e-81

succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 & G-242, C-293 & G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]


Pssm-ID: 188167  Cd Length: 448  Bit Score: 262.75  E-value: 3.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176   61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:TIGR01780   4 PATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEILYA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  141 VDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAV 220
Cdd:TIGR01780  84 ASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSALAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  221 TKLVEEVLVANNV-NPALCSLVcgeGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNEDA 299
Cdd:TIGR01780 164 ARLAEQAGIPKGVlNVITGSRA---KEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  300 DLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVAE 379
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKL--KVGNGLDEGVTQGPLINEKAVEKVEKHIAD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  380 AVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNV 459
Cdd:TIGR01780 319 AVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRI 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 115534176  460 fkWMGPKGSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRESGSDSWRQYM 509
Cdd:TIGR01780 399 --WRVAEALEYGMVGINTGLISNVV-APFGGVKQSGLGREGSKYGIEEYL 445
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
61-509 6.22e-81

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408  Cd Length: 459  Bit Score: 262.18  E-value: 6.22e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDW-CEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGK-ISAEGVGEVQ 138
Cdd:cd07089    4 PATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAMQVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 139 EYVDICDYATGLSRSLEGKI---FPSER--PGHALLEQwNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPST 213
Cdd:cd07089   84 GPIGHLRYFADLADSFPWEFdlpVPALRggPGRRVVRR-EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 214 PLTAIAVTKLVEEVlvanNVNPALCSLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNA 292
Cdd:cd07089  163 PLSALLLGEIIAET----DLPAGVVNVVTGSDNaVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 293 IIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGK 372
Cdd:cd07089  239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEAL--PVGDPADPGTVMGPLISAAQRDR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 373 YKASVAEAVASGGKIEYGGKVLER--DGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSS 450
Cdd:cd07089  317 VEGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 115534176 451 LFTTNIQNVFKwMGPKgSDCGIVNVNiPTSGAEIGGAFGGEKETGGGRESGSDSWRQYM 509
Cdd:cd07089  397 VWSADVDRAYR-VARR-IRTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
59-510 2.32e-80

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409  Cd Length: 457  Bit Score: 260.70  E-value: 2.32e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  59 FAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQ 138
Cdd:cd07090    2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 139 EYVDICDYATGLSRSLEGKIFPSERPGHALLEQwNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAI 218
Cdd:cd07090   82 SSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRR-EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 219 avtkLVEEVLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNED 298
Cdd:cd07090  161 ----LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 299 ADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVA 378
Cdd:cd07090  237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKI--RIGDPLDEDTQMGALISEEHLEKVLGYIE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 379 EAVASGGKIEYGGKVLE-----RDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFT 453
Cdd:cd07090  315 SAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 115534176 454 TNIQNVFKWMGP-KGSDCGIVNVNIptSGAEIggAFGGEKETGGGRESGSDSWRQYMR 510
Cdd:cd07090  395 RDLQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
61-456 2.45e-80

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411  Cd Length: 450  Bit Score: 260.34  E-value: 2.45e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGV-GEVQE 139
Cdd:cd07092    4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 140 YVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIA 219
Cdd:cd07092   84 AVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 220 VTKLVEEVLVANNVNpalcsLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIVNED 298
Cdd:cd07092  164 LAELAAEVLPPGVVN-----VVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 299 ADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKASVA 378
Cdd:cd07092  239 ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAI--RVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115534176 379 EAvASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNI 456
Cdd:cd07092  317 RA-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
46-508 2.74e-80

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131  Cd Length: 467  Bit Score: 260.90  E-value: 2.74e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176   46 HGKW--AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVS 123
Cdd:TIGR01804   3 DGEYveDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  124 LEMGK-ISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQwNPLGVVGVISAFNFPCAVYGWNNALALVTG 202
Cdd:TIGR01804  83 LDTGKtLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIR-EPLGVCVGIGAWNYPLQIASWKIAPALAAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  203 NSVVWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFG 281
Cdd:TIGR01804 162 NAMVFKPSENTPLTALKVAEIMEEA----GLPKGVFNVVQGDGaEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  282 KLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTII 361
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERI--KLGDPFDEATEM 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  362 GPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLER----DGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAI 437
Cdd:TIGR01804 316 GPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVI 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115534176  438 AINNEVDQGLSSSLFTTNIQNVFKWMGpkGSDCGIVNVN-IPTSGAEIggAFGGEKETGGGRESGSDSWRQY 508
Cdd:TIGR01804 396 ARANDTEYGLAGGVFTADLGRAHRVAD--QLEAGTVWINtYNLYPAEA--PFGGYKQSGIGRENGKAALAHY 463
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
58-516 1.97e-79

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427  Cd Length: 454  Bit Score: 258.32  E-value: 1.97e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  58 SFAPANNSPIANVQNGNVQDYEIAISEAKKAYN-DWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGE 136
Cdd:cd07109    1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 137 VQEYVDICDYATGLSRSLEGKIFPSErPGHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLT 216
Cdd:cd07109   81 VEAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 217 AIAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARFGKLLLELGGNNAIIV 295
Cdd:cd07109  160 ALRLAELAEEA----GLPAGALNVVTGLGaEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 296 NEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDsNTIIGPLHNQQAVGKYKA 375
Cdd:cd07109  236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRAL--RVGPGLE-DPDLGPLISAKQLDRVEG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 376 SVAEAVASGGKIEYGGKVLE---RDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLF 452
Cdd:cd07109  313 FVARARARGARIVAGGRIAEgapAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVW 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115534176 453 TTNIqNVFKWMGpKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDSWRQYMRRSTCTI 516
Cdd:cd07109  393 TRDG-DRALRVA-RRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
47-501 2.56e-79

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457  Cd Length: 471  Bit Score: 258.27  E-value: 2.56e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKWAA--SGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYND--WCEVPAPRRGEIVRQIGDKLRTQLQNLGKLV 122
Cdd:cd07139    5 GRWVApsGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 123 SLEMGK-ISAEGVGEVQEYVDICDYATGLSRSLEgkiFPSERP----GHALLEQwNPLGVVGVISAFNFPCAVYGWNNAL 197
Cdd:cd07139   85 TAENGMpISWSRRAQGPGPAALLRYYAALARDFP---FEERRPgsggGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 198 ALVTGNSVVWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQ 277
Cdd:cd07139  161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEA----GLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 278 ARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDS 357
Cdd:cd07139  237 ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAAL--KVGDPLDP 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 358 NTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKV---LERdGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLE 434
Cdd:cd07139  315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpagLDR-GWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115534176 435 EAIAINNEVDQGLSSSLFTTNIQnvfkwmgpKGSD------CGIVNVNIPTSgaEIGGAFGGEKETGGGRESG 501
Cdd:cd07139  394 DAVRIANDSDYGLSGSVWTADVE--------RGLAvarrirTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
61-499 7.70e-79

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413  Cd Length: 453  Bit Score: 256.59  E-value: 7.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:cd07094    6 PYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 141 VDICDYATGLSRSLEGKIFPSERPGHALLEQ-W---NPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPLT 216
Cdd:cd07094   86 IDTLRLAAEEAERIRGEEIPLDATQGSDNRLaWtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 217 AIAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKIVgqQVQARFGKLLLELGGNNAIIV 295
Cdd:cd07094  166 ALELAKILVEA----GVPEGVLQVVTGEReVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVIV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 296 NEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKYKA 375
Cdd:cd07094  240 DRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKL--KVGDPLDEDTDVGPLISEEAAERVER 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 376 SVAEAVASGGKIEYGGkvlERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTN 455
Cdd:cd07094  318 WVEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 115534176 456 IqNVFkWMGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRE 499
Cdd:cd07094  395 L-NVA-FKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
HpaE TIGR02299
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ...
47-509 1.64e-78

5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.


Pssm-ID: 131352  Cd Length: 488  Bit Score: 256.66  E-value: 1.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176   47 GKW--AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSL 124
Cdd:TIGR02299   7 GEFvpSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEIAVLECL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  125 E-------MGKISAEGVGEVQEYVDICDYAtglsrsLEGKIFPSErpghallEQWN-----PLGVVGVISAFNFPCAVYG 192
Cdd:TIGR02299  87 DcgqplrqTRQQVIRAAENFRFFADKCEEA------MDGRTYPVD-------THLNytvrvPVGPVGLITPWNAPFMLST 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  193 WNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEG-DVGQALVKDKRVNLVSFTGSSEIGKI 271
Cdd:TIGR02299 154 WKIAPALAFGNTVVLKPAEWSPLTAARLAEIAKEA----GLPDGVFNLVHGFGeEAGKALVAHPDVKAVSFTGETATGSI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  272 VGQQVQARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRI 351
Cdd:TIGR02299 230 IMRNGADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAI--RV 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  352 GCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLE-------RDGNFVLPTIVTGLKHDSPVVLRETFAPI 424
Cdd:TIGR02299 308 GHPLDPETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  425 LYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKwMGPKgSDCGIVNVN------IPTsgaeiggAFGGEKETGGGR 498
Cdd:TIGR02299 388 LTVIPFKDEEEAIEKANDTRYGLAGYVWTNDVGRAHR-VALA-LEAGMIWVNsqnvrhLPT-------PFGGVKASGIGR 458
                         490
                  ....*....|.
gi 115534176  499 ESGSDSWRQYM 509
Cdd:TIGR02299 459 EGGTYSFDFYT 469
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
50-518 3.61e-78

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 255.44  E-value: 3.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  50 AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAY-NDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGK 128
Cdd:cd07113   11 GQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 129 -ISAEGVGEVQEYVDICDYATGLSRSLEGKI----FPS---ERpgHALLEQWNPLGVVGVISAFNFPCAVYGWNNALALV 200
Cdd:cd07113   91 sIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPSmqgER--YTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 201 TGNSVVWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEIGKIVGQQVQARF 280
Cdd:cd07113  169 TGCTIVIKPSEFTPLTLLRVAELAKEA----GIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 281 GKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTI 360
Cdd:cd07113  245 TRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSF--QVGSPMDESVM 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 361 IGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAIN 440
Cdd:cd07113  323 FGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLI 402
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115534176 441 NEVDQGLSSSLFTTNIQNVFKwMGPKgSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDSWRQYMRRSTCTINY 518
Cdd:cd07113  403 NDTPFGLTASVWTNNLSKALR-YIPR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
61-499 6.11e-78

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465  Cd Length: 452  Bit Score: 254.09  E-value: 6.11e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  61 PANNSPIANVQNGNVQDYEIAISEAKKAYNDWCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEY 140
Cdd:cd07147    6 PYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 141 VDICDYATGLSRSLEGKIFP---SER-PGH-ALLEQWnPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKPAPSTPL 215
Cdd:cd07147   86 IDTFRIAAEEATRIYGEVLPldiSARgEGRqGLVRRF-PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 216 TAIavtkLVEEVLVANNVNPALCSLVCGEGDVGQALVKDKRVNLVSFTGSSEigkiVGQQVQARFGK--LLLELGGNNAI 293
Cdd:cd07147  165 SAL----ILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPA----VGWDLKARAGKkkVVLELGGNAAV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 294 IVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHNQQAVGKY 373
Cdd:cd07147  237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKAL--KTGDPKDDATDVGPMISESEAERV 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 374 KASVAEAVASGGKIEYGGKvleRDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVDQGLSSSLFT 453
Cdd:cd07147  315 EGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFT 391
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 115534176 454 TNIQNVFK-WmgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKETGGGRE 499
Cdd:cd07147  392 RDLEKALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
53-509 3.37e-77

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430  Cd Length: 462  Bit Score: 252.52  E-value: 3.37e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  53 GQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYND--WCEVPAPRRGEIVRQIGDKLRTQLQNLGKLVSLEMGK-I 129
Cdd:cd07112    1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKpI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 130 SAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQwNPLGVVGVISAFNFPCAVYGWNNALALVTGNSVVWKP 209
Cdd:cd07112   81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 210 APSTPLTAIAVTKLVEEVLVANNVnpalCSLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGK-IVGQQVQARFGKLLLEL 287
Cdd:cd07112  160 AEQSPLTALRLAELALEAGLPAGV----LNVVPGFGHtAGEALGLHMDVDALAFTGSTEVGRrFLEYSGQSNLKRVWLEC 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 288 GGNNAIIVNEDA-DLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKKAYAQFesRIGCPLDSNTIIGPLHN 366
Cdd:cd07112  236 GGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREW--KPGDPLDPATRMGALVS 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 367 QQAVGKYKASVAEAVASGGKIEYGGKVLERD--GNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEAIAINNEVD 444
Cdd:cd07112  314 EAHFDKVLGYIESGKAEGARLVAGGKRVLTEtgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115534176 445 QGLSSSLFTTNIQNVFKwmGPKGSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDSWRQYM 509
Cdd:cd07112  394 YGLAASVWTSDLSRAHR--VARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
31-502 3.52e-77

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 253.10  E-value: 3.52e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  31 FLKELGLTENNAgvFHGkwAASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYND-WCEVPAPRRGEIVRQIGD 109
Cdd:cd07144    4 YDQPTGLFINNE--FVK--SSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 110 KLRTQLQNLGKLVSLEMGK-ISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHA-LLEQwnPLGVVGVISAFNFP 187
Cdd:cd07144   80 LVEKNRDLLAAIEALDSGKpYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAyTLHE--PYGVCGQIIPWNYP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 188 CAVYGWNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEGDV-GQALVKDKRVNLVSFTGSS 266
Cdd:cd07144  158 LAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEA----GFPPGVVNIIPGYGAVaGSALAEHPDVDKIAFTGST 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 267 EIGKIVGQQVQARFGKLLLELGGNNAIIVNEDADLNMvvpATVFAAVG---TAGQRCTTTRRLIVHDKVYDQVLERLKKA 343
Cdd:cd07144  234 ATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQ---AVKWAAAGimyNSGQNCTATSRIYVQESIYDKFVEKFVEH 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 344 YAQfESRIGCPLDSNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERD---GNFVLPTIVTGLKHDSPVVLRET 420
Cdd:cd07144  311 VKQ-NYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEI 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 421 FAPILYVLKFSTLEEAIAINNEVDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVNiPTSGAEIGGAFGGEKETGGGRES 500
Cdd:cd07144  390 FGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA--RELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGREL 466

                 ..
gi 115534176 501 GS 502
Cdd:cd07144  467 GE 468
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
47-510 3.60e-77

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 252.80  E-value: 3.60e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176  47 GKW--AASGQVVQSFAPANNSPIANVQNGNVQDYEIAISEAKKAYND--WCEVPAPRRGEIVRQIGDKLRTQLQNLGKLV 122
Cdd:cd07142   10 GQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 123 SLEMGKISAEG-VGEVQEYVDICDYATGLSRSLEGKIFPSERPGHA--LLEqwnPLGVVGVISAFNFPCAVYGWNNALAL 199
Cdd:cd07142   90 TWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVytLHE---PIGVVGQIIPWNFPLLMFAWKVGPAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 200 VTGNSVVWKPAPSTPLTAIAVTKLVEEVlvanNVNPALCSLVCGEGD-VGQALVKDKRVNLVSFTGSSEIGKIVGQ-QVQ 277
Cdd:cd07142  167 ACGNTIVLKPAEQTPLSALLAAKLAAEA----GLPDGVLNIVTGFGPtAGAAIASHMDVDKVAFTGSTEVGKIIMQlAAK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 278 ARFGKLLLELGGNNAIIVNEDADLNMVVPATVFAAVGTAGQRCTTTRRLIVHDKVYDQVLERLKkayAQFESR-IGCPLD 356
Cdd:cd07142  243 SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAK---ARALKRvVGDPFR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 357 SNTIIGPLHNQQAVGKYKASVAEAVASGGKIEYGGKVLERDGNFVLPTIVTGLKHDSPVVLRETFAPILYVLKFSTLEEA 436
Cdd:cd07142  320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115534176 437 IAINNEVDQGLSSSLFTTNIQNVFKWMgpKGSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDSWRQYMR 510
Cdd:cd07142  400 IKRANNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
105-461 9.56e-77

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233  Cd Length: 409  Bit Score: 249.65  E-value: 9.56e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 105 RQIGDKLRTQLQNLGKLVSLEMGKISAEGVGEVQEYVDICDYATGLSRSLEGKIFPSERPGHALLEQWNPLGVVGVISAF 184
Cdd:PRK10090   2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534176 185 NFPCAVYGWNNALALVTGNSVVWKPAPSTPLTAIAVTKLVEEVLVANNVnpalCSLVCGEGD-VGQALVKDKRVNLVSFT 263
Cdd:PRK10090  82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGV----FN