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Conserved domains on  [gi|148223856|ref|NP_001087698.1|]
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alpha-aminoadipic semialdehyde dehydrogenase

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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; ...
25-499 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: 970.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  25 GVYSGTWGGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLE 104
Cdd:cd07130    1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 105 SLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICG 184
Cdd:cd07130   81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 185 NVCLWKGAPTTSLTSVAVTKIVAQVLEHNNLPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGR 264
Cdd:cd07130  161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 265 KLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPL 344
Cdd:cd07130  241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 345 HTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDsAIVHKETFAPILYVIKFKTEEEAFAWNNEVK 424
Cdd:cd07130  321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223856 425 QGLSSSIFTKDLGRIFRWLGPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRSTCTINYS 499
Cdd:cd07130  400 QGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
 
Name Accession Description Interval E-value
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
25-499 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: 970.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  25 GVYSGTWGGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLE 104
Cdd:cd07130    1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 105 SLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICG 184
Cdd:cd07130   81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 185 NVCLWKGAPTTSLTSVAVTKIVAQVLEHNNLPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGR 264
Cdd:cd07130  161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 265 KLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPL 344
Cdd:cd07130  241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 345 HTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDsAIVHKETFAPILYVIKFKTEEEAFAWNNEVK 424
Cdd:cd07130  321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223856 425 QGLSSSIFTKDLGRIFRWLGPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRSTCTINYS 499
Cdd:cd07130  400 QGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
8-510 0e+00

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 723.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   8 QPEYSWLKDLGLKEENEGVY-SGTWGGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIV 86
Cdd:PLN02315   5 RKEYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  87 RQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAF 166
Cdd:PLN02315  85 RQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 167 NFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVAVTKIVAQVLEHNNLPGAICSLTCGGADIGNAIAKDERVDLVSFTG 246
Cdd:PLN02315 165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 247 STNVGKQVALKVQERFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAY 326
Cdd:PLN02315 245 SSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVY 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 327 AQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTgLAHDSAIVHKETFAPILY 406
Cdd:PLN02315 325 KQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLY 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 407 VIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWK 486
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWK 483
                        490       500
                 ....*....|....*....|....
gi 148223856 487 HYMRRSTCTINYSKDLPLAQGIKF 510
Cdd:PLN02315 484 QYMRRSTCTINYGNELPLAQGINF 507
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
33-493 4.42e-163

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: 473.55  E-value: 4.42e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   33 GKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKIL 112
Cdd:pfam00171   4 SSSETIEVINPATGEVIATVPAATAEDVDAAVAAARAAFKAWAKTPPAERAAILRKAADLLEERRDELAELETLETGKPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  113 VEGVGEVQEYVDICDYAVGLSRIIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGA 192
Cdd:pfam00171  84 AEARGEVPRAIDTLRYYAGLARKLEGETLPS-DPGVLAYTRREPLGVVGAITPWNFPLLLAAWKIAPALAAGNTVVLKPS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  193 PTTSLTSVAVTKIVAQVlehnNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGG 271
Cdd:pfam00171 163 ELTPLTALLLAELFEEA----GLPaGVLNVVTGSGSEVGDALVEHPDVDKVSFTGSTEVGRRIAKAAAKNLKRVTLELGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  272 NNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVE 351
Cdd:pfam00171 239 KNPLIVFDDADLDAAVEAAVFGAFGNAGQVCTAGSRLLVHESIYDEFVERLVEAAKSLKVGDPLDPDTDIGPLISKAQRE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  352 MYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSI 431
Cdd:pfam00171 319 RVLSYIEDAKEEGAKLLCGGEAGLEKGYFVEPTVLADVTPDMRIAQEEIFGPVLSVIPFKDEEEAIELANDTEYGLAAGV 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223856  432 FTKDLGRIFRWLgpKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRST 493
Cdd:pfam00171 399 FTNDLERALRVA--RRLEAGMVWINDYTTGDPEALPFGGFKQSGFGREGGKEGLEEYTETKT 458
PutA COG1012
NAD-dependent aldehyde dehydrogenases [Energy production and conversion]
29-499 8.20e-144

NAD-dependent aldehyde dehydrogenases [Energy production and conversion]


Pssm-ID: 223944  Cd Length: 472  Bit Score: 424.79  E-value: 8.20e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  29 GTWGGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEM 108
Cdd:COG1012    7 GEWVDGASTIEVINPATGEVIATVPAATAEDVDAAVAAARAAFEAWSRLSAEERAAILRRIADLLEARAEELAALITLET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 109 GKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPsERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCL 188
Cdd:COG1012   87 GKPISEARGEIARAADFIRYYAEEARRLEGETIP-TDKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 189 WKGAPTTSLTSVAVTKIVAQVLehnnLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLL 267
Cdd:COG1012  166 LKPSEQTPLSALALAELAAEAG----LPaGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANLKPVTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 268 ELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTK 347
Cdd:COG1012  242 ELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPSTDLGPLISE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 348 QAVEMYLSAVEQAKCEGGTVVCGGKVIDrpGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGL 427
Cdd:COG1012  322 EQLDRVEGYIEDAVAEGARLLAGGKRPG--GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELANDTEYGL 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223856 428 SSSIFTKDLGRIFRWLgpKGSDCGLVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDSWKHYMRRSTCTINYS 499
Cdd:COG1012  400 AAAIFTRDLARAFRVA--RRLEAGMVGINDYTGGADIAYLpFGGVKQSGLGREGGKYGLEEFTEVKTVTIKLG 470
PRK13473 PRK13473
gamma-aminobutyraldehyde dehydrogenase; Provisional
33-441 2.01e-86

gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 237391  Cd Length: 475  Bit Score: 276.41  E-value: 2.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  33 GKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGK-I 111
Cdd:PRK13473  14 GEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKpL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 112 LVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKG 191
Cdd:PRK13473  94 HLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 192 APTTSLTSVAVTKIVAQVLEhnnlPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGG 271
Cdd:PRK13473 174 SEITPLTALKLAELAADILP----PGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 272 NNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVE 351
Cdd:PRK13473 250 KAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRD 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 352 MYLSAVEQAKCEG-GTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSS 430
Cdd:PRK13473 330 RVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASS 409
                        410
                 ....*....|.
gi 148223856 431 IFTKDLGRIFR 441
Cdd:PRK13473 410 VWTRDVGRAHR 420
Betaine_aldehyde_dehydrogenase TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
34-488 1.59e-83

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: 268.60  E-value: 1.59e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   34 KGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILV 113
Cdd:TIGR01804  11 AGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  114 E-GVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGA 192
Cdd:TIGR01804  91 EtIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIR-EPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  193 PTTSLTSVAVtkivAQVLEHNNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGG 271
Cdd:TIGR01804 170 ENTPLTALKV----AEIMEEAGLPKGVFNVVQGdGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  272 NNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVE 351
Cdd:TIGR01804 246 KSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLISAAHRD 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  352 MYLSAVEQAKCEGGTVVCGGKVIDRP----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGL 427
Cdd:TIGR01804 326 KVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGL 405
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223856  428 SSSIFTKDLGRIFR----------WLgpkgSDCGLVNVNIPtsgaeiggaFGGEKHTGGGRESGSDSWKHY 488
Cdd:TIGR01804 406 AGGVFTADLGRAHRvadqleagtvWI----NTYNLYPAEAP---------FGGYKQSGIGRENGKAALAHY 463
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
145-477 5.30e-31

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 123.99  E-value: 5.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 145 RPGHALIeQWNPVGLVGIITAFNFPVavygwNNAL-----ALICGNVCLWKgaptTSLTSVAVTKIVAQVLEhNNLPGAI 219
Cdd:PTZ00381  99 GPGKSYI-IPEPLGVVLVIGAWNYPL-----NLTLiplagAIAAGNTVVLK----PSELSPHTSKLMAKLLT-KYLDPSY 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 220 CSLTCGGADIGNAIAKdERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAG 299
Cdd:PTZ00381 168 VRVIEGGVEVTTELLK-EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 300 QRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPC-EPD--TLCGPLHTKQAVEMYlsaveqaKCEGGTVVCGGKViDR 376
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKkSEDysRIVNEFHTKRLAELI-------KDHGGKVVYGGEV-DI 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 377 PGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGS------DC 450
Cdd:PTZ00381 319 ENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSgavvinDC 398
                        330       340
                 ....*....|....*....|....*....
gi 148223856 451 --GLVNVNIPtsgaeiggaFGGEKHTGGG 477
Cdd:PTZ00381 399 vfHLLNPNLP---------FGGVGNSGMG 418
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
35-490 7.45e-61

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 210.43  E-value: 7.45e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  35 GEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQ--IWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKIL 112
Cdd:PLN02466  72 GKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 113 VEGVG-EVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKG 191
Cdd:PLN02466 152 EQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLH-EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 192 APTTSLTSVAVTKIvaqvLEHNNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQV-ALKVQERFGRKLLEL 269
Cdd:PLN02466 231 AEQTPLSALYAAKL----LHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAAKSNLKPVTLEL 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 270 GGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKlSKAYAQVR-IGDPCEPDTLCGPLHTKQ 348
Cdd:PLN02466 307 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK-AKARALKRvVGDPFKKGVEQGPQIDSE 385
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 349 AVEMYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLS 428
Cdd:PLN02466 386 QFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLA 465
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223856 429 SSIFTKDL---GRIFRWLgpkgsDCGLVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDSWKHYMR 490
Cdd:PLN02466 466 AGVFTQNLdtaNTLSRAL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
COG4230 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Energy production and conversion]
33-491 2.01e-53

Delta 1-pyrroline-5-carboxylate dehydrogenase [Energy production and conversion]


Pssm-ID: 226683 [Multi-domain]  Cd Length: 769  Bit Score: 192.61  E-value: 2.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  33 GKGEVVTSYCPATNAPI-ARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKI 111
Cdd:COG4230  124 AGGEPRPVINPADPDDIvGTVTEATEADVEQALEAAVAAAPIWSATPPAERAAILERAADLMEAQMPQLMGLLVREAGKT 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 112 LVEGVGEVQEYVDICDYAVGLSRiiggpiLPSERPGHAlieqwnPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKG 191
Cdd:COG4230  204 LSNAIAEVREAVDFLRYYAGQAR------DTFGNLTHR------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 192 APTTSLtsvavtkIVAQ---VLEHNNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRK-- 265
Cdd:COG4230  272 AEQTPL-------IAAQavrLLHEAGVPPGVLQLLPGrGETVGAALTADARVAGVMFTGSTEVARLIQRQLAKRQGRPip 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 266 -LLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPL 344
Cdd:COG4230  345 lIAETGGQNAMIVDSSALAEQVVADVLASAFDSAGQRCSALRVLCLQEDVADRILTMLKGAMAELRVGNPDRLTTDVGPV 424
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 345 HT---KQAVEMYLSA-------VEQAKCEGGTVVcggkvidrpGNFVEPTI--MTGLAHdsaiVHKETFAPILYVIKFKT 412
Cdd:COG4230  425 IDaeaKANIEKHIQTmrskgrlVHQAAAPNSLQK---------GTFVAPTLieLENLDE----LQREVFGPVLHVVRYKR 491
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 413 E--EEAFAWNNEVKQGLSSSIFTKDLGRIFRWLGpkGSDCGLVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdswKHYM 489
Cdd:COG4230  492 DelDEVIDQINATGYGLTLGVHTRIDETIAHVTE--RAHAGNLYVNRNIVGAVVGvQPFGGEGLSGTGPKAGG---PLYL 566

                 ..
gi 148223856 490 RR 491
Cdd:COG4230  567 LR 568
PRK11904 PRK11904
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
32-414 2.99e-45

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 170.38  E-value: 2.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   32 GGKGEVVTSYCPA-TNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGK 110
Cdd:PRK11904  558 NGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  111 ILVEGVGEVQEYVDICD-YAVGLSRIIGGPI-LPSerpghalieqwnPVG------LVG-----IITAFNFPVAVYGWNN 177
Cdd:PRK11904  638 TLQDAIAEVREAVDFCRyYAAQARRLFGAPEkLPG------------PTGesnelrLHGrgvfvCISPWNFPLAIFLGQV 705
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  178 ALALICGNVCLWKGAPTTSLTSVAVTK------IVAQVLEHnnLPGAicsltcgGADIGNAIAKDERVDLVSFTGSTNVG 251
Cdd:PRK11904  706 AAALAAGNTVIAKPAEQTPLIAAEAVKllheagIPKDVLQL--LPGD-------GATVGAALTADPRIAGVAFTGSTETA 776
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  252 KQVALKVQERFGRKL---LELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQ 328
Cdd:PRK11904  777 RIINRTLAARDGPIVpliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAE 856
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  329 VRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQAKCEgGTVVCGGKVID--RPGNFVEPTI--MTGLAHdsaiVHKETFAPI 404
Cdd:PRK11904  857 LKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAgtENGHFVAPTAfeIDSISQ----LEREVFGPI 931
                         410
                  ....*....|
gi 148223856  405 LYVIKFKTEE 414
Cdd:PRK11904  932 LHVIRYKASD 941
PaaN-DH TIGR02278
phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening ...
135-492 4.70e-25

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: 107.60  E-value: 4.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  135 IIGGPILP-SERPGHALIEQWNPVGLVGI-ITAFNFPVavygWNN----ALALICGNVCLWKGA-PTTSLTSVAVTKIVa 207
Cdd:TIGR02278 121 IPEDEFEPlSKDGSFQGRHILTPKGGVAVqINAFNFPV----WGLlekfAPAFLAGVPTLAKPAtPTAYVAEALVRTMV- 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  208 qvlEHNNLPGAICSLTCGGA-DIGNAIakDERvDLVSFTGSTNVGKQvaLKVQERFGRKLL----ELGGNNAIIVFEDA- 281
Cdd:TIGR02278 196 ---ESGLLPEGSLQLICGSAgDLLDHL--DHR-DVVAFTGSAATADR--LRAHPNVLERGIrfnaEADSLNAAILGEDAt 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  282 ----DLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAV 357
Cdd:TIGR02278 268 pdepEFDLFAQEIVRELTIKAGQKCTAIRRVIVPKALLEAVLKALQARLAKVVLGDPREEGVDMGPLVSLEQRADVEAAV 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  358 EQAKCEGGTVVCGGKViDRPGNFVEPTIMTGLAHDSAIVHK-ETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKD- 435
Cdd:TIGR02278 348 AALLAAGAEVRLGGPG-RLDGAFFPPTLLLAEDPWAGAVHAtEAFGPVATFFPYGDRAEAARLAARGGGSLVATLATSDp 426
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223856  436 -LGRIFRW-LGPKGSDCGLVNVNIPTSGAEIGGAF-----GGEKHTGGGRE-SGSDSWKHYMRRS 492
Cdd:TIGR02278 427 eEARQFILgLAPYHGRLHILNRDDAAESTGHGSPLprllhGGPGRAGGGEElGGLRSVKHYMQRT 491
 
Name Accession Description Interval E-value
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
25-499 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: 970.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  25 GVYSGTWGGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLE 104
Cdd:cd07130    1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 105 SLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICG 184
Cdd:cd07130   81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 185 NVCLWKGAPTTSLTSVAVTKIVAQVLEHNNLPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGR 264
Cdd:cd07130  161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 265 KLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPL 344
Cdd:cd07130  241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 345 HTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDsAIVHKETFAPILYVIKFKTEEEAFAWNNEVK 424
Cdd:cd07130  321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223856 425 QGLSSSIFTKDLGRIFRWLGPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRSTCTINYS 499
Cdd:cd07130  400 QGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
25-499 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: 904.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  25 GVYSGTW-GGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHL 103
Cdd:cd07086    1 GVIGGEWvGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 104 ESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALIC 183
Cdd:cd07086   81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 184 GNVCLWKGAPTTSLTSVAVTKIVAQVLEHNNLPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFG 263
Cdd:cd07086  161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 264 RKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGP 343
Cdd:cd07086  241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 344 LHTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDR--PGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNN 421
Cdd:cd07086  321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223856 422 EVKQGLSSSIFTKDLGRIFRWLGPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRSTCTINYS 499
Cdd:cd07086  401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
8-510 0e+00

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 723.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   8 QPEYSWLKDLGLKEENEGVY-SGTWGGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIV 86
Cdd:PLN02315   5 RKEYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  87 RQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAF 166
Cdd:PLN02315  85 RQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 167 NFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVAVTKIVAQVLEHNNLPGAICSLTCGGADIGNAIAKDERVDLVSFTG 246
Cdd:PLN02315 165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 247 STNVGKQVALKVQERFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAY 326
Cdd:PLN02315 245 SSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVY 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 327 AQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTgLAHDSAIVHKETFAPILY 406
Cdd:PLN02315 325 KQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLY 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 407 VIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWK 486
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWK 483
                        490       500
                 ....*....|....*....|....
gi 148223856 487 HYMRRSTCTINYSKDLPLAQGIKF 510
Cdd:PLN02315 484 QYMRRSTCTINYGNELPLAQGINF 507
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
61-496 3.38e-168

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: 485.56  E-value: 3.38e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  61 NETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPI 140
Cdd:cd07078    1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 141 LPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVAVTKIVAQVLehnnLPGAIC 220
Cdd:cd07078   81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 221 SLTCGGAD-IGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAG 299
Cdd:cd07078  157 NVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 300 QRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDR-PG 378
Cdd:cd07078  237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKG 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 379 NFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGLVNVNIP 458
Cdd:cd07078  317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDY 394
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 148223856 459 TSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRSTCTI 496
Cdd:cd07078  395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
33-493 4.42e-163

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: 473.55  E-value: 4.42e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   33 GKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKIL 112
Cdd:pfam00171   4 SSSETIEVINPATGEVIATVPAATAEDVDAAVAAARAAFKAWAKTPPAERAAILRKAADLLEERRDELAELETLETGKPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  113 VEGVGEVQEYVDICDYAVGLSRIIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGA 192
Cdd:pfam00171  84 AEARGEVPRAIDTLRYYAGLARKLEGETLPS-DPGVLAYTRREPLGVVGAITPWNFPLLLAAWKIAPALAAGNTVVLKPS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  193 PTTSLTSVAVTKIVAQVlehnNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGG 271
Cdd:pfam00171 163 ELTPLTALLLAELFEEA----GLPaGVLNVVTGSGSEVGDALVEHPDVDKVSFTGSTEVGRRIAKAAAKNLKRVTLELGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  272 NNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVE 351
Cdd:pfam00171 239 KNPLIVFDDADLDAAVEAAVFGAFGNAGQVCTAGSRLLVHESIYDEFVERLVEAAKSLKVGDPLDPDTDIGPLISKAQRE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  352 MYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSI 431
Cdd:pfam00171 319 RVLSYIEDAKEEGAKLLCGGEAGLEKGYFVEPTVLADVTPDMRIAQEEIFGPVLSVIPFKDEEEAIELANDTEYGLAAGV 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223856  432 FTKDLGRIFRWLgpKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRST 493
Cdd:pfam00171 399 FTNDLERALRVA--RRLEAGMVWINDYTTGDPEALPFGGFKQSGFGREGGKEGLEEYTETKT 458
PutA COG1012
NAD-dependent aldehyde dehydrogenases [Energy production and conversion]
29-499 8.20e-144

NAD-dependent aldehyde dehydrogenases [Energy production and conversion]


Pssm-ID: 223944  Cd Length: 472  Bit Score: 424.79  E-value: 8.20e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  29 GTWGGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEM 108
Cdd:COG1012    7 GEWVDGASTIEVINPATGEVIATVPAATAEDVDAAVAAARAAFEAWSRLSAEERAAILRRIADLLEARAEELAALITLET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 109 GKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPsERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCL 188
Cdd:COG1012   87 GKPISEARGEIARAADFIRYYAEEARRLEGETIP-TDKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 189 WKGAPTTSLTSVAVTKIVAQVLehnnLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLL 267
Cdd:COG1012  166 LKPSEQTPLSALALAELAAEAG----LPaGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANLKPVTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 268 ELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTK 347
Cdd:COG1012  242 ELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPSTDLGPLISE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 348 QAVEMYLSAVEQAKCEGGTVVCGGKVIDrpGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGL 427
Cdd:COG1012  322 EQLDRVEGYIEDAVAEGARLLAGGKRPG--GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELANDTEYGL 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223856 428 SSSIFTKDLGRIFRWLgpKGSDCGLVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDSWKHYMRRSTCTINYS 499
Cdd:COG1012  400 AAAIFTRDLARAFRVA--RRLEAGMVGINDYTGGADIAYLpFGGVKQSGLGREGGKYGLEEFTEVKTVTIKLG 470
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
29-499 1.30e-129

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: 388.63  E-value: 1.30e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  29 GTW--GGKGEVVTSYCPA-TNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLES 105
Cdd:cd07131    5 GEWvdSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 106 LEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGN 185
Cdd:cd07131   85 REMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 186 VCLWKGAPTTSltsvAVTKIVAQVLEHNNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGR 264
Cdd:cd07131  165 TVVFKPAEDTP----ACALKLVELFAEAGLPpGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 265 KLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPL 344
Cdd:cd07131  241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 345 HTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDR----PGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWN 420
Cdd:cd07131  321 INEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 421 NEVKQGLSSSIFTKDLGRIFRWLGpkgsDC--GLVNVNIPTSGAEIGGAFGGEKHTGGG-RESGSDSWKHYMRRSTCTIN 497
Cdd:cd07131  401 NDTEYGLSSAIYTEDVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYVD 476

                 ..
gi 148223856 498 YS 499
Cdd:cd07131  477 YS 478
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
65-496 3.88e-127

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: 378.11  E-value: 3.88e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  65 KKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSE 144
Cdd:cd06534    1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 145 RPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVAVTKIVAQVLehnnLPGAICSLTC 224
Cdd:cd06534   81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVVNVVP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 225 GGAD-IGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCT 303
Cdd:cd06534  157 GGGDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 304 TARRLFLHESIHDEIVEKLSkayaqvrigdpcepdtlcgplhtkqavemylsaveqakceggtvvcggkvidrpgnfvep 383
Cdd:cd06534  237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 384 TIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGLVNVNIPTSGAE 463
Cdd:cd06534  257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA--ERLRAGTVYINDSSIGVG 334
                        410       420       430
                 ....*....|....*....|....*....|...
gi 148223856 464 IGGAFGGEKHTGGGRESGSDSWKHYMRRSTCTI 496
Cdd:cd06534  335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
24-483 1.69e-117

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: 357.33  E-value: 1.69e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  24 EGVYSGTWGGKGEVVTSYCPA-TNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGH 102
Cdd:cd07097    2 RNYIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 103 LESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALI 182
Cdd:cd07097   82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 183 CGNVCLWKGAPTTSLTSVAVTKIVAQVlehnNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQER 261
Cdd:cd07097  162 YGNTVVFKPAELTPASAWALVEILEEA----GLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 262 FGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLC 341
Cdd:cd07097  238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 342 GPLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRP--GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAW 419
Cdd:cd07097  318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223856 420 NNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGLVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSD 483
Cdd:cd07097  398 ANDTEFGLSAGIVTTSLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEA 460
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
43-489 4.27e-109

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: 334.79  E-value: 4.27e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVqey 122
Cdd:cd07103    4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 123 vdicDYAVGL-------SRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTT 195
Cdd:cd07103   81 ----DYAASFlewfaeeARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 196 SLTSVAVtkivAQVLEHNNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNA 274
Cdd:cd07103  157 PLSALAL----AELAEEAGLPaGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 275 IIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYL 354
Cdd:cd07103  233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 355 SAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTK 434
Cdd:cd07103  313 ALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR 392
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148223856 435 DLGRIFRwLGpKGSDCGLVNVNIPT-SGAEIggAFGGEKHTGGGRESGSDSWKHYM 489
Cdd:cd07103  393 DLARAWR-VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
40-490 5.31e-108

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: 332.21  E-value: 5.31e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  40 SYCPATNAPIARVKQATLEEYNETVKKAKAAW--QIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVG 117
Cdd:cd07114    1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 118 EVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSL 197
Cdd:cd07114   81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 198 TSVAVTKIVAQVlehnNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAII 276
Cdd:cd07114  161 STLELAKLAEEA----GFPpGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 277 VFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSA 356
Cdd:cd07114  237 VFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 357 VEQAKCEGGTVVCGGKVIDRP----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIF 432
Cdd:cd07114  317 VARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223856 433 TKDLGRIFRWlgPKGSDCGLVNVNI-----PTSgaeiggAFGGEKHTGGGRESGSDSWKHYMR 490
Cdd:cd07114  397 TRDLARAHRV--ARAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
34-441 5.68e-107

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: 330.00  E-value: 5.68e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  34 KGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILV 113
Cdd:cd07088   11 SGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 114 EGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAP 193
Cdd:cd07088   91 LARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 194 TTSLTSVAVTKIVAQVlehnNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGN 272
Cdd:cd07088  171 ETPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGK 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 273 NAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEM 352
Cdd:cd07088  247 APAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDK 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 353 YLSAVEQAKCEGGTVVCGGKVID-RPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSI 431
Cdd:cd07088  327 VEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYI 406
                        410
                 ....*....|
gi 148223856 432 FTKDLGRIFR 441
Cdd:cd07088  407 YTENLNTAMR 416
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
61-485 4.21e-99

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: 308.31  E-value: 4.21e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  61 NETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPI 140
Cdd:cd07104    3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 141 LPSERPGhalieQWN-----PVGLVGIITAFNFPV-----AVygwnnALALICGNVCLWKGAPTTsltsvAVTK--IVAQ 208
Cdd:cd07104   83 LPSDVPG-----KESmvrrvPLGVVGVISPFNFPLilamrSV-----APALALGNAVVLKPDSRT-----PVTGglLIAE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 209 VLEHNNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFEDADLSLVT 287
Cdd:cd07104  148 IFEEAGLPkGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAV 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 288 PSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQAKCEGGTV 367
Cdd:cd07104  228 SAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 368 VCGGKvidRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFRwLGpKG 447
Cdd:cd07104  308 LTGGT---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA-ER 382
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 148223856 448 SDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSW 485
Cdd:cd07104  383 LETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASL 420
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
43-493 1.04e-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: 307.53  E-value: 1.04e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEY 122
Cdd:cd07106    4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 123 VDICDYAVGLSriiggpiLPSER----PGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLT 198
Cdd:cd07106   84 VAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 199 SVAVTKIVAQVLEhnnlPGAICSLTcGGADIGNAIAKDERVDLVSFTGSTNVGKQVA------LKvqerfgRKLLELGGN 272
Cdd:cd07106  157 TLKLGELAQEVLP----PGVLNVVS-GGDELGPALTSHPDIRKISFTGSTATGKKVMasaaktLK------RVTLELGGN 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 273 NAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEM 352
Cdd:cd07106  226 DAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDK 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 353 YLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIF 432
Cdd:cd07106  306 VKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVW 385
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223856 433 TKDLGRIFRwLGPKgSDCGLVNVNiptSGAEIGGA--FGGEKHTGGGRESGSDSWKHYMRRST 493
Cdd:cd07106  386 SSDLERAEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
43-488 1.75e-97

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: 304.75  E-value: 1.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVG-EVQE 121
Cdd:cd07115    4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 122 YVDICDYAVGLSRIIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVA 201
Cdd:cd07115   84 AADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 202 VTKIVAQVlehnNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFED 280
Cdd:cd07115  163 IAELMAEA----GFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 281 ADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQA 360
Cdd:cd07115  239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 361 KCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIF 440
Cdd:cd07115  319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 148223856 441 RWlgPKGSDCGLVNVNipTSGA-EIGGAFGGEKHTGGGRESGSDSWKHY 488
Cdd:cd07115  399 RV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
43-484 7.14e-97

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: 303.10  E-value: 7.14e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEY 122
Cdd:cd07150    6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 123 VDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVav 202
Cdd:cd07150   86 PELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL-- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 203 tkIVAQVLEHNNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFEDA 281
Cdd:cd07150  164 --KIAEIMEEAGLPkGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 282 DLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQAK 361
Cdd:cd07150  242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 362 CEGGTVVCGGKvidRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFR 441
Cdd:cd07150  322 AKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 148223856 442 WlgPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDS 484
Cdd:cd07150  399 L--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWS 439
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
40-489 1.78e-96

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: 302.18  E-value: 1.78e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  40 SYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGev 119
Cdd:cd07093    1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 120 qeyVDI----------CDYAVGLsriiGGPILPSErPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLW 189
Cdd:cd07093   79 ---RDIpraaanfrffADYILQL----DGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 190 KGAPTTSLTSVavtkIVAQVLEHNNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLE 268
Cdd:cd07093  151 KPSEWTPLTAW----LLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 269 LGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQ 348
Cdd:cd07093  227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 349 AVEMYLSAVEQAKCEGGTVVCGGKVIDRP----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVK 424
Cdd:cd07093  307 HLEKVLGYVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTP 386
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223856 425 QGLSSSIFTKDLGRIFRWlgPKGSDCGLVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDSWKHYM 489
Cdd:cd07093  387 YGLAAYVWTRDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYSLEFYT 448
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
43-479 1.52e-94

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: 296.93  E-value: 1.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGV-GEVQE 121
Cdd:cd07092    4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 122 YVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVA 201
Cdd:cd07092   84 AVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 202 VTKIVAQVLEhnnlPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFEDA 281
Cdd:cd07092  164 LAELAAEVLP----PGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 282 DLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQAK 361
Cdd:cd07092  240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 362 cEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFR 441
Cdd:cd07092  320 -AHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 148223856 442 WLGPKGSDCGLVNVNIPTSgAEIggAFGGEKHTGGGRE 479
Cdd:cd07092  399 LSARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKD 433
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
14-489 9.88e-90

succinic semialdehyde dehydrogenase


Pssm-ID: 215157  Cd Length: 498  Bit Score: 285.82  E-value: 9.88e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  14 LKDLGLkEENEGVYSGTW--GGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGD 91
Cdd:PLN02278  17 LRNAGL-LRTQGLIGGKWtdAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  92 ALRKKIKLLGHLESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVA 171
Cdd:PLN02278  96 LIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 172 VYGWNNALALICGNVCLWKGAPTTSLTSVAVTKIVAQVlehnNLPGAICSLTCGGA-DIGNAIAKDERVDLVSFTGSTNV 250
Cdd:PLN02278 176 MITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQA----GIPPGVLNVVMGDApEIGDALLASPKVRKITFTGSTAV 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 251 GKQVALKVQERFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVR 330
Cdd:PLN02278 252 GKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLV 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 331 IGDPCEPDTLCGPLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKF 410
Cdd:PLN02278 332 VGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRF 411
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 411 KTEEEAFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGLVNVN---IPTSGAeiggAFGGEKHTGGGRESGSDSWKH 487
Cdd:PLN02278 412 KTEEEAIAIANDTEAGLAAYIFTRDLQRAWRV--SEALEYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGIDE 485

                 ..
gi 148223856 488 YM 489
Cdd:PLN02278 486 YL 487
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
43-480 9.95e-90

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: 284.63  E-value: 9.95e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEY 122
Cdd:cd07145    6 PANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 123 VDICDYAVGLSRIIGGPILPSE----RPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLT 198
Cdd:cd07145   86 IRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 199 SVAVTKIvaqvLEHNNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIV 277
Cdd:cd07145  166 AIELAKI----LEEAGLPpGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 278 FEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAV 357
Cdd:cd07145  242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 358 EQAKCEGGTVVCGGKVIDrpGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLG 437
Cdd:cd07145  322 NDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDIN 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 148223856 438 RIFRWlgPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRES 480
Cdd:cd07145  400 RALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
29-481 1.11e-89

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: 284.97  E-value: 1.11e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  29 GTW--GGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVR---QIGDALRKKIkllGHL 103
Cdd:cd07151    1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEkaaQILEERRDEI---VEW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 104 ESLEMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALIC 183
Cdd:cd07151   78 LIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 184 GNVCLWKGAPTTSLTSvavTKIVAQVLEHNNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERF 262
Cdd:cd07151  158 GNAVVLKPASDTPITG---GLLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 263 GRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCG 342
Cdd:cd07151  235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 343 PLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVidrPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNE 422
Cdd:cd07151  315 PLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148223856 423 VKQGLSSSIFTKDLGRIFRWlgPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESG 481
Cdd:cd07151  392 TEYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
43-490 3.82e-88

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: 280.34  E-value: 3.82e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEY 122
Cdd:cd07090    4 PATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 123 VDICDYAVGL-SRIIGGPI-LPSERPGHALIEqwnPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSV 200
Cdd:cd07090   84 ADCLEYYAGLaPTLSGEHVpLPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 201 avtkIVAQVLEHNNLPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFED 280
Cdd:cd07090  161 ----LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 281 ADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQA 360
Cdd:cd07090  237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 361 KCEGGTVVCGGKVID-----RPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKD 435
Cdd:cd07090  317 KQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148223856 436 LGRIFRWLGP-KGSDCGLVNVNIptSGAEIggAFGGEKHTGGGRESGSDSWKHYMR 490
Cdd:cd07090  397 LQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
43-489 7.56e-88

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: 280.35  E-value: 7.56e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQ--IWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQ 120
Cdd:cd07119   20 PANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDID 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 121 EYVDICDYAVGLSRIIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSV 200
Cdd:cd07119  100 DVANCFRYYAGLATKETGEVYDVPPHVISRTVR-EPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 201 AVTKIVAQVlehnNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFE 279
Cdd:cd07119  179 ALFELIEEA----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFA 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 280 DADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQ 359
Cdd:cd07119  255 DADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQL 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 360 AKCEGGTVVCGGKVIDRP----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKD 435
Cdd:cd07119  335 GKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKD 414
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148223856 436 LGRIFRWLgpKGSDCGLVNVN---IPTSGAEiggaFGGEKHTGGGRESGSDSWKHYM 489
Cdd:cd07119  415 IARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
43-498 7.59e-88

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: 279.65  E-value: 7.59e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEY 122
Cdd:cd07107    4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 123 VDICDYAVGLSRIIGGPILPSErPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVAV 202
Cdd:cd07107   84 AALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 203 TKIVAQVLEhnnlPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFEDAD 282
Cdd:cd07107  163 AELAREVLP----PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 283 LSLVTPSvlfAAVG----TAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVE 358
Cdd:cd07107  239 PEAAADA---AVAGmnftWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 359 QAKCEGGTVVCGGKVIDRP----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTK 434
Cdd:cd07107  316 SAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148223856 435 DLGRIFRwlGPKGSDCGLVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRSTCTINY 498
Cdd:cd07107  396 DISQAHR--TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
41-489 3.74e-87

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: 277.97  E-value: 3.74e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  41 YCPATNAPIARVKQATLEEYNETVKKAKAAWQIWA-DIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGK-------IL 112
Cdd:cd07089    2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGApvmtaraMQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 113 VEGVGEVQEYVDicDYA--VGLSRIIGGPILPSErPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWK 190
Cdd:cd07089   82 VDGPIGHLRYFA--DLAdsFPWEFDLPVPALRGG-PGRRVVRR-EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 191 GAPTTSLTSVAVTKIVAQVlehnNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLEL 269
Cdd:cd07089  158 PAPDTPLSALLLGEIIAET----DLPaGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLEL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 270 GGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQA 349
Cdd:cd07089  234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 350 VEMYLSAVEQAKCEGGTVVCGGKvidRP-----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVK 424
Cdd:cd07089  314 RDRVEGYIARGRDEGARLVTGGG---RPagldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSD 390
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223856 425 QGLSSSIFTKDLGR---IFRWLgpkgsDCGLVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYM 489
Cdd:cd07089  391 YGLSGGVWSADVDRayrVARRI-----RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
PRK13473 PRK13473
gamma-aminobutyraldehyde dehydrogenase; Provisional
33-441 2.01e-86

gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 237391  Cd Length: 475  Bit Score: 276.41  E-value: 2.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  33 GKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGK-I 111
Cdd:PRK13473  14 GEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKpL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 112 LVEGVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKG 191
Cdd:PRK13473  94 HLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 192 APTTSLTSVAVTKIVAQVLEhnnlPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGG 271
Cdd:PRK13473 174 SEITPLTALKLAELAADILP----PGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 272 NNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVE 351
Cdd:PRK13473 250 KAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRD 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 352 MYLSAVEQAKCEG-GTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSS 430
Cdd:PRK13473 330 RVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASS 409
                        410
                 ....*....|.
gi 148223856 431 IFTKDLGRIFR 441
Cdd:PRK13473 410 VWTRDVGRAHR 420
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
61-479 3.08e-86

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: 274.72  E-value: 3.08e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  61 NETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEYVDICD-YAVGLSRIIGGP 139
Cdd:cd07100    2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAFLADE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 140 ILPSErPGHALIeQWNPVGLVGIITAFNFP---VAVYGwnnALALICGNVCLWKGAPTTSLTSVAVTKIVAQVlehnNLP 216
Cdd:cd07100   82 PIETD-AGKAYV-RYEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALAIEELFREA----GFP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 217 -GAICSLTCGGADIGNAIAkDERVDLVSFTGSTNVGKQVAlkvqERFGRKL----LELGGNNAIIVFEDADLSLVTPSVL 291
Cdd:cd07100  153 eGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVA----AEAGKNLkksvLELGGSDPFIVLDDADLDKAVKTAV 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 292 FAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQAKCEGGTVVCGG 371
Cdd:cd07100  228 KGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 372 KVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLG---RIFRWLgpkgs 448
Cdd:cd07100  308 KRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEraeRVARRL----- 382
                        410       420       430
                 ....*....|....*....|....*....|..
gi 148223856 449 DCGLVNVNIPT-SGAEIggAFGGEKHTGGGRE 479
Cdd:cd07100  383 EAGMVFINGMVkSDPRL--PFGGVKRSGYGRE 412
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
41-479 6.67e-86

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: 274.47  E-value: 6.67e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  41 YCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQ 120
Cdd:cd07149    4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 121 EYVDICDYAVGLSRIIGGPILPSE-------RPGHALIEqwnPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAP 193
Cdd:cd07149   84 RAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 194 TTSLTSVAVtkivAQVLEHNNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERfgRKLLELGGN 272
Cdd:cd07149  161 QTPLSALKL----AELLLEAGLPkGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLELGSN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 273 NAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEM 352
Cdd:cd07149  235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAER 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 353 YLSAVEQAKCEGGTVVCGGKvidRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIF 432
Cdd:cd07149  315 IEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 148223856 433 TKDLGRIFRWLgpKGSDCGLVNVN-IPTSGAEiGGAFGGEKHTGGGRE 479
Cdd:cd07149  392 TNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
32-498 1.11e-85

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: 275.64  E-value: 1.11e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  32 GGK----GEVVTSYCPA-TNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESL 106
Cdd:cd07124   38 GGKevrtEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 107 EMGKILVEGVGEVQEYVDICDYAVGLSRIIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNV 186
Cdd:cd07124  118 EVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEM-VPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNT 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 187 CLWKGAPTTSLtsvaVTKIVAQVLEHNNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVG---KQVALKVQERF 262
Cdd:cd07124  197 VVLKPAEDTPV----IAAKLVEILEEAGLPpGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlriYERAAKVQPGQ 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 263 G---RKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDT 339
Cdd:cd07124  273 KwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEV 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 340 LCGPLHTKQAVEMYLSAVEQAKcEGGTVVCGGKVIDRP--GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAF 417
Cdd:cd07124  353 YMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEAL 431
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 418 AWNNEVKQGLSSSIFTKDLGRI--FRwlgpKGSDCGLVNVNIPTSGAEIG-GAFGGEKHTG-GGRESGSDSWKHYMRRST 493
Cdd:cd07124  432 EIANDTEYGLTGGVFSRSPEHLerAR----REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507

                 ....*
gi 148223856 494 CTINY 498
Cdd:cd07124  508 VTENF 512
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4' ...
41-490 3.33e-84

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: 270.25  E-value: 3.33e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  41 YCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQ 120
Cdd:cd07099    1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 121 EYVDICDYAVGLSriigGPILPSER-------PGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAP 193
Cdd:cd07099   81 LALEAIDWAARNA----PRVLAPRKvptgllmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 194 TTSLTSVAVTKIVAQVlehnNLPGAICSLTCGGADIGNAIAkDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNN 273
Cdd:cd07099  157 VTPLVGELLAEAWAAA----GPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 274 AIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMY 353
Cdd:cd07099  232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 354 LSAVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFT 433
Cdd:cd07099  312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223856 434 KDL---GRIFRWLgpkgsDCGLVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDSWKHYMR 490
Cdd:cd07099  392 RDLaraEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
43-496 3.71e-84

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: 270.00  E-value: 3.71e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKIL-VEGVGEVQE 121
Cdd:cd07108    4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 122 YVDICDYAVGLSRIIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVA 201
Cdd:cd07108   84 LADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 202 VTKIVAQVLehnnlPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFED 280
Cdd:cd07108  163 LAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 281 ADLSLVTPSVLFAAVGT-AGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVEQ 359
Cdd:cd07108  238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 360 AKCE-GGTVVCGGK----VIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTK 434
Cdd:cd07108  318 GLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223856 435 DLGRIFRwlGPKGSDCGLVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDSW-KHYMRRSTCTI 496
Cdd:cd07108  398 DLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
38-479 8.36e-84

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: 269.11  E-value: 8.36e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  38 VTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVG 117
Cdd:cd07147    1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 118 EVQEYVDICDYAVGLSRIIGGPILP---SER-PGH-ALIEQWnPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGA 192
Cdd:cd07147   81 EVARAIDTFRIAAEEATRIYGEVLPldiSARgEGRqGLVRRF-PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 193 PTTSLTSVavtkIVAQVLEHNNLP-GAICSLTCGgADIGNAIAKDERVDLVSFTGSTNVGkqvaLKVQERFGRK--LLEL 269
Cdd:cd07147  160 SRTPLSAL----ILGEVLAETGLPkGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVG----WDLKARAGKKkvVLEL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 270 GGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQA 349
Cdd:cd07147  231 GGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 350 VEMYLSAVEQAKCEGGTVVCGGKvidRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSS 429
Cdd:cd07147  311 AERVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQA 387
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148223856 430 SIFTKDLGRIFR-WlgpKGSDCGLVNVN-IPTSGAEiGGAFGGEKHTGGGRE 479
Cdd:cd07147  388 GVFTRDLEKALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
43-496 8.61e-84

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: 269.85  E-value: 8.61e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQI--WADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEG-VGEV 119
Cdd:cd07091   26 PATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESaKGDV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 120 QEYVDICDYAVGLSRIIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTS 199
Cdd:cd07091  106 ALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 200 VAVTKIVAQVlehnNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKL-LELGGNNAIIV 277
Cdd:cd07091  185 LYLAELIKEA----GFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNLKKVtLELGGKSPNIV 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 278 FEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAV 357
Cdd:cd07091  261 FDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYI 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 358 EQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLG 437
Cdd:cd07091  341 ESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDIN 420
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 438 RIFR----------WLgpkgsDC-GLVNVNIPtsgaeiggaFGGEKHTGGGRESGSDSWKHYMRRSTCTI 496
Cdd:cd07091  421 KALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
Betaine_aldehyde_dehydrogenase TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
34-488 1.59e-83

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: 268.60  E-value: 1.59e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   34 KGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILV 113
Cdd:TIGR01804  11 AGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  114 E-GVGEVQEYVDICDYAVGLSRIIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGA 192
Cdd:TIGR01804  91 EtIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIR-EPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  193 PTTSLTSVAVtkivAQVLEHNNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGG 271
Cdd:TIGR01804 170 ENTPLTALKV----AEIMEEAGLPKGVFNVVQGdGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  272 NNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVE 351
Cdd:TIGR01804 246 KSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLISAAHRD 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  352 MYLSAVEQAKCEGGTVVCGGKVIDRP----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGL 427
Cdd:TIGR01804 326 KVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGL 405
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223856  428 SSSIFTKDLGRIFR----------WLgpkgSDCGLVNVNIPtsgaeiggaFGGEKHTGGGRESGSDSWKHY 488
Cdd:TIGR01804 406 AGGVFTADLGRAHRvadqleagtvWI----NTYNLYPAEAP---------FGGYKQSGIGRENGKAALAHY 463
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
43-496 3.07e-83

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: 267.67  E-value: 3.07e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQI--WADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQ 120
Cdd:cd07118    4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 121 EYVDICDYAVGLSRIIGGPI---LPSERPGHALIEqwnPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSL 197
Cdd:cd07118   84 GAADLWRYAASLARTLHGDSynnLGDDMLGLVLRE---PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 198 TSVavtkIVAQVLEHNNLPGAICS-LTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAII 276
Cdd:cd07118  161 TTL----MLAELLIEAGLPAGVVNiVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 277 VFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSA 356
Cdd:cd07118  237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 357 VEQAKCEGGTVVCGGKVID-RPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKD 435
Cdd:cd07118  317 VDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223856 436 LGRIFrwLGPKGSDCGLVNVN-IPTSGAEIggAFGGEKHTGGGRESGSDSWKHYMRRSTCTI 496
Cdd:cd07118  397 IDTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
29-481 3.39e-82

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: 265.21  E-value: 3.39e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  29 GTW--GGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQ--IWADIPAPKRGEIVRQIGDALRKKIKLLGHLE 104
Cdd:cd07139    5 GRWvaPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADELARLW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 105 SLEMGK-ILVEGVGEVQEYVDICDYAVGLSRiigGPILPSERP----GHALIEQwNPVGLVGIITAFNFPVAVYGWNNAL 179
Cdd:cd07139   85 TAENGMpISWSRRAQGPGPAALLRYYAALAR---DFPFEERRPgsggGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 180 ALICGNVCLWKGAPTTSLTSVavtkIVAQVLEHNNLPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQ 259
Cdd:cd07139  161 ALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 260 ERFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDT 339
Cdd:cd07139  237 ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPAT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 340 LCGPLHTKQA---VEMYlsaVEQAKCEGGTVVCGGKvidRP-----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFK 411
Cdd:cd07139  317 QIGPLASARQrerVEGY---IAKGRAEGARLVTGGG---RPagldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYD 390
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223856 412 TEEEAFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGLVNVNIPTSgaEIGGAFGGEKHTGGGRESG 481
Cdd:cd07139  391 DEDDAVRIANDSDYGLSGSVWTADVERglaVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
43-496 3.88e-81

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: 262.17  E-value: 3.88e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWA-DIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQE 121
Cdd:cd07109    4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 122 YVDICDYAVGLSRIIGGPILPSErPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSVA 201
Cdd:cd07109   84 AARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 202 VtkivAQVLEHNNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVFED 280
Cdd:cd07109  163 L----AELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 281 ADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGdPCEPDTLCGPL---HTKQAVEMYlsaV 357
Cdd:cd07109  239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLisaKQLDRVEGF---V 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 358 EQAKCEGGTVVCGGKVIDRP---GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTK 434
Cdd:cd07109  315 ARARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223856 435 DLGRIFRWlgPKGSDCGLVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMRRSTCTI 496
Cdd:cd07109  395 DGDRALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
43-481 2.92e-80

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428  Cd Length: 456  Bit Score: 259.98  E-value: 2.92e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQEY 122
Cdd:cd07110    4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 123 VDICDYAVGLS---RIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTS 199
Cdd:cd07110   84 AGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 200 VAVTKIVAQVlehnNLP-GAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVF 278
Cdd:cd07110  164 LELAEIAAEA----GLPpGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 279 EDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVE 358
Cdd:cd07110  240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 359 QAKCEGGTVVCGGKVID--RPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDL 436
Cdd:cd07110  320 RGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 148223856 437 GRIFRWlgPKGSDCGLVNVNIPTSgAEIGGAFGGEKHTGGGRESG 481
Cdd:cd07110  400 ERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELG 441
Succinate-semialdehyde_dehydrogenase_mitochondrial TIGR01780
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ...
41-489 3.03e-79

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: 256.97  E-value: 3.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   41 YCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEGVGEVQ 120
Cdd:TIGR01780   2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  121 EYVDICDYAVGLSRIIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSLTSV 200
Cdd:TIGR01780  82 YAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  201 AVtkivAQVLEHNNLP-GAICSLTCGGA-DIGNAIAKDERVDLVSFTGSTNVGKQVALKVQERFGRKLLELGGNNAIIVF 278
Cdd:TIGR01780 162 AL----ARLAEQAGIPkGVLNVITGSRAkEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  279 EDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLSAVE 358
Cdd:TIGR01780 238 DDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  359 QAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKDLGR 438
Cdd:TIGR01780 318 DAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSR 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 148223856  439 IFRWlgPKGSDCGLVNVNIPTSGAEIgGAFGGEKHTGGGRESGSDSWKHYM 489
Cdd:TIGR01780 398 IWRV--AEALEYGMVGINTGLISNVV-APFGGVKQSGLGREGSKYGIEEYL 445
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
43-490 3.97e-79

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: 257.42  E-value: 3.97e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  43 PATNAPIARVKQATLEEYNETVKKAKAAWQI--WADIPAPKRGEIVRQIGDALRKKIKLLGHLESLEMGKILVEG-VGEV 119
Cdd:cd07142   26 PRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 120 QEYVDICDYAVGLSRIIGGPILPSERPGHA--LIEqwnPVGLVGIITAFNFPVAVYGWNNALALICGNVCLWKGAPTTSL 197
Cdd:cd07142  106 PLAARLFRYYAGWADKIHGMTLPADGPHHVytLHE---PIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 198 TSVAVTKIVAQVlehnNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVA-LKVQERFGRKLLELGGNNAI 275
Cdd:cd07142  183 SALLAAKLAAEA----GLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMqLAAKSNLKPVTLELGGKSPF 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 276 IVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTLCGPLHTKQAVEMYLS 355
Cdd:cd07142  259 IVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILS 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 356 AVEQAKCEGGTVVCGGKVIDRPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEAFAWNNEVKQGLSSSIFTKD 435
Cdd:cd07142  339 YIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKN 418
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148223856 436 LGRIFRWLgpKGSDCGLVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDSWKHYMR 490
Cdd:cd07142  419 IDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
29-488 4.47e-79

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 257.38  E-value: 4.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  29 GTW--GGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESL 106
Cdd:cd07117    7 GEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 107 EMGKILVEGVGevqeyVDIcDYAVGLSRIIGGPILPSERPGHALIEQW------NPVGLVGIITAFNFPVAVYGWNNALA 180
Cdd:cd07117   87 DNGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 181 LICGNVCLWKGAPTTSLTSVAVTKIVAQVLEHnnlpGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQE 260
Cdd:cd07117  161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPK----GVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 261 RFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPDTL 340
Cdd:cd07117  237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 341 CGPLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRP----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFKTEEEA 416
Cdd:cd07117  317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223856 417 FAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGLVNVN----IPTsgaeiGGAFGGEKHTGGGRESGSDSWKHY 488
Cdd:cd07117  397 IDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRETHKSMLDAY 465
NAD-dependent_succinate_aldehyde_dehydrogenases TIGR02299
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ...
32-489 1.40e-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: 256.27  E-value: 1.40e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856   32 GGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESLE---- 107
Cdd:TIGR02299  12 SESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEIAVLECLDcgqp 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  108 ---MGKILVEGVGEVQEYVDICDYAVGlsriigGPILPSErpghaliEQWN-----PVGLVGIITAFNFPVAVYGWNNAL 179
Cdd:TIGR02299  92 lrqTRQQVIRAAENFRFFADKCEEAMD------GRTYPVD-------THLNytvrvPVGPVGLITPWNAPFMLSTWKIAP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  180 ALICGNVCLWKGAPTTSLTSVavtkIVAQVLEHNNLPGAICSLTCG-GADIGNAIAKDERVDLVSFTGSTNVGKQVALKV 258
Cdd:TIGR02299 159 ALAFGNTVVLKPAEWSPLTAA----RLAEIAKEAGLPDGVFNLVHGfGEEAGKALVAHPDVKAVSFTGETATGSIIMRNG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  259 QERFGRKLLELGGNNAIIVFEDADLSLVTPSVLFAAVGTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGDPCEPD 338
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  339 TLCGPLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVID-------RPGNFVEPTIMTGLAHDSAIVHKETFAPILYVIKFK 411
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  412 TEEEAFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGLVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDSW 485
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRV--ALALEAGMIWVNsqnvrhLPT-------PFGGVKASGIGREGGTYSF 465

                  ....
gi 148223856  486 KHYM 489
Cdd:TIGR02299 466 DFYT 469
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
29-498 1.46e-78

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471  Cd Length: 480  Bit Score: 256.12  E-value: 1.46e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856  29 GTW--GGKGEVVTSYCPATNAPIARVKQATLEEYNETVKKAKAAWQIWADIPAPKRGEIVRQIGDALRKKIKLLGHLESL 106
Cdd:cd07559    7 GEWvaPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 107 EMGKILVEGVGevqeyVDIcDYAVGLSRIIGGPILPSERPGHALIEQ------WNPVGLVGIITAFNFPVAVYGWNNALA 180
Cdd:cd07559   87 DNGKPIRETLA-----ADI-PLAIDHFRYFAGVIRAQEGSLSEIDEDtlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 181 LICGNVCLWKGAPTTSLTSVAVTKIVAQVLEhnnlPGAICSLTCGGADIGNAIAKDERVDLVSFTGSTNVGKQVALKVQE 260
Cdd:cd07559  161 LAAGNTVVLKPASQTPLSILVLMELIGDLLP----KGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 261 RFGRKLLELGGNNAIIVFEDA-------DLSLVTPSVLFAAvgTAGQRCTTARRLFLHESIHDEIVEKLSKAYAQVRIGD 333
Cdd:cd07559  237 NLIPVTLELGGKSPNIFFDDAmdadddfDDKAEEGQLGFAF--NQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGN 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 334 PCEPDTLCGPLHTKQAVEMYLSAVEQAKCEGGTVVCGGKVIDRP----GNFVEPTIMTGLAHDSAIVHKETFAPILYVIK 409
Cdd:cd07559  315 PLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVIT 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223856 410 FKTEEEAFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGLVNVN----IPTsgaeiGGAFGGEKHTG