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Conserved domains on  [gi|148231575|ref|NP_001084963|]
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serine palmitoyltransferase, long chain base subunit 1 L homeolog [Xenopus laevis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
23-471 1.01e-170

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member PLN02822:

Pssm-ID: 327488  Cd Length: 481  Bit Score: 493.49  E-value: 1.01e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  23 HLILEGILILWIIRLIFFKTYKLQERSdLTEKEKEELIDEWRPEPLVPPVSK----DHPALNYniVSGPpsHKIVvNGKE 98
Cdd:PLN02822  37 HLVVEGLLIVVIVFLLSQKSYKPPKRP-LTEKEIDELCDEWTPEPLIPPITEemrpEPPVLES--AAGP--HTII-NGKD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  99 CINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASAIPAYS 178
Cdd:PLN02822 111 VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFC 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 179 KRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQELEDqKNPRKacvTRRFIVAEGLYMNTGDICPLPK 258
Cdd:PLN02822 191 KKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN-KRKKK---LRRYIVVEAIYQNSGQIAPLDE 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 259 LVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSA 338
Cdd:PLN02822 267 IVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSA 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 339 SLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQGISGLKVVGESFSPAFHLQLEKSTGCREKDMKLLQNIIDHC 418
Cdd:PLN02822 347 SLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKSTGSAKEDLSLLEHIADRM 426
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148231575 419 MTRE---IALTQARYLEKEEkflPPPSIRVVVTVEQTEEELDTAASIIKQAASLFL 471
Cdd:PLN02822 427 LKEDsvlVVVSKRSTLDKCR---LPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
23-471 1.01e-170

serine palmitoyltransferase


Pssm-ID: 178417  Cd Length: 481  Bit Score: 493.49  E-value: 1.01e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  23 HLILEGILILWIIRLIFFKTYKLQERSdLTEKEKEELIDEWRPEPLVPPVSK----DHPALNYniVSGPpsHKIVvNGKE 98
Cdd:PLN02822  37 HLVVEGLLIVVIVFLLSQKSYKPPKRP-LTEKEIDELCDEWTPEPLIPPITEemrpEPPVLES--AAGP--HTII-NGKD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  99 CINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASAIPAYS 178
Cdd:PLN02822 111 VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFC 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 179 KRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQELEDqKNPRKacvTRRFIVAEGLYMNTGDICPLPK 258
Cdd:PLN02822 191 KKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN-KRKKK---LRRYIVVEAIYQNSGQIAPLDE 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 259 LVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSA 338
Cdd:PLN02822 267 IVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSA 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 339 SLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQGISGLKVVGESFSPAFHLQLEKSTGCREKDMKLLQNIIDHC 418
Cdd:PLN02822 347 SLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKSTGSAKEDLSLLEHIADRM 426
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148231575 419 MTRE---IALTQARYLEKEEkflPPPSIRVVVTVEQTEEELDTAASIIKQAASLFL 471
Cdd:PLN02822 427 LKEDsvlVVVSKRSTLDKCR---LPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];
92-466 1.09e-97

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];


Pssm-ID: 223234  Cd Length: 388  Bit Score: 302.64  E-value: 1.09e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  92 IVVNGKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVA 171
Cdd:COG0156   34 IRADGRKVLNFCSNDYLGLASHPELIEAAKAAIRRYGVGAGGSRLISGTSDLHVELEEELADFLGAEAALLFSSGFVANL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 172 SAIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEqeledqknPRKACVTRRFIVAEGLYMNTG 251
Cdd:COG0156  114 GLLSALLKKGDLIFSDELNHASIIDGIRLSRAEVRRFKHNDLDHLEALLEE--------ARENGARRKLIVTEGVFSMDG 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 252 DICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSG 331
Cdd:COG0156  186 DIAPLPELVELAEKYGALLYVDEAHAVGVLGPNGRGLAEHFGLEPEEVDIIVGTLGKALGSSGGYIAGSAALIDYLRNRA 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 332 QGYCFSASLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQgISGLkVVGESFSPAFHLQLekstgcreKDMKLL 411
Cdd:COG0156  266 RPFIFSTALPPAVAAAALAALRILEEGPERRERLQELAAFFRSLLK-ALGL-VLLPSESPIIPVIL--------GDEERA 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148231575 412 QNIIDHCMTREIaLTQArylekeekFLPP------PSIRVVVTVEQTEEELDTAASIIKQA 466
Cdd:COG0156  336 LEASRALLEEGI-YVSA--------IRPPtvpkgtARLRITLTAAHTEEDIDRLAEALSEV 387
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
97-466 2.81e-78

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747  Cd Length: 349  Bit Score: 250.94  E-value: 2.81e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  97 KECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASAIPA 176
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 177 YSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQeledqknprKACVTRRFIVAEGLYMNTGDICPL 256
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA---------RRPYGKKLIVTEGVYSMDGDIAPL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 257 PKLVELKYKYKVRIFLEESLSFGVLGEHGRGVtEHFGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCF 336
Cdd:cd06454  152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 337 SASLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQGIsGLKVVGESFSPAFHLQLEkstgcrekDMKLLQNIID 416
Cdd:cd06454  231 STSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPVGGSPSHIIPPLIGD--------DPAKAVAFSD 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148231575 417 HCMTREIALTQARY---LEKEEKflpppsIRVVVTVEQTEEELDTAASIIKQA 466
Cdd:cd06454  302 ALLERGIYVQAIRYptvPRGTAR------LRISLSAAHTKEDIDRLLEALKEV 348
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
83-467 1.14e-64

pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme subfamily related to three known enzymes; it appears closest to glycine C-acteyltransferase, shows no overlap with it in species distribution, and may share that function. The three closely related enzymes are glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), 5-aminolevulinic acid synthase, and 8-amino-7-oxononanoate synthase. All transfer the R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly, Gly, Ala, respectively), with release of CO2 for the latter two reactions.


Pssm-ID: 130884  Cd Length: 385  Bit Score: 216.61  E-value: 1.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575   83 IVSGPPSHKIVVNGKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAII 162
Cdd:TIGR01825  19 VLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLHEELEEKLAKFKKTEAALV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  163 YSYGFATVASAIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEqeledQKNPRKacvtrRFIV 242
Cdd:TIGR01825  99 FQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLRE-----NPSYGK-----KLIV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  243 AEGLYMNTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINiDDIDLISANMENALASIGGFCCGRSF 322
Cdd:TIGR01825 169 TDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLE-DKVDIQVGTLSKAIGVVGGYAAGHKE 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  323 VIDHQRLSGQGYCFSASLPPLLASAAIEGLNIMEENSEVfHDLRVKCKRIHKALQGISGLKvVGESFSPAFHLQLEKSTG 402
Cdd:TIGR01825 248 LIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPEL-MERLWDNTRFFKAGLGKLGYD-TGGSETPITPVVIGDEKA 325
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148231575  403 CREKDMKLL-QNIIDHCMT-REIALTQARylekeekflpppsIRVVVTVEQTEEELDTAASIIKQAA 467
Cdd:TIGR01825 326 AQEFSRRLFdEGIFAQSIVfPTVPRGTAR-------------IRNIPTAEHTKDDLDQALDAYEKVG 379
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
97-463 1.38e-28

Aminotransferase class I and II;


Pssm-ID: 306629  Cd Length: 351  Bit Score: 115.87  E-value: 1.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575   97 KECINFASFNFLGLLdnarVKSAALASLRkygVGTCGPRGFYGTFDVHLELEERLAKFM--------KTEEAIIYSYGFA 168
Cdd:pfam00155   1 TDKINLGSNEYLGDT----LPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  169 TVASAIPAYSK-RGDIVFADEAACFAIQKGLQASRSSIKYFK-------HNDMDDLERLLKEQeledqknprkacvtRRF 240
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK--------------PKV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  241 IVAEGLYMNTGDICPLP---KLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGinIDDIDLISAN-MENALASIG-- 314
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRALL--AEGPNLLVVGsFSKAFGLAGwr 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  315 -GFCCGRSFVIDHQRLSGQGYCFSASLPPLLASAAIEGLNI---MEENSEVFHDLRvkcKRIHKALQGIsGLKVVGeSFS 390
Cdd:pfam00155 218 vGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVaseLEEMRQRIKERR---DYLRDGLQAA-GLSVLP-SQA 292
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148231575  391 PAFHLQLekstGCREKDMKLLQNIIDHCmtrEIALTQARYlekeekFLPPPSIRVVVTVeQTEEELDTAASII 463
Cdd:pfam00155 293 GFFLLTG----LDPETAKELAQVLLEEV---GVYVTPGSS------PGVPGWLRITVAG-GTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
23-471 1.01e-170

serine palmitoyltransferase


Pssm-ID: 178417  Cd Length: 481  Bit Score: 493.49  E-value: 1.01e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  23 HLILEGILILWIIRLIFFKTYKLQERSdLTEKEKEELIDEWRPEPLVPPVSK----DHPALNYniVSGPpsHKIVvNGKE 98
Cdd:PLN02822  37 HLVVEGLLIVVIVFLLSQKSYKPPKRP-LTEKEIDELCDEWTPEPLIPPITEemrpEPPVLES--AAGP--HTII-NGKD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  99 CINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASAIPAYS 178
Cdd:PLN02822 111 VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFC 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 179 KRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQELEDqKNPRKacvTRRFIVAEGLYMNTGDICPLPK 258
Cdd:PLN02822 191 KKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN-KRKKK---LRRYIVVEAIYQNSGQIAPLDE 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 259 LVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSA 338
Cdd:PLN02822 267 IVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSA 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 339 SLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQGISGLKVVGESFSPAFHLQLEKSTGCREKDMKLLQNIIDHC 418
Cdd:PLN02822 347 SLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKSTGSAKEDLSLLEHIADRM 426
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148231575 419 MTRE---IALTQARYLEKEEkflPPPSIRVVVTVEQTEEELDTAASIIKQAASLFL 471
Cdd:PLN02822 427 LKEDsvlVVVSKRSTLDKCR---LPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
100-471 3.65e-108

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766  Cd Length: 392  Bit Score: 329.94  E-value: 3.65e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 100 INFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASAIPAYSK 179
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 180 RGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQELEDQKNPRKACVTRRFIVAEGLYMNTGDICPLPKL 259
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 260 VELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGIN-IDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSA 338
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 339 SLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQGIS---------GLKVVGESFSPAFHLQLEKSTGCREKDMK 409
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNSShpyalklrnRLVITSDPISPIIYLRLSDQEATRRTDET 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148231575 410 L-LQNIIDHCMTREIALTQAR-YLEKEEKFLPPPSIRVVVTVEQTEEELDTAASIIKQAASLFL 471
Cdd:PLN03227 321 LiLDQIAHHSLSEGVAVVSTGgHVKKFLQLVPPPCLRVVANASHTREDIDKLLTVLGEAVEAIL 384
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];
92-466 1.09e-97

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism];


Pssm-ID: 223234  Cd Length: 388  Bit Score: 302.64  E-value: 1.09e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  92 IVVNGKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVA 171
Cdd:COG0156   34 IRADGRKVLNFCSNDYLGLASHPELIEAAKAAIRRYGVGAGGSRLISGTSDLHVELEEELADFLGAEAALLFSSGFVANL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 172 SAIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEqeledqknPRKACVTRRFIVAEGLYMNTG 251
Cdd:COG0156  114 GLLSALLKKGDLIFSDELNHASIIDGIRLSRAEVRRFKHNDLDHLEALLEE--------ARENGARRKLIVTEGVFSMDG 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 252 DICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSG 331
Cdd:COG0156  186 DIAPLPELVELAEKYGALLYVDEAHAVGVLGPNGRGLAEHFGLEPEEVDIIVGTLGKALGSSGGYIAGSAALIDYLRNRA 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 332 QGYCFSASLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQgISGLkVVGESFSPAFHLQLekstgcreKDMKLL 411
Cdd:COG0156  266 RPFIFSTALPPAVAAAALAALRILEEGPERRERLQELAAFFRSLLK-ALGL-VLLPSESPIIPVIL--------GDEERA 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148231575 412 QNIIDHCMTREIaLTQArylekeekFLPP------PSIRVVVTVEQTEEELDTAASIIKQA 466
Cdd:COG0156  336 LEASRALLEEGI-YVSA--------IRPPtvpkgtARLRITLTAAHTEEDIDRLAEALSEV 387
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
97-466 2.81e-78

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747  Cd Length: 349  Bit Score: 250.94  E-value: 2.81e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  97 KECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASAIPA 176
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 177 YSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQeledqknprKACVTRRFIVAEGLYMNTGDICPL 256
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA---------RRPYGKKLIVTEGVYSMDGDIAPL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 257 PKLVELKYKYKVRIFLEESLSFGVLGEHGRGVtEHFGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCF 336
Cdd:cd06454  152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 337 SASLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQGIsGLKVVGESFSPAFHLQLEkstgcrekDMKLLQNIID 416
Cdd:cd06454  231 STSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPVGGSPSHIIPPLIGD--------DPAKAVAFSD 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148231575 417 HCMTREIALTQARY---LEKEEKflpppsIRVVVTVEQTEEELDTAASIIKQA 466
Cdd:cd06454  302 ALLERGIYVQAIRYptvPRGTAR------LRISLSAAHTKEDIDRLLEALKEV 348
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
83-467 1.14e-64

pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme subfamily related to three known enzymes; it appears closest to glycine C-acteyltransferase, shows no overlap with it in species distribution, and may share that function. The three closely related enzymes are glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), 5-aminolevulinic acid synthase, and 8-amino-7-oxononanoate synthase. All transfer the R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly, Gly, Ala, respectively), with release of CO2 for the latter two reactions.


Pssm-ID: 130884  Cd Length: 385  Bit Score: 216.61  E-value: 1.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575   83 IVSGPPSHKIVVNGKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAII 162
Cdd:TIGR01825  19 VLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLHEELEEKLAKFKKTEAALV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  163 YSYGFATVASAIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEqeledQKNPRKacvtrRFIV 242
Cdd:TIGR01825  99 FQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLRE-----NPSYGK-----KLIV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  243 AEGLYMNTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINiDDIDLISANMENALASIGGFCCGRSF 322
Cdd:TIGR01825 169 TDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLE-DKVDIQVGTLSKAIGVVGGYAAGHKE 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  323 VIDHQRLSGQGYCFSASLPPLLASAAIEGLNIMEENSEVfHDLRVKCKRIHKALQGISGLKvVGESFSPAFHLQLEKSTG 402
Cdd:TIGR01825 248 LIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPEL-MERLWDNTRFFKAGLGKLGYD-TGGSETPITPVVIGDEKA 325
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148231575  403 CREKDMKLL-QNIIDHCMT-REIALTQARylekeekflpppsIRVVVTVEQTEEELDTAASIIKQAA 467
Cdd:TIGR01825 326 AQEFSRRLFdEGIFAQSIVfPTVPRGTAR-------------IRNIPTAEHTKDDLDQALDAYEKVG 379
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
83-464 1.15e-63

8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273303  Cd Length: 360  Bit Score: 213.28  E-value: 1.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575   83 IVSGPPSHKIVVNGKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAII 162
Cdd:TIGR00858   2 PLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  163 YSYGFATVASAIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQELEDQKnprkacvtrrFIV 242
Cdd:TIGR00858  82 FSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRK----------LIV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  243 AEGLYMNTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINIDDIDLISANMENALASIGGFCCGRSF 322
Cdd:TIGR00858 152 TDGVFSMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  323 VIDHQRLSGQGYCFSASLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHKALQGISGlkVVGESFSPAFHLQLEKStg 402
Cdd:TIGR00858 232 LIDYLINRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGF--TLMPSCTPIVPVIIGDN-- 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148231575  403 crekdmkllqniidhcmtrEIALTQARYLEKEEKFLP---PPS-------IRVVVTVEQTEEELDTAASIIK 464
Cdd:TIGR00858 308 -------------------ASALALAEELQQQGIFVGairPPTvpagtsrLRLTLSAAHTPGDIDRLAEALK 360
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
83-360 8.31e-53

2-amino-3-ketobutyrate coenzyme A ligase; Provisional


Pssm-ID: 235893  Cd Length: 397  Bit Score: 185.01  E-value: 8.31e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  83 IVSGPPSHKI-VVNGKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAI 161
Cdd:PRK06939  27 VITSPQGADItVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 162 IYSYGFATVASAIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQeledqknpRKACVTRRFI 241
Cdd:PRK06939 107 LYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEA--------KEAGARHKLI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 242 VAEGLYMNTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGInIDDIDLISANMENALA-SIGGFCCGR 320
Cdd:PRK06939 179 ATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGV-MDRVDIITGTLGKALGgASGGYTAGR 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148231575 321 SFVIDHQRLSGQGYCFSASLPPLLASAAIEGLNIMEENSE 360
Cdd:PRK06939 258 KEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDE 297
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
83-360 9.32e-52

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655  Cd Length: 385  Bit Score: 181.89  E-value: 9.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  83 IVSGPPSHKIVVNGKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAII 162
Cdd:PRK05958  25 PREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 163 YSYGFATVASAIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLkeqeledqknpRKACVTRRFIV 242
Cdd:PRK05958 105 FSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALL-----------AKWRAGRALIV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 243 AEGLYMNTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGInIDDIDLIS-ANMENALASIGGFCCGRS 321
Cdd:PRK05958 174 TESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGL-AGEPDVILvGTLGKALGSSGAAVLGSE 252
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148231575 322 FVIDHQRLSGQGYCFSASLPPLLASAAIEGLNIMEENSE 360
Cdd:PRK05958 253 TLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE 291
PLN02483 PLN02483
serine palmitoyltransferase
95-391 8.82e-51

serine palmitoyltransferase


Pssm-ID: 178101  Cd Length: 489  Bit Score: 181.88  E-value: 8.82e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  95 NGKECINFASFNFLGLLD-NARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASA 173
Cdd:PLN02483  98 KTRRCLNLGSYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTI 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 174 IPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQELEDQknPRkacvTRR-----FIVAEGLYM 248
Cdd:PLN02483 178 IPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQ--PR----THRpwkkiIVIVEGIYS 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 249 NTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINIDDIDLISANMENALASIGGFCCGRSFVIDHQR 328
Cdd:PLN02483 252 MEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLK 331
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148231575 329 LSGQGYCFSASLPPLLASAAI---------EGLNI-------MEENSEVFHDlrvkckrihkALQGIsGLKVVGESFSP 391
Cdd:PLN02483 332 RTCPAHLYATSMSPPAVQQVIsaikvilgeDGTNRgaqklaqIRENSNFFRS----------ELQKM-GFEVLGDNDSP 399
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
83-459 1.32e-46

glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130881  Cd Length: 393  Bit Score: 168.06  E-value: 1.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575   83 IVSGPPSHKIVVN-GKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAI 161
Cdd:TIGR01822  23 IITSPQGADIRVAdGREVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFICGTQDIHKELEAKIAAFLGTEDTI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  162 IYSYGFATVASAIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQeledqknpRKACVTRRFI 241
Cdd:TIGR01822 103 LYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEA--------RAAGARHRLI 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  242 VAEGLYMNTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGInIDDIDLISANMENAL-ASIGGFCCGR 320
Cdd:TIGR01822 175 ATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGV-MGRVDIITGTLGKALgGASGGFTTAR 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  321 SFVIDHQRLSGQGYCFSASLPPLLASAAIEGLNIMEENSEVFHDLRVKCKRIHkalqgiSGLKVVGESFSPAFHLQLEKS 400
Cdd:TIGR01822 254 KEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFR------ERMEAAGFDIKPADHPIIPVM 327
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148231575  401 TGcrekDMKLLQNIIDHCMTREIALT----------QARylekeekflpppsIRVVVTVEQTEEELDTA 459
Cdd:TIGR01822 328 LY----DAVLAQRFARRLLEEGIYVTgffypvvpkgQAR-------------IRVQISAAHTEEQLDRA 379
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
99-377 1.37e-37

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820  Cd Length: 402  Bit Score: 142.94  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575   99 CINfasfNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGF-------ATVA 171
Cdd:TIGR01821  51 CSN----DYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYvandatlATLA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  172 SAIPayskrGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEqelEDQKNPrkacvtrRFIVAEGLYMNTG 251
Cdd:TIGR01821 127 KIIP-----GCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQS---VDPNRP-------KIIAFESVYSMDG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  252 DICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGInIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSG 331
Cdd:TIGR01821 192 DIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYA 270
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 148231575  332 QGYCFSASLPPLLASAAIEGLNIMEENSevfhDLRVK----CKRIHKALQ 377
Cdd:TIGR01821 271 PGFIFTTSLPPAIAAGATASIRHLKESQ----DLRRAhqenVKRLKNLLE 316
PRK09064 PRK09064
5-aminolevulinate synthase; Validated
99-348 2.80e-36

5-aminolevulinate synthase; Validated


Pssm-ID: 236370  Cd Length: 407  Bit Score: 139.22  E-value: 2.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  99 CINfasfNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGF-------ATVA 171
Cdd:PRK09064  52 CSN----DYLGMGQHPKVIEAMIEALDRCGAGAGGTRNISGTNHYHVELERELADLHGKEAALVFTSGYvsndatlSTLA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 172 SAIPayskrGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQELEDQKnprkacvtrrFIVAEGLYMNTG 251
Cdd:PRK09064 128 KLIP-----DCVIFSDELNHASMIEGIRRSRCEKHIFRHNDVAHLEELLAAADPDRPK----------LIAFESVYSMDG 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 252 DICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGInIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSG 331
Cdd:PRK09064 193 DIAPIAEICDLADKYNALTYLDEVHAVGMYGPRGGGIAERDGL-MDRIDIIEGTLAKAFGVMGGYIAGSAALVDAVRSYA 271
                        250
                 ....*....|....*..
gi 148231575 332 QGYCFSASLPPLLASAA 348
Cdd:PRK09064 272 PGFIFTTSLPPAIAAAA 288
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
97-348 1.42e-31

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023  Cd Length: 410  Bit Score: 125.35  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  97 KECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASAIPA 176
Cdd:PRK13392  46 RRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALST 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 177 YSKR--GDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQELEDQKnprkacvtrrFIVAEGLYMNTGDIC 254
Cdd:PRK13392 126 LGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPK----------LIAFESVYSMDGDIA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 255 PLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGInIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGY 334
Cdd:PRK13392 196 PIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGF 274
                        250
                 ....*....|....
gi 148231575 335 CFSASLPPLLASAA 348
Cdd:PRK13392 275 IFTTALPPAVAAGA 288
PRK13393 PRK13393
5-aminolevulinate synthase; Provisional
104-348 2.15e-31

5-aminolevulinate synthase; Provisional


Pssm-ID: 184024  Cd Length: 406  Bit Score: 124.82  E-value: 2.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 104 SFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGF-------ATVASAIPa 176
Cdd:PRK13393  52 SNDYLGMGQHPAVLAAMHEALDTCGAGAGGTRNISGTNHYHVLLEAELADLHGKEAALLFTSGYvsnwaalSTLGSRLP- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 177 yskrGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQeleDQKNPRkacvtrrfIVA-EGLYMNTGDICP 255
Cdd:PRK13393 131 ----GCVILSDELNHASMIEGIRHSRAEKRIFRHNDPADLERKLSDL---DPHRPK--------LVAfESVYSMDGDIAP 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 256 LPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGInIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYC 335
Cdd:PRK13393 196 IAEICDVAEKHGAMTYLDEVHAVGLYGPRGGGIAEREGL-ADRLTIIEGTLAKAFGVMGGYITGSAALCDFIRSFASGFI 274
                        250
                 ....*....|...
gi 148231575 336 FSASLPPLLASAA 348
Cdd:PRK13393 275 FTTSLPPAVAAGA 287
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
97-463 1.38e-28

Aminotransferase class I and II;


Pssm-ID: 306629  Cd Length: 351  Bit Score: 115.87  E-value: 1.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575   97 KECINFASFNFLGLLdnarVKSAALASLRkygVGTCGPRGFYGTFDVHLELEERLAKFM--------KTEEAIIYSYGFA 168
Cdd:pfam00155   1 TDKINLGSNEYLGDT----LPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  169 TVASAIPAYSK-RGDIVFADEAACFAIQKGLQASRSSIKYFK-------HNDMDDLERLLKEQeledqknprkacvtRRF 240
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK--------------PKV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  241 IVAEGLYMNTGDICPLP---KLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGinIDDIDLISAN-MENALASIG-- 314
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRALL--AEGPNLLVVGsFSKAFGLAGwr 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  315 -GFCCGRSFVIDHQRLSGQGYCFSASLPPLLASAAIEGLNI---MEENSEVFHDLRvkcKRIHKALQGIsGLKVVGeSFS 390
Cdd:pfam00155 218 vGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVaseLEEMRQRIKERR---DYLRDGLQAA-GLSVLP-SQA 292
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148231575  391 PAFHLQLekstGCREKDMKLLQNIIDHCmtrEIALTQARYlekeekFLPPPSIRVVVTVeQTEEELDTAASII 463
Cdd:pfam00155 293 GFFLLTG----LDPETAKELAQVLLEEV---GVYVTPGSS------PGVPGWLRITVAG-GTEEELEELLEAI 351
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
97-349 2.16e-17

8-amino-7-oxononanoate synthase


Pssm-ID: 178541  Cd Length: 476  Bit Score: 84.34  E-value: 2.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  97 KECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFA-------- 168
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAanmaamva 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 169 --TVASAIPAYSK----RGDIVFADEAACFAIQKGLQ-ASR---SSIKYFKHNDMDDLERLLKEQELEdqknprkacvtR 238
Cdd:PLN02955 182 igSVASLLAASGKplknEKVAIFSDALNHASIIDGVRlAERqgnVEVFVYRHCDMYHLNSLLSSCKMK-----------R 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 239 RFIVAEGLYMNTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINiDDIDLISANMENALASIGGF-- 316
Cdd:PLN02955 251 KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFia 329
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148231575 317 CCGRSFVIDHQRlsGQGYCFSASLPPLLASAAI 349
Cdd:PLN02955 330 CSKKWKQLIQSR--GRSFIFSTAIPVPMAAAAY 360
PRK07179 PRK07179
hypothetical protein; Provisional
96-342 4.42e-17

hypothetical protein; Provisional


Pssm-ID: 180866  Cd Length: 407  Bit Score: 82.75  E-value: 4.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  96 GKECINFASFNFLGLLDNARVKSAALASLRKYGVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVASAIP 175
Cdd:PRK07179  53 GPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQ 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 176 AYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLkeqeledqknprkacvtRRF----IVAEGLYMNTG 251
Cdd:PRK07179 133 TIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQI-----------------ERHgpgiIVVDSVYSTTG 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 252 DICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFGINiDDIDLISANMENALASIGGFCCGRSFVIDHQRLSG 331
Cdd:PRK07179 196 TIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLAKAFAGRAGIITCPRELAEYVPFVS 274
                        250
                 ....*....|.
gi 148231575 332 QGYCFSASLPP 342
Cdd:PRK07179 275 YPAIFSSTLLP 285
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
100-293 1.68e-16

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071  Cd Length: 370  Bit Score: 80.60  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 100 INFASFNFLGLLDNARVKSAALASLRKY-------GVGTCGPRGFYGTFDVHLELEERLAKFMKTEEAIIYSYGFATVAS 172
Cdd:PRK05937   7 IDFVTNDFLGFSRSTTLVHEVEKRYRLYceqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 173 AIPAYSKRGDIVFADEAACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQeledqknpRKACVTRRFIVAEGLYMNTGD 252
Cdd:PRK05937  87 LCAHLSSVTDYVLWDEQVHISVVYSLSVISGKHQSFRHNDLDHLESLLESC--------RAVSFGRIFIFVCSVYSFKGT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148231575 253 ICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRGVTEHFG 293
Cdd:PRK05937 159 LAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG 199
PRK07505 PRK07505
hypothetical protein; Provisional
96-349 1.72e-16

hypothetical protein; Provisional


Pssm-ID: 181006  Cd Length: 402  Bit Score: 81.18  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575  96 GKECINFASFNFLGLLDNARVKSAALASLRKYGV-GTCGPRGFYgTFDVHLELEERLAKFMKTEEAIIYSYGFAT----- 169
Cdd:PRK07505  45 GHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRV-RSQILKDLEEALSELFGASVLTFTSCSAAHlgilp 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 170 -VASAIPAYSKRGDIVFADEA-ACFAIQKGLQASRSSIKYFKHNDMDDLERLLKEQEledqknprkacvtRRFIVAEGLY 247
Cdd:PRK07505 124 lLASGHLTGGVPPHMVFDKNAhASLNILKGICADETEVETIDHNDLDALEDICKTNK-------------TVAYVADGVY 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148231575 248 mNTGDICPLPKLVELKYKYKVRIFLEESLSFGVLGEHGRG-VTEHFGINIDDIDLISANMENALASIGGFC-CGRSFVID 325
Cdd:PRK07505 191 -SMGGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRLNERTIIAASLGKAFGASGGVImLGDAEQIE 269
                        250       260
                 ....*....|....*....|....*....
gi 148231575 326 HQRLSGQGYCFSASL--PPL---LASAAI 349
Cdd:PRK07505 270 LILRYAGPLAFSQSLnvAALgaiLASAEI 298
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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