|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
1-396 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 635.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 1 MSSKVLDqFLETNLEDLKEKGLFNTIDVLEGSNGPIITVND-KKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAV 79
Cdd:PRK06939 1 MSGAFYA-QLREELEEIKAEGLYKEERVITSPQGADITVADgKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 80 RTINGTLDIHQKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDME 159
Cdd:PRK06939 80 RFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 160 DLEAKAKAATESGeYNKVMYITDGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMG-HGHGTVKHFEMQDHIDFQ 238
Cdd:PRK06939 160 DLEAQLKEAKEAG-ARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGeNGRGTVEHFGVMDRVDII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 239 MGTLSKGI-GVVGGYVAGTKQLITWLKSQARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGY 317
Cdd:PRK06939 239 TGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1646957387 318 DIGKSETPITPVIVGDEKLAQEFSKKLLENGVYVKPIVYPTVPLGTGRVRNMPNAGHTKEMLDDAIKVYEKVGKELGII 396
Cdd:PRK06939 319 TLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| gly_Cac_T_rel |
TIGR01825 |
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ... |
10-396 |
0e+00 |
|
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 [Multi-domain] Cd Length: 385 Bit Score: 599.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 10 LETNLEDLKEKGLFNTIDVLEGSNGPIITVNDKKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGTLDIH 89
Cdd:TIGR01825 1 LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 90 QKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKaat 169
Cdd:TIGR01825 81 EELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 170 ESGEYNKVMYITDGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMG-HGHGTVKHFEMQDHIDFQMGTLSKGIGV 248
Cdd:TIGR01825 158 ENPSYGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGeAGRGTVHHFGLEDKVDIQVGTLSKAIGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 249 VGGYVAGTKQLITWLKSQARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGYDIGKSETPITP 328
Cdd:TIGR01825 238 VGGYAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1646957387 329 VIVGDEKLAQEFSKKLLENGVYVKPIVYPTVPLGTGRVRNMPNAGHTKEMLDDAIKVYEKVGKELGII 396
Cdd:TIGR01825 318 VVIGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDAYEKVGKELGLI 385
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
6-392 |
0e+00 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 581.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 6 LDQFLETNLEDLKEKGLFNTIDVLEGSNGPIITVNDKKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGT 85
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 86 LDIHQKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKA 165
Cdd:COG0156 81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 166 KAAtesGEYNKVMYITDGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMG-HGHGTVKHFEMQDHIDFQMGTLSK 244
Cdd:COG0156 161 KKA---RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGeTGRGLVEHFGLEDRVDIIMGTLSK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 245 GIGVVGGYVAGTKQLITWLKSQARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGYDIGKSET 324
Cdd:COG0156 238 ALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSES 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1646957387 325 PITPVIVGDEKLAQEFSKKLLENGVYVKPIVYPTVPLGTGRVRNMPNAGHTKEMLDDAIKVYEKVGKE 392
Cdd:COG0156 318 PIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
42-390 |
9.18e-171 |
|
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 [Multi-domain] Cd Length: 349 Bit Score: 480.90 E-value: 9.18e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 42 KKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGTLDIHQKLEEKIAEFKGTEAAIAFQSGFNCNMGAISA 121
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 122 VMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKAATESgeYNKVMYITDGVFSMDGDVAKIPEIVEIC 201
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRP--YGKKLIVTEGVYSMDGDIAPLPELVDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 202 EKYNVITYVDDAHGTGVMG-HGHGTVKHFEMQDHIDFQMGTLSKGIGVVGGYVAGTKQLITWLKSQARPFLFSTSLTPGA 280
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGpHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 281 AGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGYDIGKSE-TPITPVIVGDEKLAQEFSKKLLENGVYVKPIVYPTV 359
Cdd:cd06454 239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318
|
330 340 350
....*....|....*....|....*....|.
gi 1646957387 360 PLGTGRVRNMPNAGHTKEMLDDAIKVYEKVG 390
Cdd:cd06454 319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
29-387 |
1.12e-149 |
|
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 [Multi-domain] Cd Length: 360 Bit Score: 427.84 E-value: 1.12e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 29 LEGSNGPIITVNDKKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGTLDIHQKLEEKIAEFKGTEAAIAF 108
Cdd:TIGR00858 3 LDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 109 QSGFNCNMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKaatESGEYNKVMYITDGVFSMD 188
Cdd:TIGR00858 83 SSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLE---KNRGERRKLIVTDGVFSMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 189 GDVAKIPEIVEICEKYNVITYVDDAHGTGVMG-HGHGTVKHFEM-QDHIDFQMGTLSKGIGVVGGYVAGTKQLITWLKSQ 266
Cdd:TIGR00858 160 GDIAPLPQLVALAERYGAWLMVDDAHGTGVLGeDGRGTLEHFGLkPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 267 ARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGYDIGKSETPITPVIVGDEKLAQEFSKKLLE 346
Cdd:TIGR00858 240 ARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQ 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1646957387 347 NGVYVKPIVYPTVPLGTGRVRNMPNAGHTKEMLDDAIKVYE 387
Cdd:TIGR00858 320 QGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
10-385 |
2.74e-145 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 417.64 E-value: 2.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 10 LETNLEDLKEKGLFNTIDVLEGSNGPIITVNDKKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGTLDIH 89
Cdd:PRK05958 7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 90 QKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKAAT 169
Cdd:PRK05958 87 EALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 170 EsgeyNKVMYITDGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMG-HGHGTVKHFEMQDHID-FQMGTLSKGIG 247
Cdd:PRK05958 167 A----GRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGpQGRGLAAEAGLAGEPDvILVGTLGKALG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 248 VVGGYVAGTKQLITWLKSQARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGYDIGKSETPIT 327
Cdd:PRK05958 243 SSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQ 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1646957387 328 PVIVGDEKLAQEFSKKLLENGVYVKPIVYPTVPLGTGRVRNMPNAGHTKEMLDDAIKV 385
Cdd:PRK05958 323 PLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEA 380
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
26-395 |
1.71e-89 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 278.95 E-value: 1.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 26 IDVLE----GSNGPII-TVNDKKMINLASNNYLGFATRPELIEADVEAT-KHYGAGAGAVRTINGTLDIHQKLEEKIAEF 99
Cdd:PLN02483 79 FDVVErvsnDNNKTLKrTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESlKKYSASTCSSRVDGGTTKLHRELEELVARF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 100 KGTEAAIAFQSGFNCNMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKAATESGE------ 173
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQprthrp 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 174 YNKVMYITDGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMGH-GHGTVKHF--EMQDhIDFQMGTLSKGIGVVG 250
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKtGRGVCELLgvDPAD-VDIMMGTFTKSFGSCG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 251 GYVAGTKQLITWLKSQARPFLFSTSLTPGAAGACIKAIDLI------EEHPEYVDTLWDNANYFKAELKRIGYD-IGKSE 323
Cdd:PLN02483 318 GYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVIlgedgtNRGAQKLAQIRENSNFFRSELQKMGFEvLGDND 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1646957387 324 TPITPVIVGDEKLAQEFSKKLLENGVYVKPIVYPTVPLGTGRVRNMPNAGHTKEMLDDAIKVYEKVGKELGI 395
Cdd:PLN02483 398 SPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
7-380 |
4.80e-83 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 259.79 E-value: 4.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 7 DQFLETNLEDLKEKGLFNTIDVLEGSNGPIITVND------KKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVR 80
Cdd:PRK13392 5 DSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDhgpdgpRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 81 TINGTLDIHQKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMKK--GDAILSDELNHASIIDGCRLSGAKIIRVNHQDM 158
Cdd:PRK13392 85 NISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 159 EDLEAKAKAATESgeyNKVMYITDGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMG-HGHGTVKHFEMQDHIDF 237
Cdd:PRK13392 165 ADLEEQLASVDPD---RPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGaRGGGIAERDGLMDRIDM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 238 QMGTLSKGIGVVGGYVAGTKQLITWLKSQARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGY 317
Cdd:PRK13392 242 IQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGI 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1646957387 318 DIGKSETPITPVIVGDEKLAQEFSKKLL-ENGVYVKPIVYPTVPLGTGRVRNMPNAGHTKEMLD 380
Cdd:PRK13392 322 PVMPSPSHIVPVMVGDPTLCKAISDRLMsEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDID 385
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-384 |
4.41e-69 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 221.80 E-value: 4.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 42 KKMINLASNNYLGfatrpELIEADVEATKHygAGAGAVRTINGTLDIHQKLEEKIAEFKGT--------EAAIAFQSGFN 113
Cdd:pfam00155 1 TDKINLGSNEYLG-----DTLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 114 CNMGAISAVMK-KGDAILSDELNHASIIDGCRLSGAKIIRVN-------HQDMEDLEAKAKAATesgeynKVMYITdGVF 185
Cdd:pfam00155 74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP------KVVLHT-SPH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 186 SMDGDVAKIPEIVEI---CEKYNVITYVDDAHGTGVMGHGHGTVKHFEMQDHID-FQMGTLSKGIGVVG---GYVAGTKQ 258
Cdd:pfam00155 147 NPTGTVATLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 259 LITWLKSQARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGYDIGKSETPITPVIVGDEKLAQ 338
Cdd:pfam00155 227 VISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAK 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1646957387 339 EFSKKLLEN-GVYVKPIVYPTVPlGTGRVrNMpnAGHTKEMLDDAIK 384
Cdd:pfam00155 307 ELAQVLLEEvGVYVTPGSSPGVP-GWLRI-TV--AGGTEEELEELLE 349
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
42-377 |
1.16e-56 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 192.97 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 42 KKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGTLDIHQKLEEKIAEFKGTEAAIAFQSGFNCNM----- 116
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMaamva 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 117 -GAISAVMKKGD--------AILSDELNHASIIDGCRLS----GAKIIRVNHQDMEDLEAKAKAATesgeYNKVMYITDG 183
Cdd:PLN02955 182 iGSVASLLAASGkplknekvAIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCK----MKRKVVVTDS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 184 VFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMG-HGHGTVKHFEMQDHIDFQMGTLSKGIGVVGGYVAGTKQLITW 262
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGeNGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 263 LKSQARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAelkRIGYDIGkseTPITPVIVGDEKLAQEFSK 342
Cdd:PLN02955 338 IQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKA---LSGVDIS---SPIISLVVGNQEKALKASR 411
|
330 340 350
....*....|....*....|....*....|....*
gi 1646957387 343 KLLENGVYVKPIVYPTVPLGTGRVRNMPNAGHTKE 377
Cdd:PLN02955 412 YLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
28-391 |
2.11e-55 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 189.57 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 28 VLEGSNGPIITVNDKKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGTLDIHQKLEEKIAEFKGTEAAIA 107
Cdd:PLN02822 95 VLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSIL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 108 FQSGFNCNMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKAATESGEYNKVM--YI-TDGV 184
Cdd:PLN02822 175 YSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKRKKKLrrYIvVEAI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 185 FSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMGH-GHGTVKHFEMQ-DHIDFQMGTLSKGIGVVGGYVAGTKQLITW 262
Cdd:PLN02822 255 YQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKsGRGLSEHFGVPiEKIDIITAAMGHALATEGGFCTGSARVVDH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 263 LKSQARPFLFSTSLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELKRI-GYDIGKSetPITPVI----------- 330
Cdd:PLN02822 335 QRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIpGLSIGSN--TLSPIVflhlekstgsa 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1646957387 331 VGDEKLAQEFSKKLL-ENGVYVKPIVYPTV-----PLGtgrVRNMPNAGHTKEmldDAIKVYEKVGK 391
Cdd:PLN02822 413 KEDLSLLEHIADRMLkEDSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTES---DILKASESLKR 473
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
24-381 |
7.97e-52 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 178.25 E-value: 7.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 24 NTIDVLEGSNGPIITVNDKKMINLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGTLDIHQKLEEKIAEFKGTE 103
Cdd:PRK07505 28 NGLTVGEREGILITLADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSSRTRVRSQILKDLEEALSELFGAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 104 AaIAFQSGFNCNMGAI----SAVMKKGDAILS--DELNHASiidgcrLSGAK--------IIRVNHQDMEDLEAKAKaat 169
Cdd:PRK07505 108 V-LTFTSCSAAHLGILpllaSGHLTGGVPPHMvfDKNAHAS------LNILKgicadeteVETIDHNDLDALEDICK--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 170 esgEYNKVMYITDGVFSMdGDVAKIPEIVEICEKYNVITYVDDAHGTGVMG-HGHGTVKhfemqDHIDFQM-------GT 241
Cdd:PRK07505 178 ---TNKTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGkNGEGYVR-----SELDYRLnertiiaAS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 242 LSKGIGVVGGYVA-GTKQLITWLKSQARPFLFSTSLTPGAAGACIK--AIDLIEEHPEYVDTLWDNANYFKAElkrIGYD 318
Cdd:PRK07505 249 LGKAFGASGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILAsaEIHLSEELDQLQQKLQNNIALFDSL---IPTE 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1646957387 319 IGKSETPITPVIVGDEKLAQEFSKKLLENGVYVKPIVYPTVPLGTGRVRNMPNAGHTKEMLDD 381
Cdd:PRK07505 326 QSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKR 388
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
45-395 |
5.55e-40 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 146.69 E-value: 5.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 45 INLASNNYLGFATRPELIEADVEATKHYGAGA--GAVRTINGTLdiHQKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAV 122
Cdd:PRK07179 57 IILQSNDYLNLSGHPDIIKAQIAALQEEGDSLvmSAVFLHDDSP--KPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 123 MKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKaatesgEYNKVMYITDGVFSMDGDVAKIPEIVEICE 202
Cdd:PRK07179 135 ADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIE------RHGPGIIVVDSVYSTTGTIAPLADIVDIAE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 203 KYNVITYVDDAHGTGVMG-HGHGTVKHFEMQDHIDFQMGTLSKGIGVVGGYVAGTKQLITWLKSQARPFLFSTSLTPGAA 281
Cdd:PRK07179 209 EFGCVLVVDESHSLGTHGpQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 282 GACIKAIDLIEEHPEYVDTLWDNANYFKAELKRIGYDIGkSETPITPVIVGDEKLAQEFSKKLLENGVYVKPIVYPtvpl 361
Cdd:PRK07179 289 AGLEATLEVIESADDRRARLHANARFLREGLSELGYNIR-SESQIIALETGSERNTEVLRDALEERNVFGAVFCAP---- 363
|
330 340 350
....*....|....*....|....*....|....*...
gi 1646957387 362 GTGRVRNMP----NAGHTKEMLDDAIKVYEKVGKELGI 395
Cdd:PRK07179 364 ATPKNRNLIrlslNADLTASDLDRVLEVCREARDEVDL 401
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
45-388 |
6.16e-40 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 146.59 E-value: 6.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 45 INLASNNYLGFATRPELIEADVEATKHYGAGAGAVRTINGTLDIHQKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMK 124
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 125 KGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDL-------EAKAKAATESGEYNKVMYITDGVFSMDGDVAKIPEI 197
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvRAQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 198 VEICEKYNVITYVDDAHGTGVMGH-GHGTVKHFEMQ--DHIDFQMGTLSKGIGVVGGYVAGTKQLITWLKSQARPFLFST 274
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKsGRGSLEHAGLKpmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 275 SLTPGAAGACIKAIDLIEEHPEYVDTLWDNANYFKAELK----------RIGYDIGKSE-TPITPV----IVGDEKLAQ- 338
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTnsshpyalklRNRLVITSDPiSPIIYLrlsdQEATRRTDEt 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 339 ----EFSKKLLENGVYV------KPIVYPTVPLGTGRVrnMPNAGHTKEMLDDAIKVYEK 388
Cdd:PLN03227 321 lildQIAHHSLSEGVAVvstgghVKKFLQLVPPPCLRV--VANASHTREDIDKLLTVLGE 378
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
45-280 |
2.56e-21 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 94.46 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 45 INLASNNYLGFATRPELIEAdVEAT--------KHYGAGAGAVRTINGTLDIHQKLEEKIAEFKGTEAAIAFQSGFNCNM 116
Cdd:PRK05937 7 IDFVTNDFLGFSRSDTLVHE-VEKRyrlycrqfPHAQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 117 GAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKAATESGeYNKVMYITDGVFSMDGDVAKIPE 196
Cdd:PRK05937 86 GLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRS-FGRIFIFVCSVYSFKGTLAPLEQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 197 IVEICEKYNVITYVDDAHGTGVMGHGHGTVKHFEMQDHIDFQMGTLSKGIGVVGGYVAGTKQLITWLKSQARPFLFSTSL 276
Cdd:PRK05937 165 IIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGL 244
|
....
gi 1646957387 277 TPGA 280
Cdd:PRK05937 245 PPHL 248
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
45-384 |
8.53e-17 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 80.85 E-value: 8.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 45 INLASNNYLgFATRPELIEADVEA-----TKHYGAGAGavrtingtldiHQKLEEKIAEF-------KGTEAAIAFQSGf 112
Cdd:cd00609 1 IDLSIGEPD-FPPPPEVLEALAAAalragLLGYYPDPG-----------LPELREAIAEWlgrrggvDVPPEEIVVTNG- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 113 ncNMGAISAVM----KKGDAILSDELNHASIIDGCRLSGAKIIRV----NHQDMEDLEAKAKAATESgeyNKVMYI---- 180
Cdd:cd00609 68 --AQEALSLLLrallNPGDEVLVPDPTYPGYEAAARLAGAEVVPVpldeEGGFLLDLELLEAAKTPK---TKLLYLnnpn 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 181 --TDGVFSMDgdvaKIPEIVEICEKYNVITYVDDAHG---TGvmGHGHGTVKHFEMQDHIdFQMGTLSKGIGVVG---GY 252
Cdd:cd00609 143 npTGAVLSEE----ELEELAELAKKHGILIISDEAYAelvYD--GEPPPALALLDAYERV-IVLRSFSKTFGLPGlriGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 253 VAGTKQ-LITWLKSQARPFLFSTSLTpgAAGACIKAIDLIEEH-PEYVDTLWDNANYFKAELKRIGYDIgKSETPITPVI 330
Cdd:cd00609 216 LIAPPEeLLERLKKLLPYTTSGPSTL--SQAAAAAALDDGEEHlEELRERYRRRRDALLEALKELGPLV-VVKPSGGFFL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1646957387 331 ---VGDEKLAQEFSKKLLENGVYV-KPIVYPTVPLGTGRVrnmpNAGHTKEMLDDAIK 384
Cdd:cd00609 293 wldLPEGDDEEFLERLLLEAGVVVrPGSAFGEGGEGFVRL----SFATPEEELEEALE 346
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
89-257 |
1.42e-13 |
|
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).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 68.18 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 89 HQKLEEKIAEF--KGTEAAIAFQSGFNCNMGAISAVMKKGDAILSDELNHASII-DGCRLSGAKIIRV----------NH 155
Cdd:cd01494 2 LEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYwVAAELAGAKPVPVpvddagygglDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 156 QDMEDLEAKAkaatesgeyNKVMYITDGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMGHGhgtvKHFEMQDHI 235
Cdd:cd01494 82 AILEELKAKP---------NVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAP----GVLIPEGGA 148
|
170 180
....*....|....*....|..
gi 1646957387 236 DFQMGTLSKGIGVVGGYVAGTK 257
Cdd:cd01494 149 DVVTFSLHKNLGGEGGGVVIVK 170
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
80-255 |
1.85e-10 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 61.83 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 80 RTINGTLDIhqkLEEKIAEFKGTEAAIAFQSGfncnMGAISAVM----KKGDAILS-DELNHASIIDGCRLSGAKIIRVN 154
Cdd:cd00614 36 RIGNPTVDA---LEKKLAALEGGEAALAFSSG----MAAISTVLlallKAGDHVVAsDDLYGGTYRLFERLLPKLGIEVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 155 HQDMEDLEAKAKAATESGeynKVMYItDGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMGH--GHGtvkhfemq 232
Cdd:cd00614 109 FVDPDDPEALEAAIKPET---KLVYV-ESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYLQRplELG-------- 176
|
170 180
....*....|....*....|....*..
gi 1646957387 233 dhIDFQMGTLSKGIG----VVGGYVAG 255
Cdd:cd00614 177 --ADIVVHSATKYIGghsdVIAGVVVG 201
|
|
| PRK05968 |
PRK05968 |
hypothetical protein; Provisional |
80-271 |
6.27e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 168320 [Multi-domain] Cd Length: 389 Bit Score: 54.32 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 80 RTINGTLdihQKLEEKIAEFKGTEAAIAFQSGfncnMGAIS----AVMKKGDAILSdeLNHAsIIDGCRLSGAKIIR--- 152
Cdd:PRK05968 59 RGDNPTV---RAFEEMLAKLEGAEDARGFASG----MAAISstvlSFVEPGDRIVA--VRHV-YPDAFRLFETILKRmgv 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 153 -VNHQDMEDLEAKAKAATESgeynKVMYI---TDGVFSMDgDVAKIpeiVEICEKYNVITYVDDAHGTGV----MGHGhg 224
Cdd:PRK05968 129 eVDYVDGRDEEAVAKALPGA----KLLYLespTSWVFELQ-DVAAL---AALAKRHGVVTMIDNSWASPVfqrpITLG-- 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1646957387 225 tvkhfemqdhIDFQMGTLSKGIG----VVGGYVAGTKQLITWLKSQARPFL 271
Cdd:PRK05968 199 ----------VDLVIHSASKYLGghsdTVAGVVAGSKEHIARINAEAYPYL 239
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
90-268 |
2.35e-07 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 51.83 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 90 QKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMKKGDAILSDELNHaSIIDGCR----LSGAKIIRVNHQ-----DMED 160
Cdd:pfam01212 35 NRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAH-IHFDETGghaeLGGVQPRPLDGDeagnmDLED 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 161 LEAKAKAATESGEYN-KVMYITDGVFSMDGDV---AKIPEIVEICEKYNVITYVDDAH------GTGVmghghgTVKhfE 230
Cdd:pfam01212 114 LEAAIREVGADIFPPtGLISLENTHNSAGGQVvslENLREIAALAREHGIPVHLDGARfanaavALGV------IVK--E 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1646957387 231 MQDHID-FQMGtLSKGIGV-VGGYVAGTKQLITWLKSQAR 268
Cdd:pfam01212 186 ITSYADsVTMC-LSKGLGApVGSVLAGSDDFIAKAIRQRK 224
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
88-215 |
2.55e-07 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 51.87 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 88 IHQKLEEKIAEFKGTEAAIAFQSGFNC-NMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVN-----------H 155
Cdd:cd00615 60 PIKEAQELAARAFGAKHTFFLVNGTSSsNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKpernpyygiagG 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 156 QDMEDLeakaKAATESGEYNKVMYITDGVFsmDGDVAKIPEIVEICEKYNVITYVDDAHG 215
Cdd:cd00615 140 IPPETF----KKALIEHPDAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAHG 193
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
46-389 |
2.03e-05 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 46.17 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 46 NLASNNYLGfATrPELIEADVEATkhYGAGAgavrtiNGTLDIHQKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMKK 125
Cdd:cd06502 1 DFRSDTVTG-PT-PEMLEAMAAAN--VGDDV------YGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 126 GDAILSDELNHAsIIDGC----RLSGAKIIRVNHQD----MEDLEAKAKAatesgeYNKVMYITDGVFSMD-----GDVA 192
Cdd:cd06502 71 GGSVICHETAHI-YTDEAgapeFLSGVKLLPVPGENgkltPEDLEAAIRP------RDDIHFPPPSLVSLEnttegGTVY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 193 KIPEIVEICE---KYNVITYVDDAH--------GTGVMghghgtvkhfEMQDHIDFQMGTLSKGIGVVGG-YVAGTKQLI 260
Cdd:cd06502 144 PLDELKAISAlakENGLPLHLDGARlanaaaalGVALK----------TYKSGVDSVSFCLSKGGGAPVGaVVVGNRDFI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 261 ----TWLKSQARpfLFSTSLTPGAAGACikaidLIEEHPeYVDTLW---DNANYFKAELKRIGYDIGKSETPItpVIVGD 333
Cdd:cd06502 214 ararRRRKQAGG--GMRQSGFLAAAGLA-----ALENDL-WLRRLRhdhEMARRLAEALEELGGLESEVQTNI--VLLDP 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1646957387 334 EKLAQ---EFSKKLLEN---GVYVKPIvyptvplGTGRVRNMPNAGHTKEMLDDAIKVYEKV 389
Cdd:cd06502 284 VEANAvfvELSKEAIERrgeGVLFYAW-------GEGGVRFVTHWDTTEEDVDELLSALKAV 338
|
|
| PRK06234 |
PRK06234 |
methionine gamma-lyase; Provisional |
92-216 |
4.38e-04 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 168478 [Multi-domain] Cd Length: 400 Bit Score: 42.12 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 92 LEEKIAEFKGTEAAIAFQSGfncnMGAISA----VMKKGDAILSDE---------LNHasiidGCRLSGAKIIRVNHQDM 158
Cdd:PRK06234 69 VENKLALLEGGEAAVVAASG----MGAISSslwsALKAGDHVVASDtlygctfalLNH-----GLTRYGVEVTFVDTSNL 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1646957387 159 EDLEAKAKAATE----SGEYNKVMYITDgvfsmdgdvakIPEIVEICEKYN--VITYVDDAHGT 216
Cdd:PRK06234 140 EEVRNALKANTKvvylETPANPTLKVTD-----------IKAISNIAHENNkeCLVFVDNTFCT 192
|
|
| PRK08574 |
PRK08574 |
cystathionine gamma-synthase family protein; |
80-255 |
1.18e-03 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 236298 [Multi-domain] Cd Length: 385 Bit Score: 40.82 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 80 RTINGTLdihQKLEEKIAEFKGTEAAIAFQSGfncnMGAISAV----MKKGDAIL-SDELNHASI--IDGCRLSGAKIIR 152
Cdd:PRK08574 49 REENPTL---RPLEEALAKLEGGVDALAFNSG----MAAISTLffslLKAGDRVVlPMEAYGTTLrlLKSLEKFGVKVVL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 153 VnhqdMEDLEAKAKAATEsGEYNKVMY--ITDGVFSmdgdVAKIPEIVEICEKYNVITYVDDAHGTGVM----GHGHGTV 226
Cdd:PRK08574 122 A----YPSTEDIIEAIKE-GRTKLVFIetMTNPTLK----VIDVPEVAKAAKELGAILVVDNTFATPLLyrplRHGADFV 192
|
170 180 190
....*....|....*....|....*....|...
gi 1646957387 227 KHfemqdhidfqmgTLSKGIG----VVGGYVAG 255
Cdd:PRK08574 193 VH------------SLTKYIAghndVVGGVAVA 213
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
94-219 |
1.75e-03 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 40.07 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 94 EKIAEFKGTEAAIAFQSGFNCNMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVNHQDMEDLEAKAKAAT---- 169
Cdd:cd06452 51 HDLAEFLGMDEARVTPGAREGKFAVMHSLCEKGDWVVVDGLAHYTSYVAAERAGLNVREVPNTGHPEYHITPEGYAevie 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1646957387 170 ----ESGEYNKVMYIT--DGVFsmdGDVAKIPEIVEICEKYNVITYVDDAHGTGVM 219
Cdd:cd06452 131 evkdEFGKPPALALLThvDGNY---GNLHDAKKIAKVCHEYGVPLLLNGAYTVGRM 183
|
|
| PRK06434 |
PRK06434 |
cystathionine gamma-lyase; Validated |
90-131 |
1.91e-03 |
|
cystathionine gamma-lyase; Validated
Pssm-ID: 102374 [Multi-domain] Cd Length: 384 Bit Score: 40.27 E-value: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1646957387 90 QKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAVMKKGDAILS 131
Cdd:PRK06434 67 QAFEEKYAVLENAEHALSFSSGMGAITSAILSLIKKGKRILS 108
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
39-219 |
2.22e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 39.74 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 39 VNDKKMINLasnNYLGFATRPE-LIEA------DVEATKHYGAGAGAVRTingTLDIHQkLEEKIAEFKGTEAA--IAFQ 109
Cdd:COG0520 11 VLGKPLVYL---DNAATGQKPRpVIDAirdyyePYNANVHRGAHELSAEA---TDAYEA-AREKVARFIGAASPdeIIFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 110 SG--FNCNMGAIS-AVMKKGDAILSDELNHASIIDG----CRLSGAKIIRV-----NHQDMEDLEAKAKAATesgeynKV 177
Cdd:COG0520 84 RGttEAINLVAYGlGRLKPGDEILITEMEHHSNIVPwqelAERTGAEVRVIpldedGELDLEALEALLTPRT------KL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1646957387 178 MYITdGVFSMDGDVAKIPEIVEICEKYNVITYVDDAHGTGVM 219
Cdd:COG0520 158 VAVT-HVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHL 198
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
115-215 |
2.74e-03 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 39.79 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 115 NMGAISAVMKKGDAILSDELNHASIIDGCRLSGAKIIRVN--------------HQDMEDLEAKAKAATESGEYNKVMYI 180
Cdd:pfam01276 95 NKTVGMAVCTPGDTILIDRNCHKSIHHALMLSGATPVYLEpsrnaygiiggiplHEFQEETLKEAIAEVPDAKGPRLAVI 174
|
90 100 110
....*....|....*....|....*....|....*
gi 1646957387 181 TDGVFsmDGDVAKIPEIVEICEKYNVITYVDDAHG 215
Cdd:pfam01276 175 TNPTY--DGVLYNAKEIVDTLHHLSDPILFDSAWV 207
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
90-223 |
7.41e-03 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 38.03 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1646957387 90 QKLEEKIAEFKGTEAAIAFQSGFNCNMGAISAV-MKKGDAILSDELNHASIIDGCRLSGAKIIRVnhqDME------DLE 162
Cdd:pfam01041 27 REFERAFAAYLGVKHAIAVSSGTAALHLALRALgVGPGDEVITPSFTFVATANAALRLGAKPVFV---DIDpdtyniDPE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1646957387 163 AKAKAATESgeynkvmyiTDGVFS--MDGDVAKIPEIVEICEKYNVITYVDDAHGTGVMGHGH 223
Cdd:pfam01041 104 AIEAAITPR---------TKAIIPvhLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGK 157
|
|
| |
