|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
4-423 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 707.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:PRK00011 9 YDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGAEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 ANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSPVNFSGRLYEAHFYGVQEDTGRLDYDNILKIAQEVKPQM 163
Cdd:PRK00011 89 ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLALEHKPKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 164 LIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLILMgedfdnpf 243
Cdd:PRK00011 169 IIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILT-------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 244 gltlkngNPQKMSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAKGYHLISGGTDN 323
Cdd:PRK00011 241 -------NDEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 324 HMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFDDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDFIDRVIQNPDNE 403
Cdd:PRK00011 314 HLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDE 393
|
410 420
....*....|....*....|
gi 2474876906 404 AELQAVAQEVHSLMEGRPLF 423
Cdd:PRK00011 394 AVIEEVKEEVKELCKRFPLY 413
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
4-423 |
0e+00 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 700.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:COG0112 8 VDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELFGAEH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 ANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSPVNFSGRLYEAHFYGVQEDTGRLDYDNILKIAQEVKPQM 163
Cdd:COG0112 88 ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLALEHKPKL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 164 LIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLILMGEDFdnpf 243
Cdd:COG0112 168 IIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNEEL---- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 244 gltlkngnpqkmSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAKGYHLISGGTDN 323
Cdd:COG0112 244 ------------AKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 324 HMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFDDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDFIDRVIQNPDNE 403
Cdd:COG0112 312 HLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDE 391
|
410 420
....*....|....*....|
gi 2474876906 404 AELQAVAQEVHSLMEGRPLF 423
Cdd:COG0112 392 AVLAEVREEVKELCKRFPLY 411
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
4-416 |
0e+00 |
|
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.
Pssm-ID: 99733 Cd Length: 402 Bit Score: 576.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:cd00378 3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 ANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSP--VNFSGRLYEAHFYGVQEDTGRLDYDNILKIAQEVKP 161
Cdd:cd00378 83 ANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 162 QMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLILMGEDfdn 241
Cdd:cd00378 163 KLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKG--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 242 pfgltlkngnpqKMSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAKGYHLISGGT 321
Cdd:cd00378 240 ------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 322 DNHMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFDDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDFIDRVIQNPD 401
Cdd:cd00378 308 DNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAE 387
|
410
....*....|....*
gi 2474876906 402 NEAELQAVAQEVHSL 416
Cdd:cd00378 388 DVAVAEEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
4-393 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 538.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGA-- 81
Cdd:pfam00464 4 SDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLdp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 82 --AYANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSPVNF-----SGRLYEAHFYGVQEDTGRLDYDNILK 154
Cdd:pfam00464 84 akWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQLEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 155 IAQEVKPQMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLIL 234
Cdd:pfam00464 164 NAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 235 mgedFDNPFGLTLKNGN--PQKMSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAK 312
Cdd:pfam00464 244 ----YRKGVKSVDKTGKeiLYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 313 GYHLISGGTDNHMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFdDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDF 392
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPG-DKSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398
|
.
gi 2474876906 393 I 393
Cdd:pfam00464 399 I 399
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
4-423 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 707.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:PRK00011 9 YDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGAEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 ANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSPVNFSGRLYEAHFYGVQEDTGRLDYDNILKIAQEVKPQM 163
Cdd:PRK00011 89 ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLALEHKPKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 164 LIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLILMgedfdnpf 243
Cdd:PRK00011 169 IIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILT-------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 244 gltlkngNPQKMSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAKGYHLISGGTDN 323
Cdd:PRK00011 241 -------NDEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 324 HMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFDDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDFIDRVIQNPDNE 403
Cdd:PRK00011 314 HLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDE 393
|
410 420
....*....|....*....|
gi 2474876906 404 AELQAVAQEVHSLMEGRPLF 423
Cdd:PRK00011 394 AVIEEVKEEVKELCKRFPLY 413
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
4-423 |
0e+00 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 700.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:COG0112 8 VDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELFGAEH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 ANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSPVNFSGRLYEAHFYGVQEDTGRLDYDNILKIAQEVKPQM 163
Cdd:COG0112 88 ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLALEHKPKL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 164 LIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLILMGEDFdnpf 243
Cdd:COG0112 168 IIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNEEL---- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 244 gltlkngnpqkmSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAKGYHLISGGTDN 323
Cdd:COG0112 244 ------------AKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 324 HMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFDDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDFIDRVIQNPDNE 403
Cdd:COG0112 312 HLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDE 391
|
410 420
....*....|....*....|
gi 2474876906 404 AELQAVAQEVHSLMEGRPLF 423
Cdd:COG0112 392 AVLAEVREEVKELCKRFPLY 411
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
4-423 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 621.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:PRK13034 12 YDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLFGCDY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 ANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSPVNFSGRLYEAHFYGVQEDTGRLDYDNILKIAQEVKPQM 163
Cdd:PRK13034 92 ANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAKEHKPKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 164 LIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLILMgedfdnpf 243
Cdd:PRK13034 172 IIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILT-------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 244 gltlkngNPQKMSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAKGYHLISGGTDN 323
Cdd:PRK13034 244 -------NDEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 324 HMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFDDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDFIDRVIQNPDNE 403
Cdd:PRK13034 317 HLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNA 396
|
410 420
....*....|....*....|
gi 2474876906 404 AELQAVAQEVHSLMEGRPLF 423
Cdd:PRK13034 397 ALEQRVRKEVKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
4-416 |
0e+00 |
|
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.
Pssm-ID: 99733 Cd Length: 402 Bit Score: 576.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:cd00378 3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 ANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSP--VNFSGRLYEAHFYGVQEDTGRLDYDNILKIAQEVKP 161
Cdd:cd00378 83 ANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 162 QMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLILMGEDfdn 241
Cdd:cd00378 163 KLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKG--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 242 pfgltlkngnpqKMSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAKGYHLISGGT 321
Cdd:cd00378 240 ------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 322 DNHMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFDDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDFIDRVIQNPD 401
Cdd:cd00378 308 DNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAE 387
|
410
....*....|....*
gi 2474876906 402 NEAELQAVAQEVHSL 416
Cdd:cd00378 388 DVAVAEEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
4-393 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 538.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGA-- 81
Cdd:pfam00464 4 SDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLdp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 82 --AYANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSPVNF-----SGRLYEAHFYGVQEDTGRLDYDNILK 154
Cdd:pfam00464 84 akWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQLEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 155 IAQEVKPQMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLIL 234
Cdd:pfam00464 164 NAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 235 mgedFDNPFGLTLKNGN--PQKMSHLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAK 312
Cdd:pfam00464 244 ----YRKGVKSVDKTGKeiLYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 313 GYHLISGGTDNHMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFdDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDF 392
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPG-DKSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398
|
.
gi 2474876906 393 I 393
Cdd:pfam00464 399 I 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
4-398 |
1.76e-165 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 472.55 E-value: 1.76e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:PTZ00094 18 ADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFGLDP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 ----ANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHG-----SPVNFSGRLYEAHFYGVQEDtGRLDYDNILK 154
Cdd:PTZ00094 98 eewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEK-GLIDYDKLEE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 155 IAQEVKPQMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLIl 234
Cdd:PTZ00094 177 LAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSGLI- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 235 mgedFDNpfgltlKNGNPQKMShLLNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVAKGY 314
Cdd:PTZ00094 256 ----FYR------KKVKPDIEN-KINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 315 HLISGGTDNHMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFdDKSPFVTSGIRVGAAAITTRGLKEAEMATIVDFID 394
Cdd:PTZ00094 325 DLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPG-DKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLD 403
|
....
gi 2474876906 395 RVIQ 398
Cdd:PTZ00094 404 RAVK 407
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
4-398 |
1.30e-156 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 450.97 E-value: 1.30e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 4 QDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAY 83
Cdd:PLN03226 18 VDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFRLDP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 84 A----NVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHG-----SPVNFSGRLYEAHFYGVQEDTGRLDYDNILK 154
Cdd:PLN03226 98 EkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgKKISATSIYFESMPYRLDESTGLIDYDKLEK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 155 IAQEVKPQMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRGGLIL 234
Cdd:PLN03226 178 KAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMIF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 235 MGEDFDNPfgltlKNGNPQKMSHL---LNMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYMEQVRKNAQAMAAAFVA 311
Cdd:PLN03226 258 FRKGPKPP-----KGQGEGAVYDYedkINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 312 KGYHLISGGTDNHMMLIDLRNKNITGKDAEKALVSAEITANKNMVPfDDKSPFVTSGIRVGAAAITTRGLKEAEMATIVD 391
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVP-GDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAE 411
|
....*..
gi 2474876906 392 FIDRVIQ 398
Cdd:PLN03226 412 FLHRAVT 418
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
8-423 |
3.25e-139 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 407.12 E-value: 3.25e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 8 VFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFGAAYANVQ 87
Cdd:PRK13580 37 IAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 88 PHSGSQANTAVFHAFL------------------------------KPGD-KILGFDLSHGGHLTHGSPVNFSGRLYEAH 136
Cdd:PRK13580 117 PHSGADANLVAFWAILahkvespaleklgaktvndlteedwealraELGNqRLLGMSLDSGGHLTHGFRPNISGKMFHQR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 137 FYGVQEDTGRLDYDNILKIAQEVKPQMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLS---NPIPH 213
Cdd:PRK13580 197 SYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTgdeDPVPH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 214 CHVVTTTTHKTLRGPRGGLILMGEDFDNpfglTLKNGNPQKMshllnmavfpgnqGGPLMHVIAGKAVAFQEALDPSFKS 293
Cdd:PRK13580 277 ADIVTTTTHKTLRGPRGGLVLAKKEYAD----AVDKGCPLVL-------------GGPLPHVMAAKAVALAEARTPEFQK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 294 YMEQVRKNAQAMAAAFVAKGYHLISGGTDNHMMLIDLRNKNITGKDAEKALVSAEITANKNMVPFDDKSPFVTSGIRVGA 373
Cdd:PRK13580 340 YAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGT 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2474876906 374 AAITTRGLKEAEMATIVDFIDRVIQN-----------PDNEAEL-QAVAQEVHS----LMEGRPLF 423
Cdd:PRK13580 420 PALTTLGMGSDEMDEVAELIVKVLSNttpgttaegapSKAKYELdEGVAQEVRArvaeLLARFPLY 485
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
1-422 |
3.16e-113 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 343.71 E-value: 3.16e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 1 MTLQDTAVFDLIKEEEQRQLNGIELIASENFTSPAVMEATGSVLTNKYAEGYPGKRYYGGCEVVDEVERIAIERAKELFG 80
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 81 AAYA----NVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHG--SP----VNFSGRLYEAHFYGVQEDTGRLDYD 150
Cdd:PLN02271 209 LDSEkwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyyTPggkkVSGASIFFESLPYKVNPQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 151 NILKIAQEVKPQMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLRGPRG 230
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 231 GLILMgedfdnpfgltLKNGNPQKMSHLL---------------NMAVFPGNQGGPLMHVIAGKAVAFQEALDPSFKSYM 295
Cdd:PLN02271 369 GIIFY-----------RKGPKLRKQGMLLshgddnshydfeekiNFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYM 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 296 EQVRKNAQAMAAAFVAKGYHLISGGTDNHMMLIDLRNKNITGKDAEKALVSAEITANKNMVpFDDKSPFVTSGIRVGAAA 375
Cdd:PLN02271 438 QQVKKNAQALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPA 516
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2474876906 376 ITTRGLKEAEMATIVDFIDRViqnpdneAELQAVAQEVHSLMEGRPL 422
Cdd:PLN02271 517 MTSRGCLESDFETIADFLLRA-------AQIASAVQREHGKLQKEFL 556
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
71-235 |
2.87e-09 |
|
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: 55.85 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 71 AIERAKELFGA-AYANVQPHSGSQANTAVFHAFLKPGDKILGFDLSHGGHLTHGSPVNFsgrlYEAHFYGVQEDTGRLDY 149
Cdd:cd01494 5 LEEKLARLLQPgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAG----AKPVPVPVDDAGYGGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 150 DNIL---KIAQEVKPQMLIAGASAYSRDIDFAKFREIADAVGAFLLADISHPSGMIATGMLSNPIPHCHVVTTTTHKTLR 226
Cdd:cd01494 81 VAILeelKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLG 160
|
....*....
gi 2474876906 227 GPRGGLILM 235
Cdd:cd01494 161 GEGGGVVIV 169
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
31-197 |
9.22e-04 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 41.14 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 31 FTSPAVMEATgsvltNKYAEGYPGKRYyGGCEVVDEVEriaiERAKELFGAAY-------ANVQPHSGSQAN-TAVFHAF 102
Cdd:pfam00155 14 DTLPAVAKAE-----KDALAGGTRNLY-GPTDGHPELR----EALAKFLGRSPvlkldreAAVVFGSGAGANiEALIFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 103 LKPGDKILGFDLSHGGHLT----HGSPVnfsgrlYEAHFYgvQEDTGRLDYDNIL-KIAQEVKpQMLIAGAS-----AYS 172
Cdd:pfam00155 84 ANPGDAILVPAPTYASYIRiarlAGGEV------VRYPLY--DSNDFHLDFDALEaALKEKPK-VVLHTSPHnptgtVAT 154
|
170 180
....*....|....*....|....*
gi 2474876906 173 RDiDFAKFREIADAVGAFLLADISH 197
Cdd:pfam00155 155 LE-ELEKLLDLAKEHNILLLVDEAY 178
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
64-213 |
9.29e-03 |
|
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: 37.95 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474876906 64 VDEVERI--AIERAKelFGAAYAnvqphSGSQANTAVFHAFLKPGDKILGFDLSHGGhlTHgspvNFSGRLyeAHFYGVQ 141
Cdd:cd00614 42 VDALEKKlaALEGGE--AALAFS-----SGMAAISTVLLALLKAGDHVVASDDLYGG--TY----RLFERL--LPKLGIE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2474876906 142 ED-TGRLDYDNILKIAQEvKPQMLIAG--ASAYSRDIDFAKFREIADAVGAFLLADishpsGMIATGMLSNPIPH 213
Cdd:cd00614 107 VTfVDPDDPEALEAAIKP-ETKLVYVEspTNPTLKVVDIEAIAELAHEHGALLVVD-----NTFATPYLQRPLEL 175
|
|
|