|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-405 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 837.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 1 MKYLPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQ 80
Cdd:PRK00011 3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 81 LFGAEHANVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHGSPVNFSGVQYNFVAYGVDPETHVIDYDDVREKAR 160
Cdd:PRK00011 83 LFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 161 LHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRGGMILC-Q 239
Cdd:PRK00011 163 EHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTnD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 240 EQFAKQIDKAIFPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEGFTLVSGGTDNHLLLVDLRP 319
Cdd:PRK00011 243 EELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 320 QQLTGKTAEKVLDEVGITVNKNTIPYDPESPFVTSGIRIGTAAVTTRGFGLEEMDEIAAIIGLVLKNVGSEQALEEARQR 399
Cdd:PRK00011 323 KGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEE 402
|
....*.
2W7D_A 400 VAALTD 405
Cdd:PRK00011 403 VKELCK 408
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
1-405 |
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: 829.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 1 MKYLPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQ 80
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 81 LFGAEHANVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHGSPVNFSGVQYNFVAYGVDPETHVIDYDDVREKAR 160
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 161 LHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRGGMILCQE 240
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 241 QFAKQIDKAIFPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEGFTLVSGGTDNHLLLVDLRPQ 320
Cdd:COG0112 242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 321 QLTGKTAEKVLDEVGITVNKNTIPYDPESPFVTSGIRIGTAAVTTRGFGLEEMDEIAAIIGLVLKNVGSEQALEEARQRV 400
Cdd:COG0112 322 GLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEV 401
|
....*
2W7D_A 401 AALTD 405
Cdd:COG0112 402 KELCK 406
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
4-405 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 714.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 4 LPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQLFG 83
Cdd:PRK13034 9 LEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLFG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 84 AEHANVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHGSPVNFSGVQYNFVAYGVDPETHVIDYDDVREKARLHR 163
Cdd:PRK13034 89 CDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAKEHK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 164 PKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRGGMILCQ-EQF 242
Cdd:PRK13034 169 PKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNdEEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 243 AKQIDKAIFPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEGFTLVSGGTDNHLLLVDLRPQQL 322
Cdd:PRK13034 249 AKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRPKGL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 323 TGKTAEKVLDEVGITVNKNTIPYDPESPFVTSGIRIGTAAVTTRGFGLEEMDEIAAIIGLVLKNVGSEQALEEARQRVAA 402
Cdd:PRK13034 329 SGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKEVKA 408
|
...
2W7D_A 403 LTD 405
Cdd:PRK13034 409 LCS 411
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
5-403 |
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: 700.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 5 PQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQLFGA 84
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 85 EHANVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHGSP--VNFSGVQYNFVAYGVDPETHVIDYDDVREKARLH 162
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 163 RPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRGGMILCQ-EQ 241
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRkGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 242 FAKQIDKAIFPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEGFTLVSGGTDNHLLLVDLRPQQ 321
Cdd:cd00378 241 LAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 322 LTGKTAEKVLDEVGITVNKNTIPYDPESPFVTSGIRIGTAAVTTRGFGLEEMDEIAAIIGLVLKNVGSEQALEEARQRVA 401
Cdd:cd00378 321 ITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVA 400
|
..
2W7D_A 402 AL 403
Cdd:cd00378 401 EL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
4-380 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 652.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 4 LPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQLFG 83
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 84 AE----HANVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHGSPVNF-----SGVQYNFVAYGVDPETHVIDYDD 154
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 155 VREKARLHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRGG 234
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 235 MILCQ--------------EQFAKQIDKAIFPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEG 300
Cdd:pfam00464 241 MIFYRkgvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 301 FTLVSGGTDNHLLLVDLRPQQLTGKTAEKVLDEVGITVNKNTIPYDpESPFVTSGIRIGTAAVTTRGFGLEEMDEIAAII 380
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
4-385 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 539.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 4 LPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQLFG 83
Cdd:PTZ00094 15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 84 AEH----ANVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHG-----SPVNFSGVQYNFVAYGVDPEThVIDYDD 154
Cdd:PTZ00094 95 LDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKG-LIDYDK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 155 VREKARLHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRGG 234
Cdd:PTZ00094 174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 235 MIL----CQEQFAKQIDKAIFPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEGFTLVSGGTDN 310
Cdd:PTZ00094 254 LIFyrkkVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDN 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2W7D_A 311 HLLLVDLRPQQLTGKTAEKVLDEVGITVNKNTIPYDpESPFVTSGIRIGTAAVTTRGFGLEEMDEIAAIIGLVLK 385
Cdd:PTZ00094 334 HLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGD-KSALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVK 407
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
9-405 |
0e+00 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 535.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 9 PQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQLFGAEHAN 88
Cdd:PRK13580 35 PRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 89 VQPHSGAQANMAVYFTVLEH------------------------------GDTV-LGMNLSHGGHLTHGSPVNFSGVQYN 137
Cdd:PRK13580 115 VQPHSGADANLVAFWAILAHkvespaleklgaktvndlteedwealraelGNQRlLGMSLDSGGHLTHGFRPNISGKMFH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 138 FVAYGVDPETHVIDYDDVREKARLHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGL---HPNPV 214
Cdd:PRK13580 195 QRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVftgDEDPV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 215 PYAHFVTTTTHKTLRGPRGGMILCQEQFAKQIDKAIfPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLAS 294
Cdd:PRK13580 275 PHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 295 ALQNEGFTLVSGGTDNHLLLVDLRPQQLTGKTAEKVLDEVGITVNKNTIPYDPESPFVTSGIRIGTAAVTTRGFGLEEMD 374
Cdd:PRK13580 354 GFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMD 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
2W7D_A 375 EIAAIIGLVLKN----------------VGSEQALEEARQRVAALTD 405
Cdd:PRK13580 434 EVAELIVKVLSNttpgttaegapskakyELDEGVAQEVRARVAELLA 480
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
4-377 |
1.57e-174 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 495.66 E-value: 1.57e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 4 LPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQLFG 83
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 84 AEHA----NVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHG---SPVNFSGVQYNF--VAYGVDPETHVIDYDD 154
Cdd:PLN03226 95 LDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtDGKKISATSIYFesMPYRLDESTGLIDYDK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 155 VREKARLHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRGG 234
Cdd:PLN03226 175 LEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 235 MIL----------CQEQ----FAKQIDKAIFPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEG 300
Cdd:PLN03226 255 MIFfrkgpkppkgQGEGavydYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKG 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2W7D_A 301 FTLVSGGTDNHLLLVDLRPQQLTGKTAEKVLDEVGITVNKNTIPYDpESPFVTSGIRIGTAAVTTRGFGLEEMDEIA 377
Cdd:PLN03226 335 YKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDFEKVA 410
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
4-377 |
2.37e-127 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 379.53 E-value: 2.37e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 4 LPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNKFAEGYPGRRYYGGCEYVDIVEELARERAKQLFG 83
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 84 AEHA----NVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHG----SPVNFSGVQYNF--VAYGVDPETHVIDYD 153
Cdd:PLN02271 209 LDSEkwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyytpGGKKVSGASIFFesLPYKVNPQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 154 DVREKARLHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRG 233
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 234 GMIL--------------------CQEQFAKQIDKAIFPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLA 293
Cdd:PLN02271 369 GIIFyrkgpklrkqgmllshgddnSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 294 SALQNEGFTLVSGGTDNHLLLVDLRPQQLTGKTAEKVLDEVGITVNKNTIpYDPESPFVTSGIRIGTAAVTTRGFGLEEM 373
Cdd:PLN02271 449 SALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSRGCLESDF 527
|
....
2W7D_A 374 DEIA 377
Cdd:PLN02271 528 ETIA 531
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
71-236 |
6.15e-24 |
|
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: 97.45 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 71 EELARERAKQLF--GAEHANVQPhSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHGspVNFSGVQYNFVAYGVDPETH 148
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVA--AELAGAKPVPVPVDDAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 149 vIDYDDVREKARLHRPKLIVAAASAYPR--IIDFAKFREIADEVGAYLMVDMAHIAGLVAAGLHPNPVPYAHFVTTTTHK 226
Cdd:cd01494 79 -LDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHK 157
|
170
....*....|
2W7D_A 227 TLRGPRGGMI 236
Cdd:cd01494 158 NLGGEGGGVV 167
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
75-380 |
7.01e-17 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 81.20 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 75 RERAKQLFGAEH-------ANVQPHSGAQANMAVYFTVL-EHGDTVLGMNLSHGGHLTHgspVNFSGVQYNFVAYgVDPE 146
Cdd:pfam00155 45 REALAKFLGRSPvlkldreAAVVFGSGAGANIEALIFLLaNPGDAILVPAPTYASYIRI---ARLAGGEVVRYPL-YDSN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 147 THVIDYDDVrEKARLHRPKLIVAA------ASAYPRIiDFAKFREIADEVGAYLMVDMAHIAG----LVAAGLHPNPVPY 216
Cdd:pfam00155 121 DFHLDFDAL-EAALKEKPKVVLHTsphnptGTVATLE-ELEKLLDLAKEHNILLLVDEAYAGFvfgsPDAVATRALLAEG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 217 AH-FVTTTTHKT--LRGPRGGMILCQEQFAKQIDKAIFPGIQGGPLMHvIAAKAVAFGEALQDDFKAYAKRVVDNAKRLA 293
Cdd:pfam00155 199 PNlLVVGSFSKAfgLAGWRVGYILGNAAVISQLRKLARPFYSSTHLQA-AAAAALSDPLLVASELEEMRQRIKERRDYLR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 294 SALQNEGFTLVSGGTdNHLLLVDLRPqQLTGKTAEKVLDEVGITVNKNTIPYDPESpfvtsgIRIGTAAVTTrgfglEEM 373
Cdd:pfam00155 278 DGLQAAGLSVLPSQA-GFFLLTGLDP-ETAKELAQVLLEEVGVYVTPGSSPGVPGW------LRITVAGGTE-----EEL 344
|
....*..
2W7D_A 374 DEIAAII 380
Cdd:pfam00155 345 EELLEAI 351
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
93-381 |
6.98e-11 |
|
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: 63.13 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 93 SGA-QANMAVYFTVLEHGDTVLGMNLSHGGHLTHgspvnFSGVQYNFVAYGVDPETHVIDYDDVREKARLHRPKLIVAAA 171
Cdd:cd00609 66 NGAqEALSLLLRALLNPGDEVLVPDPTYPGYEAA-----ARLAGAEVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYLNN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 172 SAYP--RIIDFAKFREIAD---EVGAYLMVDMAHiAGLVAAGLHPNPVPYAH-----FVTTTTHKTLRGP--RGGMILCQ 239
Cdd:cd00609 141 PNNPtgAVLSEEELEELAElakKHGILIISDEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGLPglRIGYLIAP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 240 EQFAKQIDKAIFPGIQGGPLMHVIAAKAVAFGEAlQDDFKAYAKRVVDNAKRLASALQNEGFTLVSGGTDNHLLLVDLrP 319
Cdd:cd00609 220 PEELLERLKKLLPYTTSGPSTLSQAAAAAALDDG-EEHLEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDL-P 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
2W7D_A 320 QQLTGKTAEKVLDEVGITVNKNTIPYDPESPFvtsgIRIGTAAVTtrgfglEEMDEIAAIIG 381
Cdd:cd00609 298 EGDDEEFLERLLLEAGVVVRPGSAFGEGGEGF----VRLSFATPE------EELEEALERLA 349
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
74-228 |
8.36e-08 |
|
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: 53.41 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 74 ARERAKQLFGAEHANVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHlTHGspVNFSGVQYNFVAYGVDPETHV---I 150
Cdd:cd00615 64 AQELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSV-ING--LVLSGAVPVYLKPERNPYYGIaggI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 151 DYDDVREK-ARLHRPKLIVAAASAYPRII-DFAKFREIADEVGAYLMVDMAHIAglvAAGLHPN-PVPY----AHFVTTT 223
Cdd:cd00615 141 PPETFKKAlIEHPDAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGA---HFRFHPIlPSSAamagADIVVQS 217
|
....*
2W7D_A 224 THKTL 228
Cdd:cd00615 218 THKTL 222
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
61-383 |
5.15e-07 |
|
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: 51.18 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 61 YGGCEYVDIVEELARErakqLFGAEHANVQPhSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHGSPVNFSGVQynfvA 140
Cdd:cd06502 28 YGEDPTTAKLEARAAE----LFGKEAALFVP-SGTAANQLALAAHTQPGGSVICHETAHIYTDEAGAPEFLSGVK----L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 141 YGVDPETHVIDYDDVREKARLH------RPKLIV-----AAASAYPrIIDFAKFREIADEVGAYLMVDMAHIAGLVAAGl 209
Cdd:cd06502 99 LPVPGENGKLTPEDLEAAIRPRddihfpPPSLVSlenttEGGTVYP-LDELKAISALAKENGLPLHLDGARLANAAAAL- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 210 hpnPVP------YAHFVTTTTHKTLRGPRGGMILCQEQFAKQID---KAIFPGI-QGGplmhVIAAKAVAfgeALQDDF- 278
Cdd:cd06502 177 ---GVAlktyksGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARrrrKQAGGGMrQSG----FLAAAGLA---ALENDLw 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 279 KAYAKRVVDNAKRLASALQNEGfTLVSGGTDNHLLLVDLRPQQLTGKTAEKVLDEVGITVNKNTIPYDpespfvtsGIRI 358
Cdd:cd06502 247 LRRLRHDHEMARRLAEALEELG-GLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEG--------GVRF 317
|
330 340
....*....|....*....|....*
2W7D_A 359 GTAAVTTRgfglEEMDEIAAIIGLV 383
Cdd:cd06502 318 VTHWDTTE----EDVDELLSALKAV 338
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
151-305 |
1.03e-06 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 50.39 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 151 DYDDVREKARLHRPKLIVAAaSAYPRIIDFAKFR---EIADEVGAYLMVDMAHI--------AGLVAA-GLhpnpVPYAH 218
Cdd:PRK07179 169 DVDHLRRQIERHGPGIIVVD-SVYSTTGTIAPLAdivDIAEEFGCVLVVDESHSlgthgpqgAGLVAElGL----TSRVH 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 219 FVTTTTHKTLRGpRGGMILCQEQFAKQIDKAIFPGIQGGPLM-HVIA--AKAVAFGEAlQDDFKAyakRVVDNAKRLASA 295
Cdd:PRK07179 244 FITASLAKAFAG-RAGIITCPRELAEYVPFVSYPAIFSSTLLpHEIAglEATLEVIES-ADDRRA---RLHANARFLREG 318
|
170
....*....|
2W7D_A 296 LQNEGFTLVS 305
Cdd:PRK07179 319 LSELGYNIRS 328
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
71-308 |
2.99e-04 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 42.45 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 71 EELARERAkQLFGAEHA---NvqphSGAQANMAVYFTVLEHGDTVLGMNLSH-----GGHLthgSPVNFSGVQYNfvayg 142
Cdd:PRK05958 87 EALEEELA-EWFGAERAllfS----SGYAANLAVLTALAGKGDLIVSDKLNHaslidGARL---SRARVRRYPHN----- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 143 vdpethviDYDDVRE--KARLHRPKLIVAAA--SAYPRIIDFAKFREIADEVGAYLMVDMAHI--------AGLVA-AGL 209
Cdd:PRK05958 154 --------DVDALEAllAKWRAGRALIVTESvfSMDGDLAPLAELVALARRHGAWLLVDEAHGtgvlgpqgRGLAAeAGL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 210 --HPNPVpyahfVTTTTHKTLrGPRGGMILCQEQFAKQ-IDKA---IF----PgiqggPLMhviaakAVAFGEALQ--DD 277
Cdd:PRK05958 226 agEPDVI-----LVGTLGKAL-GSSGAAVLGSETLIDYlINRArpfIFttalP-----PAQ------AAAARAALRilRR 288
|
250 260 270
....*....|....*....|....*....|.
2W7D_A 278 FKAYAKRVVDNAKRLASALQNEGFTLVSGGT 308
Cdd:PRK05958 289 EPERRERLAALIARLRAGLRALGFQLMDSQS 319
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
68-240 |
4.25e-04 |
|
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: 42.16 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 68 DIVEELARERAKqLFGAEHANVQpHSGAQANMAVYFTVLEHGDTVLGMNLSH-----GGHLTHGSPVNFsgvQYNfvayg 142
Cdd:cd06454 46 DLHEELEEELAE-FHGKEAALVF-SSGYAANDGVLSTLAGKGDLIISDSLNHasiidGIRLSGAKKRIF---KHN----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 143 vdpethviDYDDVREKAR----LHRPKLIVAAaSAYPRIIDFAKFREI---ADEVGAYLMVDMAH--------IAGLVAA 207
Cdd:cd06454 116 --------DMEDLEKLLRearrPYGKKLIVTE-GVYSMDGDIAPLPELvdlAKKYGAILFVDEAHsvgvygphGRGVEEF 186
|
170 180 190
....*....|....*....|....*....|...
2W7D_A 208 GLHPNPVPyahFVTTTTHKTLrGPRGGMILCQE 240
Cdd:cd06454 187 GGLTDDVD---IIMGTLGKAF-GAVGGYIAGSK 215
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
76-317 |
5.31e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 41.43 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 76 ERAKQLFGAEHAnVQPHSGAQANMAVYFTVLEHGDTVLGMNLSHGGHLTHGSPVNFSGVQYNFVaygVDPETHVIDYDDV 155
Cdd:pfam01212 39 DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGGHAELGGVQPRPL---DGDEAGNMDLEDL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 156 REKARLH------RPKLI---VAAASAYPRII---DFAKFREIADEVGAYLMVDMAHIA-GLVAAGLHPNPV-PYAHFVT 221
Cdd:pfam01212 115 EAAIREVgadifpPTGLIsleNTHNSAGGQVVsleNLREIAALAREHGIPVHLDGARFAnAAVALGVIVKEItSYADSVT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 222 TTTHKTLRGPRGGMILCQEQFakqIDKAI-FPGIQGGPL--MHVIAAKAVAfgeALQDDfKAYAKRVVDNAKRLASALQN 298
Cdd:pfam01212 195 MCLSKGLGAPVGSVLAGSDDF---IAKAIrQRKYLGGGLrqAGVLAAAGLR---ALEEG-VARLARDHATARRLAEGLEL 267
|
250 260
....*....|....*....|
2W7D_A 299 EGFTLVSG-GTDNHLLLVDL 317
Cdd:pfam01212 268 LRLAIPRRvYTNTHMVYVAA 287
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
67-197 |
9.03e-04 |
|
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: 41.03 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W7D_A 67 VDIVEE-LARerakqLFGAEHANVQPhSGAQANMAVYFTVLEHGDTVL-GMNLSHGGH--LTHGSPvnFSGVQYNFVayg 142
Cdd:cd00614 42 VDALEKkLAA-----LEGGEAALAFS-SGMAAISTVLLALLKAGDHVVaSDDLYGGTYrlFERLLP--KLGIEVTFV--- 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
2W7D_A 143 vDPEthviDYDDVREKARlHRPKLIVAAASAYP--RIIDFAKFREIADEVGAYLMVD 197
Cdd:cd00614 111 -DPD----DPEALEAAIK-PETKLVYVESPTNPtlKVVDIEAIAELAHEHGALLVVD 161
|
|
| |
