|
Name |
Accession |
Description |
Interval |
E-value |
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
1-413 |
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: 821.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 1 MEQLRKNDPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKE 80
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 81 LFGAEHVNVQPHSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHGSPVNASGLLYNFVAYGVQEDTFLIDYDEVRKAAF 160
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 161 KHRPRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGGMILCRK 240
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 241 AWAAAIDKAVFPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLIAEGLNIVSGGTDNHLMLIDTRSV 320
Cdd:COG0112 242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 321 NITGKEAEHVLDSIGITVNKNAIPFDPTSPFVTSGIRIGTPAATSRGMNEEAMVAIGKIIAKTLKNPKDTAKLDEARAEV 400
Cdd:COG0112 322 GLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEV 401
|
410
....*....|...
gi 516288621 401 TALTDQFPLYTDL 413
Cdd:COG0112 402 KELCKRFPLYPDL 414
|
|
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-413 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 820.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 1 MEQLRKNDPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKE 80
Cdd:PRK00011 3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 81 LFGAEHVNVQPHSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHGSPVNASGLLYNFVAYGVQEDTFLIDYDEVRKAAF 160
Cdd:PRK00011 83 LFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 161 KHRPRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGGMILCR- 239
Cdd:PRK00011 163 EHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 240 KAWAAAIDKAVFPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLIAEGLNIVSGGTDNHLMLIDTRS 319
Cdd:PRK00011 243 EELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 320 VNITGKEAEHVLDSIGITVNKNAIPFDPTSPFVTSGIRIGTPAATSRGMNEEAMVAIGKIIAKTLKNPKDTAKLDEARAE 399
Cdd:PRK00011 323 KGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEE 402
|
410
....*....|....
gi 516288621 400 VTALTDQFPLYTDL 413
Cdd:PRK00011 403 VKELCKRFPLYKYL 416
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
1-410 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 697.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 1 MEQLRKNDPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKE 80
Cdd:PRK13034 6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 81 LFGAEHVNVQPHSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHGSPVNASGLLYNFVAYGVQEDTFLIDYDEVRKAAF 160
Cdd:PRK13034 86 LFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 161 KHRPRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGGMILCRK 240
Cdd:PRK13034 166 EHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTND 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 241 A-WAAAIDKAVFPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLIAEGLNIVSGGTDNHLMLIDTRS 319
Cdd:PRK13034 246 EeIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 320 VNITGKEAEHVLDSIGITVNKNAIPFDPTSPFVTSGIRIGTPAATSRGMNEEAMVAIGKIIAKTLKNPKDTAKLDEARAE 399
Cdd:PRK13034 326 KGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKE 405
|
410
....*....|.
gi 516288621 400 VTALTDQFPLY 410
Cdd:PRK13034 406 VKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
6-403 |
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: 655.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 6 KNDPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKELFGAE 85
Cdd:cd00378 2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 86 HVNVQPHSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHGSP--VNASGLLYNFVAYGVQEDTFLIDYDEVRKAAFKHR 163
Cdd:cd00378 82 YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 164 PRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGGMILCRKA-W 242
Cdd:cd00378 162 PKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGeL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 243 AAAIDKAVFPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLIAEGLNIVSGGTDNHLMLIDTRSVNI 322
Cdd:cd00378 242 AKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 323 TGKEAEHVLDSIGITVNKNAIPFDPTSPFVTSGIRIGTPAATSRGMNEEAMVAIGKIIAKTLKNPKDTAKLDEARAEVTA 402
Cdd:cd00378 322 TGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAE 401
|
.
gi 516288621 403 L 403
Cdd:cd00378 402 L 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
4-380 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 602.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 4 LRKNDPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKELFG 83
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 84 AE----HVNVQPHSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHGSPVN-----ASGLLYNFVAYGVQEDTFLIDYDE 154
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNskkisASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 155 VRKAAFKHRPRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGG 234
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 235 MILCRKAWAAA--------------IDKAVFPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLIAEG 300
Cdd:pfam00464 241 MIFYRKGVKSVdktgkeilyelekkINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 301 LNIVSGGTDNHLMLIDTRSVNITGKEAEHVLDSIGITVNKNAIPFDpTSPFVTSGIRIGTPAATSRGMNEEAMVAIGKII 380
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
4-409 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 523.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 4 LRKNDPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKELFG 83
Cdd:PTZ00094 15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 84 AEH----VNVQPHSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHG-----SPVNASGLLYNFVAYGVQEDTfLIDYDE 154
Cdd:PTZ00094 95 LDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKG-LIDYDK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 155 VRKAAFKHRPRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGG 234
Cdd:PTZ00094 174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 235 MILCRK----AWAAAIDKAVFPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLIAEGLNIVSGGTDN 310
Cdd:PTZ00094 254 LIFYRKkvkpDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 311 HLMLIDTRSVNITGKEAEHVLDSIGITVNKNAIPFDpTSPFVTSGIRIGTPAATSRGMNEEAMVAIGKIIAKTL------ 384
Cdd:PTZ00094 334 HLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGD-KSALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVklaqei 412
|
410 420 430
....*....|....*....|....*....|....*..
gi 516288621 385 ------------KNPKDTAKLDEARAEVTALTDQFPL 409
Cdd:PTZ00094 413 qkqvgkklvdfkKALEKNPELQKLRQEVVEFASQFPF 449
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
1-413 |
0e+00 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 514.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 1 MEQLRKNDPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKE 80
Cdd:PRK13580 27 LDVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 81 LFGAEHVNVQPHSGAQANMAVYLAAL------------------------------KPGDTV-LGMNLAHGGHLTHGSPV 129
Cdd:PRK13580 107 LFGAEHAYVQPHSGADANLVAFWAILahkvespaleklgaktvndlteedwealraELGNQRlLGMSLDSGGHLTHGFRP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 130 NASGLLYNFVAYGVQEDTFLIDYDEVRKAAFKHRPRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGL 209
Cdd:PRK13580 187 NISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 210 ---HPNPVPHAHFVTTTTHKTLRGPRGGMILCRKAWAAAIDKAVfPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVV 286
Cdd:PRK13580 267 ftgDEDPVPHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 287 KNAQVLAETLIAEGLNIVSGGTDNHLMLIDTRSVNITGKEAEHVLDSIGITVNKNAIPFDPTSPFVTSGIRIGTPAATSR 366
Cdd:PRK13580 346 DNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTL 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516288621 367 GMNEEAMVAIGKIIAKTLKN--PKDTAK--------------LDEARAEVTALTDQFPLYTDL 413
Cdd:PRK13580 426 GMGSDEMDEVAELIVKVLSNttPGTTAEgapskakyeldegvAQEVRARVAELLARFPLYPEI 488
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
8-408 |
1.10e-166 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 476.01 E-value: 1.10e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 8 DPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKELFGAEH- 86
Cdd:PLN03226 19 DPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFRLDPe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 87 ---VNVQPHSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHG-----SPVNASGLLYNFVAYGVQEDTFLIDYDEVRKA 158
Cdd:PLN03226 99 kwgVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgKKISATSIYFESMPYRLDESTGLIDYDKLEKK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 159 AFKHRPRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGGMILC 238
Cdd:PLN03226 179 AMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMIFF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 239 RKA--------------WAAAIDKAVFPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLIAEGLNIV 304
Cdd:PLN03226 259 RKGpkppkgqgegavydYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKGYKLV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 305 SGGTDNHLMLIDTRSVNITGKEAEHVLDSIGITVNKNAIPFDpTSPFVTSGIRIGTPAATSRGMNEEAMVAIGKII---- 380
Cdd:PLN03226 339 TGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFLhrav 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 516288621 381 -----------------AKTLKNPKDTAKLDEARAEVTALTDQFP 408
Cdd:PLN03226 418 tialkiqkehgkklkdfKKGLESNDFSKDIEALRAEVEEFATSFP 462
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
8-407 |
3.22e-119 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 358.73 E-value: 3.22e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 8 DPAVLEAMNLELKRQQNNIELIASENIVSEAVIEAMGSVLTNKYAEGYPGKRYYGGCEHVDIVEDIARDRAKELFGAEH- 86
Cdd:PLN02271 133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSe 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 87 ---VNVQPHSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHG--SP----VNASGLLYNFVAYGVQEDTFLIDYDEVRK 157
Cdd:PLN02271 213 kwgVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyyTPggkkVSGASIFFESLPYKVNPQTGYIDYDKLEE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 158 AAFKHRPRLIVAGASAYPRTIDFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLRGPRGGMIL 237
Cdd:PLN02271 293 KALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIF 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 238 CRKA--------------------WAAAIDKAVFPGSQGGPLMHVIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLI 297
Cdd:PLN02271 373 YRKGpklrkqgmllshgddnshydFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 298 AEGLNIVSGGTDNHLMLIDTRSVNITGKEAEHVLDSIGITVNKNAIpFDPTSPFVTSGIRIGTPAATSRGMNEE------ 371
Cdd:PLN02271 453 RRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSRGCLESdfetia 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 516288621 372 ------AMVA---------IGKIIAKTLKNPKDTAKLdeaRAEVTALTDQF 407
Cdd:PLN02271 532 dfllraAQIAsavqrehgkLQKEFLKGLQNNKDIVEL---RNRVEAFASQF 579
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
74-236 |
9.05e-22 |
|
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: 91.29 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 74 ARDRAKELF--GAEHVNVQPhSGAQANMAVYLAALKPGDTVLGMNLAHGGHLTHGspVNASGLLYNFVAYGVQEDtFLID 151
Cdd:cd01494 5 LEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVA--AELAGAKPVPVPVDDAGY-GGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 152 YDEVRKAAFKHRPRLIVAGASAYPRTI--DFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNPVPHAHFVTTTTHKTLR 229
Cdd:cd01494 81 VAILEELKAKPNVALIVITPNTTSGGVlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLG 160
|
....*..
gi 516288621 230 GPRGGMI 236
Cdd:cd01494 161 GEGGGVV 167
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
35-376 |
1.19e-10 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 62.32 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 35 VSEAVIEAMGSVLTNKYAEGYPGkrYYGgceHVDIVEDIArdrakELFGAEHV-------NVQPHSGAQANMAVYLAALK 107
Cdd:pfam00155 15 TLPAVAKAEKDALAGGTRNLYGP--TDG---HPELREALA-----KFLGRSPVlkldreaAVVFGSGAGANIEALIFLLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 108 -PGDTVLGMNLAHGGHLTHgspVNASGLLYNFVAYgVQEDTFLIDYDEVrKAAFKHRPRLIVAG------ASAYPRTiDF 180
Cdd:pfam00155 85 nPGDAILVPAPTYASYIRI---ARLAGGEVVRYPL-YDSNDFHLDFDAL-EAALKEKPKVVLHTsphnptGTVATLE-EL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 181 EKLASIANDVGALFMVDMAHIAG----LVAAGLHPNPVPHAH-FVTTTTHKT--LRGPRGGMILCRKAWAAAIDKAVFPG 253
Cdd:pfam00155 159 EKLLDLAKEHNILLLVDEAYAGFvfgsPDAVATRALLAEGPNlLVVGSFSKAfgLAGWRVGYILGNAAVISQLRKLARPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 254 ---SQGGPlmhvIASKAVAFGEALQPSFKTYAQNVVKNAQVLAETLIAEGLNIVSGGTdNHLMLIDTRSVniTGKEAEHV 330
Cdd:pfam00155 239 yssTHLQA----AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQA-GFFLLTGLDPE--TAKELAQV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 516288621 331 L-DSIGITVnknaipFDPTSPFVTSGIRIgTPAATSRGMNEEAMVAI 376
Cdd:pfam00155 312 LlEEVGVYV------TPGSSPGVPGWLRI-TVAGGTEEELEELLEAI 351
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
93-378 |
8.30e-08 |
|
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: 53.88 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 93 SGA-QANMAVYLAALKPGDTVLGMNLAHGGHLTHgspVNASGLlyNFVAYGVQEDTFLIDYDEVRKAAFKHRPRLIV--- 168
Cdd:cd00609 66 NGAqEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAGA--EVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYlnn 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 169 ----AGAsAYPRTiDFEKLASIANDVGALFMVDMAHiAGLVAAGLHPNPVPHAH-----FVTTTTHKTLRGP--RGGMIL 237
Cdd:cd00609 141 pnnpTGA-VLSEE-ELEELAELAKKHGILIISDEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGLPglRIGYLI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 238 CRKAWAAAIDKAVFPGSQGGP--LMHVIASKAVAFGEALqpsFKTYAQNVVKNAQVLAETLIAEGLNIVSGGTDNHLMLI 315
Cdd:cd00609 218 APPEELLERLKKLLPYTTSGPstLSQAAAAAALDDGEEH---LEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWL 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516288621 316 DTrSVNITGKEAEHVLDSIGITVNKNAIPFDPTSPFvtsgIRIGtpAATSRGMNEEAMVAIGK 378
Cdd:cd00609 295 DL-PEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGF----VRLS--FATPEEELEEALERLAE 350
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
37-246 |
1.18e-06 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 50.14 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 37 EAVIEAMGSVLTNKYAEGYPGKrYYGGCEHVDIVEDiARDRAKELFGAEHvnvqPH-----SGAQA--NMAVY-LAALKP 108
Cdd:COG0520 29 RPVIDAIRDYYEPYNANVHRGA-HELSAEATDAYEA-AREKVARFIGAAS----PDeiiftRGTTEaiNLVAYgLGRLKP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 109 GDTVLGmnlahgGHLTHGSpvnasgllyNFVA-------YGVQ------EDTFLIDYDEVRKAaFKHRPRLI-VAGASAY 174
Cdd:COG0520 103 GDEILI------TEMEHHS---------NIVPwqelaerTGAEvrviplDEDGELDLEALEAL-LTPRTKLVaVTHVSNV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516288621 175 PRTI-DFEKLASIANDVGALFMVDMAHIAGLVAAGLHPNpvpHAHFVTTTTHKtLRGPRG-GMILCRKAWAAAI 246
Cdd:COG0520 167 TGTVnPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQAL---GCDFYAFSGHK-LYGPTGiGVLYGKRELLEAL 236
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
74-228 |
2.99e-05 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 45.87 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 74 ARDRAKELFGAEH----VNvqphsGA-QANMAVYLAALKPGDTVL-GMN----LAHGGHLTHGSPV-------NASGLLY 136
Cdd:COG1982 71 AQELAAEAFGADRtfflVN-----GTsSGNKAMILAVCGPGDKVLvPRNchksVIHGLILSGAIPVylnpeidNELGIIG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 137 NfvaygvqedtflIDYDEVRKAAFKH-RPRLIVA------GASAyprtiDFEKLASIANDVGALFMVDMAHIAGLvaaGL 209
Cdd:COG1982 146 G------------ITPEAVEEALIEHpDAKAVLItnptyyGVCY-----DLKAIAELAHEHGIPVLVDEAHGAHF---GF 205
|
170 180
....*....|....*....|....*
gi 516288621 210 HPnPVPH------AHFVTTTTHKTL 228
Cdd:COG1982 206 HP-DLPRsameagADLVVQSTHKTL 229
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
74-228 |
1.24e-03 |
|
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: 40.31 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 74 ARDRAKELFGAEH--VNVQPHSGAqaNMAVYLAALKPGDTVLGM-----NLAHGGHLTHGSPV------NAsgllYNFVA 140
Cdd:cd00615 64 AQELAARAFGAKHtfFLVNGTSSS--NKAVILAVCGPGDKILIDrnchkSVINGLVLSGAVPVylkperNP----YYGIA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 141 YGVQEDTFlidyDEVRKAAfkHRPRLIVAGASAYPRTI-DFEKLASIANDVGALFMVDMAHIAglvAAGLHPNPVPH--- 216
Cdd:cd00615 138 GGIPPETF----KKALIEH--PDAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGA---HFRFHPILPSSaam 208
|
170
....*....|....
gi 516288621 217 --AHFVTTTTHKTL 228
Cdd:cd00615 209 agADIVVQSTHKTL 222
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
93-197 |
2.20e-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: 39.88 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 93 SGAQANMAVYLAALKPGDTVLGMNLAHGGhlthgspvnasglLYNFVA-----YGVQEDTFLIDYDEVRKAAFKHRPRLI 167
Cdd:cd00614 63 SGMAAISTVLLALLKAGDHVVASDDLYGG-------------TYRLFErllpkLGIEVTFVDPDDPEALEAAIKPETKLV 129
|
90 100 110
....*....|....*....|....*....|..
gi 516288621 168 VAGASAYP--RTIDFEKLASIANDVGALFMVD 197
Cdd:cd00614 130 YVESPTNPtlKVVDIEAIAELAHEHGALLVVD 161
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
73-230 |
5.96e-03 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 38.64 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 73 IARDRAKELFGAEHVNVQPHSGAQANMAVYLAALKPGDTVL-----GMNLAHGGHLTHGSPV------NASGLLYNFVAY 141
Cdd:pfam01276 70 EAQKYAARVFGADKSYFVVNGTSGSNKTVGMAVCTPGDTILidrncHKSIHHALMLSGATPVylepsrNAYGIIGGIPLH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516288621 142 GVQEDTFlidYDEVRKAAFKHRPRLIVAGASAYPRTI-DFEKLASIANDVGALFMVDMAHIAglvAAGLHPNPVPH---- 216
Cdd:pfam01276 150 EFQEETL---KEAIAEVPDAKGPRLAVITNPTYDGVLyNAKEIVDTLHHLSDPILFDSAWVG---YEQFIPIYADAspmg 223
|
170 180
....*....|....*....|.
gi 516288621 217 -------AHFVTTTTHKTLRG 230
Cdd:pfam01276 224 genengpGIFVTQSVHKLLAA 244
|
|
| |
