|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-408 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 783.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 1 MLAKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELF 80
Cdd:PRK00011 5 NLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 81 GADHVNVQPHSGSQANMAVYQALLESGDKILGMNLTDGGHLTHGSPFNFSGQLYDFYSYGVADTNEQLDYASLAAKAQEV 160
Cdd:PRK00011 85 GAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLALEH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 161 HPKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTTTHKTLRGPRGGMILCK-AE 239
Cdd:PRK00011 165 KPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNdEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 240 YAKAIDSAIFPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANAQAMAAVFDQSDLvRVVSGGTDNHLMLLDLTNS 319
Cdd:PRK00011 245 LAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGF-RVVSGGTDNHLVLVDLRSK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 320 GLNGKELQNLLDSVHITVNKNTIPFEKLSPFKTSGIRIGTPAITSRGFKETDCEQIANLILEVIEKHDQLEAMTAISEAV 399
Cdd:PRK00011 324 GLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEEV 403
|
....*....
gi 510997418 400 LKLTDQFPI 408
Cdd:PRK00011 404 KELCKRFPL 412
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
2-408 |
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: 779.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 2 LAKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELFG 81
Cdd:COG0112 5 LAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 82 ADHVNVQPHSGSQANMAVYQALLESGDKILGMNLTDGGHLTHGSPFNFSGQLYDFYSYGVADTNEQLDYASLAAKAQEVH 161
Cdd:COG0112 85 AEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLALEHK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 162 PKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTTTHKTLRGPRGGMILCKAEYA 241
Cdd:COG0112 165 PKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNEELA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 242 KAIDSAIFPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANAQAMAAVFDQSDLvRVVSGGTDNHLMLLDLTNSGL 321
Cdd:COG0112 245 KKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGF-RVVSGGTDNHLVLVDLRSKGL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 322 NGKELQNLLDSVHITVNKNTIPFEKLSPFKTSGIRIGTPAITSRGFKETDCEQIANLILEVIEKHDQLEAMTAISEAVLK 401
Cdd:COG0112 324 TGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEVKE 403
|
....*..
gi 510997418 402 LTDQFPI 408
Cdd:COG0112 404 LCKRFPL 410
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
2-408 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 666.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 2 LAKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELFG 81
Cdd:PRK13034 9 LEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLFG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 82 ADHVNVQPHSGSQANMAVYQALLESGDKILGMNLTDGGHLTHGSPFNFSGQLYDFYSYGVADTNEQLDYASLAAKAQEVH 161
Cdd:PRK13034 89 CDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAKEHK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 162 PKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTTTHKTLRGPRGGMILCK-AEY 240
Cdd:PRK13034 169 PKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNdEEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 241 AKAIDSAIFPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANAQAMAAVFDQSDLvRVVSGGTDNHLMLLDLTNSG 320
Cdd:PRK13034 249 AKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGY-DLVSGGTDNHLLLVDLRPKG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 321 LNGKELQNLLDSVHITVNKNTIPFEKLSPFKTSGIRIGTPAITSRGFKETDCEQIANLILEVIEKHDQLEAMTAISEAVL 400
Cdd:PRK13034 328 LSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKEVK 407
|
....*...
gi 510997418 401 KLTDQFPI 408
Cdd:PRK13034 408 ALCSRFPI 415
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
3-402 |
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: 633.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 3 AKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELFGA 82
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 83 DHVNVQPHSGSQANMAVYQALLESGDKILGMNLTDGGHLTHGSPF--NFSGQLYDFYSYGVADTNEQLDYASLAAKAQEV 160
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFTkvSASGKLFESVPYGVDPETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 161 HPKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTTTHKTLRGPRGGMILC-KAE 239
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 240 YAKAIDSAIFPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANAQAMAAVFdQSDLVRVVSGGTDNHLMLLDLTNS 319
Cdd:cd00378 241 LAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEAL-KERGFKVVSGGTDNHLVLVDLRPK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 320 GLNGKELQNLLDSVHITVNKNTIPFEKLSPFKTSGIRIGTPAITSRGFKETDCEQIANLILEVIEKHDQLEAMTAISEAV 399
Cdd:cd00378 320 GITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEV 399
|
...
gi 510997418 400 LKL 402
Cdd:cd00378 400 AEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
2-379 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 595.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 2 LAKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELFG 81
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 82 AD----HVNVQPHSGSQANMAVYQALLESGDKILGMNLTDGGHLTHGSPFNF-----SGQLYDFYSYGVADTNEQLDYAS 152
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 153 LAAKAQEVHPKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTTTHKTLRGPRGG 232
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 233 MILCKA--------------EYAKAIDSAIFPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANAQAMAAVFDQSD 298
Cdd:pfam00464 241 MIFYRKgvksvdktgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 299 LvRVVSGGTDNHLMLLDLTNSGLNGKELQNLLDSVHITVNKNTIPFEKlSPFKTSGIRIGTPAITSRGFKETDCEQIANL 378
Cdd:pfam00464 321 Y-KLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDK-SAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398
|
.
gi 510997418 379 I 379
Cdd:pfam00464 399 I 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
2-408 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 519.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 2 LAKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELFG 81
Cdd:PTZ00094 15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 82 ADH----VNVQPHSGSQANMAVYQALLESGDKILGMNLTDGGHLTHGSPF-----NFSGQLYDFYSYGVaDTNEQLDYAS 152
Cdd:PTZ00094 95 LDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTakkkvSATSIYFESLPYQV-NEKGLIDYDK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 153 LAAKAQEVHPKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTTTHKTLRGPRGG 232
Cdd:PTZ00094 174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 233 MIL----CKAEYAKAIDSAIFPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANAQAMAAVFDQSDLvRVVSGGTD 308
Cdd:PTZ00094 254 LIFyrkkVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGY-DLVTGGTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 309 NHLMLLDLTNSGLNGKELQNLLDSVHITVNKNTIPFEKlSPFKTSGIRIGTPAITSRGFKETDCEQIANLILEVIEKHDQ 388
Cdd:PTZ00094 333 NHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDK-SALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVKLAQE 411
|
410 420 430
....*....|....*....|....*....|....*...
gi 510997418 389 L------------------EAMTAISEAVLKLTDQFPI 408
Cdd:PTZ00094 412 IqkqvgkklvdfkkaleknPELQKLRQEVVEFASQFPF 449
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
2-384 |
1.96e-177 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 504.19 E-value: 1.96e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 2 LAKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELFG 81
Cdd:PRK13580 30 ILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 82 ADHVNVQPHSGSQANMAVYQALL------------------------------ESGD-KILGMNLTDGGHLTHGSPFNFS 130
Cdd:PRK13580 110 AEHAYVQPHSGADANLVAFWAILahkvespaleklgaktvndlteedwealraELGNqRLLGMSLDSGGHLTHGFRPNIS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 131 GQLYDFYSYGVADTNEQLDYASLAAKAQEVHPKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGV--- 207
Cdd:PRK13580 190 GKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVftg 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 208 HPSPVPYADVVTTTTHKTLRGPRGGMILCKAEYAKAIDSAIfPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANA 287
Cdd:PRK13580 270 DEDPVPHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 288 QAMAAVFDQSDLvRVVSGGTDNHLMLLDLTNSGLNGKELQNLLDSVHITVNKNTIPFEKLSPFKTSGIRIGTPAITSRGF 367
Cdd:PRK13580 349 RALAEGFLKRGA-RLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGM 427
|
410
....*....|....*..
gi 510997418 368 KETDCEQIANLILEVIE 384
Cdd:PRK13580 428 GSDEMDEVAELIVKVLS 444
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
2-384 |
1.60e-172 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 491.03 E-value: 1.60e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 2 LAKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELFG 81
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 82 ADH----VNVQPHSGSQANMAVYQALLESGDKILGMNLTDGGHLTHGspfnfsgqlydFYSYG--VADT----------- 144
Cdd:PLN03226 95 LDPekwgVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHG-----------YQTDGkkISATsiyfesmpyrl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 145 NEQ---LDYASLAAKAQEVHPKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTT 221
Cdd:PLN03226 164 DEStglIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 222 THKTLRGPRGGMILCK--------------AEYAKAIDSAIFPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANA 287
Cdd:PLN03226 244 THKSLRGPRGGMIFFRkgpkppkgqgegavYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 288 QAMAavfdqSDLVR----VVSGGTDNHLMLLDLTNSGLNGKELQNLLDSVHITVNKNTIPFEKlSPFKTSGIRIGTPAIT 363
Cdd:PLN03226 324 AALA-----NRLMSkgykLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDS-SALVPGGVRIGTPAMT 397
|
410 420
....*....|....*....|.
gi 510997418 364 SRGFKETDCEQIANLILEVIE 384
Cdd:PLN03226 398 SRGLVEKDFEKVAEFLHRAVT 418
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
2-380 |
3.04e-125 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 374.53 E-value: 3.04e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 2 LAKTDPVINDLIKQEENRQRHNIELIASENIVSGAVQEAQGSVLTNKYAEGYPNKRFYGGCEYIDQIETLAIERAKELFG 81
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 82 ADH----VNVQPHSGSQANMAVYQALLESGDKILGMNLTDGGHLTHG----SPFNFSGQ--LYDFYSYGVADTNEQLDYA 151
Cdd:PLN02271 209 LDSekwgVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyytpGGKKVSGAsiFFESLPYKVNPQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 152 SLAAKAQEVHPKMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTTTHKTLRGPRG 231
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 232 GMILCKA--------------------EYAKAIDSAIFPGIQGGPLEHVIAAKAVAFGEALQPEFTAYTKQIVANAQAMA 291
Cdd:PLN02271 369 GIIFYRKgpklrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 292 AVFDQSDlVRVVSGGTDNHLMLLDLTNSGLNGKELQNLLDSVHITVNKNTIPFEK--LSPfktSGIRIGTPAITSRGFKE 369
Cdd:PLN02271 449 SALLRRK-CRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNgtISP---GGVRIGTPAMTSRGCLE 524
|
410
....*....|.
gi 510997418 370 TDCEQIANLIL 380
Cdd:PLN02271 525 SDFETIADFLL 535
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
69-234 |
6.54e-19 |
|
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: 83.59 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 69 ETLAIERAKELF--GADHVNVQPhSGSQANMAVYQALLESGDKILGMNLTDGGHLTHGSPFNFsgqlYDFYSYGVADTNE 146
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAG----AKPVPVPVDDAGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 147 QLDYASLAAKAQEV-HPKMIVAGASAYSRTI--DFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPYADVVTTTTH 223
Cdd:cd01494 77 GGLDVAILEELKAKpNVALIVITPNTTSGGVlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|.
gi 510997418 224 KTLRGPRGGMI 234
Cdd:cd01494 157 KNLGGEGGGVV 167
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
90-358 |
1.59e-07 |
|
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: 52.73 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 90 HSGSQANMAVYQALLESGDKILGMNLTDGGHLTHgspFNFSGqlYDFYSYGVADTNEQLDYASLAAKAQEVHPKMIV--- 166
Cdd:cd00609 66 NGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAG--AEVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYlnn 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 167 ----AGasaysRTIDFPRLREIAD---QVGAYLMIDMAHiAGLVATGVHPSPVPYAD-----VVTTTTHKTLRGP--RGG 232
Cdd:cd00609 141 pnnpTG-----AVLSEEELEELAElakKHGILIISDEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGLPglRIG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 233 MILCKAEYAKAIDSAIFPGIQGGPleHVIAAKAVAfgEALQP---EFTAYTKQIVANAQAMAAVFDQSDLVRVV--SGGt 307
Cdd:cd00609 215 YLIAPPEELLERLKKLLPYTTSGP--STLSQAAAA--AALDDgeeHLEELRERYRRRRDALLEALKELGPLVVVkpSGG- 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 510997418 308 dNHLmLLDLTNsGLNGKELQNLLDSVHITVNKNTIPFEKLSPFktsgIRIG 358
Cdd:cd00609 290 -FFL-WLDLPE-GDDEEFLERLLLEAGVVVRPGSAFGEGGEGF----VRLS 333
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
58-343 |
3.23e-07 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 51.92 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 58 FYGGCEYIDQIETLAIERAKELFGADH---VNVQPHSGSQANM-AVYQALLESGDKILGMNLTdggHLTHGSPFNFSGQL 133
Cdd:pfam00155 34 LYGPTDGHPELREALAKFLGRSPVLKLdreAAVVFGSGAGANIeALIFLLANPGDAILVPAPT---YASYIRIARLAGGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 134 YDFYSYGVADtNEQLDYASLAAKAQEvHPKMIVAgASAYSRT-IDFPR-----LREIADQVGAYLMIDMAHIAGLVATGV 207
Cdd:pfam00155 111 VVRYPLYDSN-DFHLDFDALEAALKE-KPKVVLH-TSPHNPTgTVATLeelekLLDLAKEHNILLLVDEAYAGFVFGSPD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 208 HPSPVPYAD-----VVTTTTHKT--LRGPRGGMILCKAEYAKAIDSAIFPGIQGGPLEHvIAAKAVAFGEALQPEFTAYT 280
Cdd:pfam00155 188 AVATRALLAegpnlLVVGSFSKAfgLAGWRVGYILGNAAVISQLRKLARPFYSSTHLQA-AAAAALSDPLLVASELEEMR 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510997418 281 KQIVANAQAMAAVFDQSDLVRVVSGGTDNHLMLLDltnsGLNGKEL-QNLLDSVHITVNKNTIP 343
Cdd:pfam00155 267 QRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLD----PETAKELaQVLLEEVGVYVTPGSSP 326
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
90-244 |
1.91e-05 |
|
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: 46.40 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 90 HSGSQANMAVYQALLESGDKILG-----MNLTDGGHLthgspfnfSGQlyDFYSYgvadtnEQLDYASLAAKAQEVH--- 161
Cdd:cd06454 68 SSGYAANDGVLSTLAGKGDLIISdslnhASIIDGIRL--------SGA--KKRIF------KHNDMEDLEKLLREARrpy 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 162 -PKMIVAgASAYSRTIDFPRLREI---ADQVGAYLMIDMAHIAGLVatGVHPSPVPYA-------DVVTTTTHKTLrGPR 230
Cdd:cd06454 132 gKKLIVT-EGVYSMDGDIAPLPELvdlAKKYGAILFVDEAHSVGVY--GPHGRGVEEFggltddvDIIMGTLGKAF-GAV 207
|
170
....*....|....
gi 510997418 231 GGMILCKAEYAKAI 244
Cdd:cd06454 208 GGYIAGSKELIDYL 221
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
72-226 |
2.62e-05 |
|
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: 45.70 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 72 AIERAKELFGADHVNVQPHSGSQANMAVYQALLESGDKIL-GMNltdgghlTHGSPFN---FSGQL-------YDFYsYG 140
Cdd:cd00615 64 AQELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILiDRN-------CHKSVINglvLSGAVpvylkpeRNPY-YG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 141 VAD--TNEQLDYASLAAKaqevHPKMIVAGASAYSRTI-DFPRLREIADQVGAYLMIDMAHIAGLVATGVHPSPVPY--A 215
Cdd:cd00615 136 IAGgiPPETFKKALIEHP----DAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSSAAMagA 211
|
170
....*....|.
gi 510997418 216 DVVTTTTHKTL 226
Cdd:cd00615 212 DIVVQSTHKTL 222
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
74-317 |
2.94e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 42.20 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 74 ERAKELFGADHVnVQPHSGSQANMAVYQALLESGDKILgmnLTDGGHL---THGSPFNFSG-QLYDFYSygvaDTNEQLD 149
Cdd:pfam01212 39 DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVI---CGEPAHIhfdETGGHAELGGvQPRPLDG----DEAGNMD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 150 YASLAAKAQEVH------PKMIV-------AGASAYSrtIDFPR-LREIADQVGAYLMIDMAHIA-GLVATGVHPSPV-P 213
Cdd:pfam01212 111 LEDLEAAIREVGadifppTGLISlenthnsAGGQVVS--LENLReIAALAREHGIPVHLDGARFAnAAVALGVIVKEItS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 214 YADVVTTTTHKTLRGPRGGMILCKAEYakaIDSAI-FPGIQGGPLEH--VIAAKAVAfgeALQpEFTAYTKQIVANAQAM 290
Cdd:pfam01212 189 YADSVTMCLSKGLGAPVGSVLAGSDDF---IAKAIrQRKYLGGGLRQagVLAAAGLR---ALE-EGVARLARDHATARRL 261
|
250 260
....*....|....*....|....*..
gi 510997418 291 AAVFDQSDLVRVVSGGTDNHLMLLDLT 317
Cdd:pfam01212 262 AEGLELLRLAIPRRVYTNTHMVYVAAA 288
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
74-226 |
8.29e-04 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 41.64 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 74 ERAKELFGADH----VNvqphsG-SQANMAVYQALLESGDKIL-----------GMNLTDgghlthGSP----------F 127
Cdd:COG1982 73 ELAAEAFGADRtfflVN-----GtSSGNKAMILAVCGPGDKVLvprnchksvihGLILSG------AIPvylnpeidneL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 128 NFSGqlydfysyGVadTNEQLDYASLA---AKAqevhpkMIVAGASAYSRTIDFPRLREIADQVGAYLMIDMAHIAGLva 204
Cdd:COG1982 142 GIIG--------GI--TPEAVEEALIEhpdAKA------VLITNPTYYGVCYDLKAIAELAHEHGIPVLVDEAHGAHF-- 203
|
170 180
....*....|....*....|....*...
gi 510997418 205 tGVHPsPVPY------ADVVTTTTHKTL 226
Cdd:COG1982 204 -GFHP-DLPRsameagADLVVQSTHKTL 229
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
91-195 |
6.66e-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: 38.34 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997418 91 SGSQANMAVYQALLESGDKIL-GMNLtdgghltHGSPFNFSGQLydFYSYGV-ADTNEQLDYASLAAKAQEvHPKMIVAG 168
Cdd:cd00614 63 SGMAAISTVLLALLKAGDHVVaSDDL-------YGGTYRLFERL--LPKLGIeVTFVDPDDPEALEAAIKP-ETKLVYVE 132
|
90 100
....*....|....*....|....*....
gi 510997418 169 --ASAYSRTIDFPRLREIADQVGAYLMID 195
Cdd:cd00614 133 spTNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| |
