|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
5-427 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 683.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 5 NDMTLAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAK 84
Cdd:PRK00011 2 FMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 85 QVFGGDYVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLNFSGKNYRAVAYEVDRETMRIEPEKVREAA 164
Cdd:PRK00011 82 ELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 165 LAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSGMILsS 244
Cdd:PRK00011 162 LEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLIL-T 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 245 RGEQWGKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgaddaKNAGIKLVTGGTDVHL 324
Cdd:PRK00011 241 NDEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEAL-----AERGFRVVSGGTDNHL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 325 VLVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAVTSGLRIGTPALATRGFDAEDFAEVADIIGTTLSqgASGGN 404
Cdd:PRK00011 316 VLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLD--NPDDE 393
|
410 420
....*....|....*....|...
gi 881057965 405 VEVDALRARVKKLTDKHPLYAGL 427
Cdd:PRK00011 394 AVIEEVKEEVKELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
6-427 |
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: 672.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 6 DMTLAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQ 85
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 86 VFGGDYVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLNFSGKNYRAVAYEVDRETMRIEPEKVREAAL 165
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 166 AEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSGMILSsr 245
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILC-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 246 GEQWGKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgaddaKNAGIKLVTGGTDVHLV 325
Cdd:COG0112 240 NEELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEAL-----AERGFRVVSGGTDNHLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 326 LVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAVTSGLRIGTPALATRGFDAEDFAEVADIIGTTLSQGASGGNV 405
Cdd:COG0112 315 LVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVL 394
|
410 420
....*....|....*....|..
gi 881057965 406 EvdALRARVKKLTDKHPLYAGL 427
Cdd:COG0112 395 A--EVREEVKELCKRFPLYPDL 414
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
10-417 |
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: 553.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 10 AQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQVFGG 89
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 90 DYVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMR--LNFSGKNYRAVAYEVDRETMRIEPEKVREAALAE 167
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 168 HPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSGMILSSRGE 247
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 248 QWgKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgaddaKNAGIKLVTGGTDVHLVLV 327
Cdd:cd00378 241 LA-KKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEAL-----KERGFKVVSGGTDNHLVLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 328 DLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAVTSGLRIGTPALATRGFDAEDFAEVADIIGTTLSQGASGGnvEV 407
Cdd:cd00378 315 DLRPKGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVA--VA 392
|
410
....*....|
gi 881057965 408 DALRARVKKL 417
Cdd:cd00378 393 EEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
9-392 |
1.55e-179 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 506.21 E-value: 1.55e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 9 LAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQVFG 88
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 89 GD----YVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLNF-----SGKNYRAVAYEVDRETMRIEPEK 159
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 160 VREAALAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSG 239
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 240 MILSSRG------------EQWGKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgadd 307
Cdd:pfam00464 241 MIFYRKGvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEAL---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 308 aKNAGIKLVTGGTDVHLVLVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDpRPPAVTSGLRIGTPALATRGFDAEDFAE 387
Cdd:pfam00464 317 -TERGYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEK 394
|
....*
gi 881057965 388 VADII 392
Cdd:pfam00464 395 VAGFI 399
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
5-427 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 683.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 5 NDMTLAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAK 84
Cdd:PRK00011 2 FMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 85 QVFGGDYVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLNFSGKNYRAVAYEVDRETMRIEPEKVREAA 164
Cdd:PRK00011 82 ELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 165 LAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSGMILsS 244
Cdd:PRK00011 162 LEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLIL-T 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 245 RGEQWGKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgaddaKNAGIKLVTGGTDVHL 324
Cdd:PRK00011 241 NDEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEAL-----AERGFRVVSGGTDNHL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 325 VLVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAVTSGLRIGTPALATRGFDAEDFAEVADIIGTTLSqgASGGN 404
Cdd:PRK00011 316 VLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLD--NPDDE 393
|
410 420
....*....|....*....|...
gi 881057965 405 VEVDALRARVKKLTDKHPLYAGL 427
Cdd:PRK00011 394 AVIEEVKEEVKELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
6-427 |
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: 672.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 6 DMTLAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQ 85
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 86 VFGGDYVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLNFSGKNYRAVAYEVDRETMRIEPEKVREAAL 165
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 166 AEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSGMILSsr 245
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILC-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 246 GEQWGKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgaddaKNAGIKLVTGGTDVHLV 325
Cdd:COG0112 240 NEELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEAL-----AERGFRVVSGGTDNHLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 326 LVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAVTSGLRIGTPALATRGFDAEDFAEVADIIGTTLSQGASGGNV 405
Cdd:COG0112 315 LVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVL 394
|
410 420
....*....|....*....|..
gi 881057965 406 EvdALRARVKKLTDKHPLYAGL 427
Cdd:COG0112 395 A--EVREEVKELCKRFPLYPDL 414
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
1-424 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 586.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 1 MDSLNDMTLAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAI 80
Cdd:PRK13034 1 LMFFFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 81 ERAKQVFGGDYVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLNFSGKNYRAVAYEVDRETMRIEPEKV 160
Cdd:PRK13034 81 ERAKQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 161 REAALAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSGM 240
Cdd:PRK13034 161 EELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 241 ILsSRGEQWGKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgaddaKNAGIKLVTGGT 320
Cdd:PRK13034 241 IL-TNDEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVL-----KERGYDLVSGGT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 321 DVHLVLVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAVTSGLRIGTPALATRGFDAEDFAEVADIIGTTLSqga 400
Cdd:PRK13034 315 DNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLD--- 391
|
410 420
....*....|....*....|....*
gi 881057965 401 SGGNVEVDA-LRARVKKLTDKHPLY 424
Cdd:PRK13034 392 DLGNAALEQrVRKEVKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
10-417 |
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: 553.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 10 AQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQVFGG 89
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 90 DYVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMR--LNFSGKNYRAVAYEVDRETMRIEPEKVREAALAE 167
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 168 HPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSGMILSSRGE 247
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 248 QWgKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgaddaKNAGIKLVTGGTDVHLVLV 327
Cdd:cd00378 241 LA-KKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEAL-----KERGFKVVSGGTDNHLVLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 328 DLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAVTSGLRIGTPALATRGFDAEDFAEVADIIGTTLSQGASGGnvEV 407
Cdd:cd00378 315 DLRPKGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVA--VA 392
|
410
....*....|
gi 881057965 408 DALRARVKKL 417
Cdd:cd00378 393 EEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
9-392 |
1.55e-179 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 506.21 E-value: 1.55e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 9 LAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQVFG 88
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 89 GD----YVNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLNF-----SGKNYRAVAYEVDRETMRIEPEK 159
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 160 VREAALAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSG 239
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 240 MILSSRG------------EQWGKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgadd 307
Cdd:pfam00464 241 MIFYRKGvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEAL---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 308 aKNAGIKLVTGGTDVHLVLVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDpRPPAVTSGLRIGTPALATRGFDAEDFAE 387
Cdd:pfam00464 317 -TERGYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEK 394
|
....*
gi 881057965 388 VADII 392
Cdd:pfam00464 395 VAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
3-423 |
1.99e-155 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 447.12 E-value: 1.99e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 3 SLNDMTLAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIER 82
Cdd:PTZ00094 9 LPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 83 AKQVFGGDY----VNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGM-----RLNFSGKNYRAVAYEVDRETM 153
Cdd:PTZ00094 89 ALEAFGLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFytakkKVSATSIYFESLPYQVNEKGL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 154 rIEPEKVREAALAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTL 233
Cdd:PTZ00094 169 -IDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 234 GGPRSGMILSSRG--EQWGKKLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLgaddaKNA 311
Cdd:PTZ00094 248 RGPRSGLIFYRKKvkPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAAL-----EKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 312 GIKLVTGGTDVHLVLVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAvTSGLRIGTPALATRGFDAEDFAEVADI 391
Cdd:PTZ00094 323 GYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALN-PSGVRLGTPALTTRGAKEKDFKFVADF 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 881057965 392 I--GTTLS---QGASG-----------GNVEVDALRARVKKLTDKHPL 423
Cdd:PTZ00094 402 LdrAVKLAqeiQKQVGkklvdfkkaleKNPELQKLRQEVVEFASQFPF 449
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
9-427 |
6.91e-150 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 434.47 E-value: 6.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 9 LAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQVFG 88
Cdd:PRK13580 30 ILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 89 GDYVNVQPH---------------AGAQANAAALMAMANVGD----------------PILGLSLAHGGHLTHGMRLNFS 137
Cdd:PRK13580 110 AEHAYVQPHsgadanlvafwailaHKVESPALEKLGAKTVNDlteedwealraelgnqRLLGMSLDSGGHLTHGFRPNIS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 138 GKNYRAVAYEVDRETMRIEPEKVREAALAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGL--- 214
Cdd:PRK13580 190 GKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVftg 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 215 HPNPVPFADVVTTTVHKTLGGPRSGMILSsrGEQWGKKLNTAVfPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLE 294
Cdd:PRK13580 270 DEDPVPHADIVTTTTHKTLRGPRGGLVLA--KKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 295 GAQIIAERLgaddAKNaGIKLVTGGTDVHLVLVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDPRPPAVTSGLRIGTPA 374
Cdd:PRK13580 347 NARALAEGF----LKR-GARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPA 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881057965 375 LATRGFDAEDFAEVADII---------GTTLSQGASGGNVEVDA-----LRARVKKLTDKHPLYAGL 427
Cdd:PRK13580 422 LTTLGMGSDEMDEVAELIvkvlsnttpGTTAEGAPSKAKYELDEgvaqeVRARVAELLARFPLYPEI 488
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
9-422 |
2.63e-136 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 399.36 E-value: 2.63e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 9 LAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQVFG 88
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 89 GDY----VNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLnfSGKNYRAVA-------YEVDRETMRIEP 157
Cdd:PLN03226 95 LDPekwgVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQT--DGKKISATSiyfesmpYRLDESTGLIDY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 158 EKVREAALAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPR 237
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 238 SGMILSSRGEQWGK------------KLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQIIAERLga 305
Cdd:PLN03226 253 GGMIFFRKGPKPPKgqgegavydyedKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRL-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 306 ddaKNAGIKLVTGGTDVHLVLVDLVDSELNGQQAEDLLHEVGITVNRNAVPFDpRPPAVTSGLRIGTPALATRGFDAEDF 385
Cdd:PLN03226 331 ---MSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDF 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 881057965 386 AEVADII--GTTLS---QGASGG--------------NVEVDALRARVKKLTDKHP 422
Cdd:PLN03226 407 EKVAEFLhrAVTIAlkiQKEHGKklkdfkkglesndfSKDIEALRAEVEEFATSFP 462
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
9-390 |
1.30e-97 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 303.65 E-value: 1.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 9 LAQLDPEIQAVLDAELGRQRDTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGRRYYGGCEFVDVAESLAIERAKQVFG 88
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 89 GDY----VNVQPHAGAQANAAALMAMANVGDPILGLSLAHGGHLTHGMRLNfSGKN-------YRAVAYEVDRETMRIEP 157
Cdd:PLN02271 209 LDSekwgVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTP-GGKKvsgasifFESLPYKVNPQTGYIDY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 158 EKVREAALAEHPRVIIAGWSAYPRHLDFQAFRDIADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPR 237
Cdd:PLN02271 288 DKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPR 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 238 SGMILSSRGEQWGK------------------KLNTAVFPGQQGGPLMHVIAAKAIAMKVAQTDEFKDRQRRTLEGAQII 299
Cdd:PLN02271 368 GGIIFYRKGPKLRKqgmllshgddnshydfeeKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQAL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 300 AERLgaddaKNAGIKLVTGGTDVHLVLVDLVDSELNGQQAEDLLHEVGITVNRNAVpFDPRPPAVTSGLRIGTPALATRG 379
Cdd:PLN02271 448 ASAL-----LRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSRG 521
|
410
....*....|.
gi 881057965 380 FDAEDFAEVAD 390
Cdd:PLN02271 522 CLESDFETIAD 532
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
114-241 |
4.31e-17 |
|
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: 78.58 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881057965 114 GDPILGLSLAHGGHLTHGMRLNFsgknYRAVAYEVDRET-MRIEPEKVREAALAEHPRVIIAGWSAYPRHL--DFQAFRD 190
Cdd:cd01494 41 GDEVIVDANGHGSRYWVAAELAG----AKPVPVPVDDAGyGGLDVAILEELKAKPNVALIVITPNTTSGGVlvPLKEIRK 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 881057965 191 IADEVGAALWVDMAHFAGLVAAGLHPNPVPFADVVTTTVHKTLGGPRSGMI 241
Cdd:cd01494 117 IAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGVV 167
|
|
| |
