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Conserved domains on  [gi|1972264317|ref|NP_001379624|]
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Serine hydroxymethyltransferase [Caenorhabditis elegans]

Protein Classification

serine hydroxymethyltransferase( domain architecture ID 11477583)

serine hydroxymethyltransferase catalyzes the reversible, simultaneous conversions of L-serine to glycine (retro-aldol cleavage) and tetrahydrofolate to 5,10-methylenetetrahydrofolate (hydrolysis)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
28-480 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 215639  Cd Length: 475  Bit Score: 851.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  28 HVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVF 107
Cdd:PLN03226   14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 108 GLDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYD 187
Cdd:PLN03226   94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 188 KLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRG 267
Cdd:PLN03226  174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 268 ALIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKH 347
Cdd:PLN03226  254 GMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 348 GYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 427
Cdd:PLN03226  334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFL 413
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972264317 428 HEGVQIAKKYNAEAGKTLKDFKSFTETNePFKKDVADLAKRVEEFSTKFEIPG 480
Cdd:PLN03226  414 HRAVTIALKIQKEHGKKLKDFKKGLESN-DFSKDIEALRAEVEEFATSFPMPG 465
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
28-480 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 851.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  28 HVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVF 107
Cdd:PLN03226   14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 108 GLDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYD 187
Cdd:PLN03226   94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 188 KLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRG 267
Cdd:PLN03226  174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 268 ALIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKH 347
Cdd:PLN03226  254 GMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 348 GYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 427
Cdd:PLN03226  334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFL 413
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972264317 428 HEGVQIAKKYNAEAGKTLKDFKSFTETNePFKKDVADLAKRVEEFSTKFEIPG 480
Cdd:PLN03226  414 HRAVTIALKIQKEHGKKLKDFKKGLESN-DFSKDIEALRAEVEEFATSFPMPG 465
SHMT pfam00464
Serine hydroxymethyltransferase;
29-427 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 728.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  29 VEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFG 108
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 109 LDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYDK 188
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 189 LEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGA 268
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 269 LIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHG 348
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972264317 349 YALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 427
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
30-465 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: 648.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  30 EKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFGL 109
Cdd:cd00378     1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 110 DpakwGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTparKVSATSEFFQSLPYKVDPTTGLIDYDKL 189
Cdd:cd00378    81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 190 EQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGAL 269
Cdd:cd00378   154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 270 IFYRKGvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHGY 349
Cdd:cd00378   234 ILTRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 350 ALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVS-ALRPGGIRLGTPALTSRGFQEQDFEKVGDFIH 428
Cdd:cd00378   301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1972264317 429 EGVQIAKKynaeagktlkdfksfTETNEPFKKDVADL 465
Cdd:cd00378   381 RALKDAED---------------VAVAEEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
27-481 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: 584.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  27 DHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEV 106
Cdd:COG0112     3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 107 FGldpAKWgVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFftparKVSATSEFFQSLPYKVDPTTGLIDY 186
Cdd:COG0112    83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKGYNVVSYGVDPETGLIDY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 187 DKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPR 266
Cdd:COG0112   154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 267 GALIFYRKgvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKK 346
Cdd:COG0112   234 GGLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 347 HGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDV-SALRPGGIRLGTPALTSRGFQEQDFEKVGD 425
Cdd:COG0112   300 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEEIAE 379
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972264317 426 FIHEgvqiakkynaeagkTLKDFKSftetnepfKKDVADLAKRVEEFSTKFEIPGN 481
Cdd:COG0112   380 LIAD--------------VLDNPED--------EAVLAEVREEVKELCKRFPLYPD 413
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
28-480 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 851.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  28 HVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVF 107
Cdd:PLN03226   14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 108 GLDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYD 187
Cdd:PLN03226   94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 188 KLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRG 267
Cdd:PLN03226  174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 268 ALIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKH 347
Cdd:PLN03226  254 GMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 348 GYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 427
Cdd:PLN03226  334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFL 413
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972264317 428 HEGVQIAKKYNAEAGKTLKDFKSFTETNePFKKDVADLAKRVEEFSTKFEIPG 480
Cdd:PLN03226  414 HRAVTIALKIQKEHGKKLKDFKKGLESN-DFSKDIEALRAEVEEFATSFPMPG 465
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
29-480 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 764.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  29 VEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFG 108
Cdd:PTZ00094   15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 109 LDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPtTGLIDYDK 188
Cdd:PTZ00094   95 LDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNE-KGLIDYDK 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 189 LEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGA 268
Cdd:PTZ00094  174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 269 LIFYRKGVRStnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHG 348
Cdd:PTZ00094  254 LIFYRKKVKP----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRG 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 349 YALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFIH 428
Cdd:PTZ00094  324 YDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLD 403
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1972264317 429 EGVQIAKKYNAEAGKTLKDFKSFTETNEpfkkDVADLAKRVEEFSTKFEIPG 480
Cdd:PTZ00094  404 RAVKLAQEIQKQVGKKLVDFKKALEKNP----ELQKLRQEVVEFASQFPFPG 451
SHMT pfam00464
Serine hydroxymethyltransferase;
29-427 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 728.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  29 VEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFG 108
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 109 LDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYDK 188
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 189 LEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGA 268
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 269 LIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHG 348
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972264317 349 YALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 427
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
30-465 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: 648.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  30 EKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFGL 109
Cdd:cd00378     1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 110 DpakwGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTparKVSATSEFFQSLPYKVDPTTGLIDYDKL 189
Cdd:cd00378    81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 190 EQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGAL 269
Cdd:cd00378   154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 270 IFYRKGvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHGY 349
Cdd:cd00378   234 ILTRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 350 ALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVS-ALRPGGIRLGTPALTSRGFQEQDFEKVGDFIH 428
Cdd:cd00378   301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1972264317 429 EGVQIAKKynaeagktlkdfksfTETNEPFKKDVADL 465
Cdd:cd00378   381 RALKDAED---------------VAVAEEVRKEVAEL 402
PLN02271 PLN02271
serine hydroxymethyltransferase
33-480 0e+00

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 594.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  33 DPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFGLDPA 112
Cdd:PLN02271  133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSE 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 113 KWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPA-RKVSATSEFFQSLPYKVDPTTGLIDYDKLEQ 191
Cdd:PLN02271  213 KWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGgKKVSGASIFFESLPYKVNPQTGYIDYDKLEE 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 192 NAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGALIF 271
Cdd:PLN02271  293 KALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIF 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 272 YRKGVRSTNAKGV------DTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMK 345
Cdd:PLN02271  373 YRKGPKLRKQGMLlshgddNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALL 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 346 KHGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGD 425
Cdd:PLN02271  453 RRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESDFETIAD 532
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972264317 426 FIHEGVQIAKKYNAEAGKTLKDFKSFTETNepfkKDVADLAKRVEEFSTKFEIPG 480
Cdd:PLN02271  533 FLLRAAQIASAVQREHGKLQKEFLKGLQNN----KDIVELRNRVEAFASQFAMPG 583
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
27-481 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: 584.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  27 DHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEV 106
Cdd:COG0112     3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 107 FGldpAKWgVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFftparKVSATSEFFQSLPYKVDPTTGLIDY 186
Cdd:COG0112    83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKGYNVVSYGVDPETGLIDY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 187 DKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPR 266
Cdd:COG0112   154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 267 GALIFYRKgvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKK 346
Cdd:COG0112   234 GGLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 347 HGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDV-SALRPGGIRLGTPALTSRGFQEQDFEKVGD 425
Cdd:COG0112   300 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEEIAE 379
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972264317 426 FIHEgvqiakkynaeagkTLKDFKSftetnepfKKDVADLAKRVEEFSTKFEIPGN 481
Cdd:COG0112   380 LIAD--------------VLDNPED--------EAVLAEVREEVKELCKRFPLYPD 413
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
27-481 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 571.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  27 DHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEV 106
Cdd:PRK00011    4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 107 FGldpAKWgVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGfftpaRKVSATSEFFQSLPYKVDPTTGLIDY 186
Cdd:PRK00011   84 FG---AEY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGLIDY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 187 DKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPR 266
Cdd:PRK00011  155 DEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 267 GALIFYRKGvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKK 346
Cdd:PRK00011  235 GGLILTNDE-------------ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAE 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 347 HGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDV-SALRPGGIRLGTPALTSRGFQEQDFEKVGD 425
Cdd:PRK00011  302 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPrSPFVTSGIRIGTPAITTRGFKEAEMKEIAE 381
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972264317 426 FIHEgvqIAKKYNAEAgktlkdfksftetnepfkkDVADLAKRVEEFSTKFEIPGN 481
Cdd:PRK00011  382 LIAD---VLDNPDDEA-------------------VIEEVKEEVKELCKRFPLYKY 415
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
21-468 4.46e-177

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 502.95  E-value: 4.46e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  21 NENILVDHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQ 100
Cdd:PRK13034    1 LMFFFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 101 KRALEVFGLDPAkwgvNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGfftpaRKVSATSEFFQSLPYKVDPT 180
Cdd:PRK13034   81 ERAKQLFGCDYA----NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 181 TGLIDYDKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHK 260
Cdd:PRK13034  152 TGLIDYDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 261 SLRGPRGALIFyrkgvrsTNAKgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTL 340
Cdd:PRK13034  232 TLRGPRGGMIL-------TNDE------EIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQAL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 341 AERMKKHGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDV-SALRPGGIRLGTPALTSRGFQEQD 419
Cdd:PRK13034  299 AEVLKERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTeSPFVTSGIRIGTPAGTTRGFGEAE 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1972264317 420 FEKVGDFIHEgvqiakkynaeagkTLKDFKSfTETNEPFKKDVADLAKR 468
Cdd:PRK13034  379 FREIANWILD--------------VLDDLGN-AALEQRVRKEVKALCSR 412
PRK13580 PRK13580
glycine hydroxymethyltransferase;
27-429 3.67e-129

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 384.01  E-value: 3.67e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  27 DHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEV 106
Cdd:PRK13580   28 DVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKEL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 107 FGLDPAKwgvnVQPLSGSPANFAVYTAIVG-------------------------------SNGRIMGLDLPDGGHLTHG 155
Cdd:PRK13580  108 FGAEHAY----VQPHSGADANLVAFWAILAhkvespaleklgaktvndlteedwealraelGNQRLLGMSLDSGGHLTHG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 156 FftparKVSATSEFFQSLPYKVDPTTGLIDYDKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHI 235
Cdd:PRK13580  184 F-----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHF 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 236 SGLVAAGLIP---SPFEYSDVVTTTTHKSLRGPRGALIFYRKgvrstnakgvdtlyDLEEKINSAVfPGLQGGPHNHTIA 312
Cdd:PRK13580  259 AGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVLAKK--------------EYADAVDKGC-PLVLGGPLPHVMA 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 313 GIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCP 392
Cdd:PRK13580  324 AKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIP 403
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1972264317 393 GDVS-ALRPGGIRLGTPALTSRGFQEQDFEKVGDFIHE 429
Cdd:PRK13580  404 SDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVK 441
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
99-273 2.69e-23

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: 96.30  E-value: 2.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317  99 CQKRALEVFGldPAKWGVNVQPlSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLThgfftparkVSATSEFFQSLPYKVD 178
Cdd:cd01494     5 LEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYW---------VAAELAGAKPVPVPVD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972264317 179 PTT-GLIDYDKLEQNAMLFRPKAIIAGVSCYARHL--DYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVT 255
Cdd:cd01494    73 DAGyGGLDVAILEELKAKPNVALIVITPNTTSGGVlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVT 152
                         170
                  ....*....|....*...
gi 1972264317 256 TTTHKSLRGPRGALIFYR 273
Cdd:cd01494   153 FSLHKNLGGEGGGVVIVK 170
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
177-234 3.67e-04

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 42.75  E-value: 3.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972264317 177 VDPTTGLIDYDKLEQnAMLFRPKAII----AGVSCyarhlDYERFRKIATKAGAYLMSDMAH 234
Cdd:COG0399    99 IDPDTYNIDPEALEA-AITPRTKAIIpvhlYGQPA-----DMDAIMAIAKKHGLKVIEDAAQ 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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