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Conserved domains on  [gi|25144732|ref|NP_741197|]
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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
51-503 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 25144732   51 HVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVF 130
Cdd:PLN03226  14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  131 GLDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYD 210
Cdd:PLN03226  94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  211 KLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRG 290
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  291 ALIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKH 370
Cdd:PLN03226 254 GMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  371 GYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 450
Cdd:PLN03226 334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFL 413
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 25144732  451 HEGVQIAKKYNAEAGKTLKDFKSFTETNePFKKDVADLAKRVEEFSTKFEIPG 503
Cdd:PLN03226 414 HRAVTIALKIQKEHGKKLKDFKKGLESN-DFSKDIEALRAEVEEFATSFPMPG 465
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
51-503 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 25144732   51 HVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVF 130
Cdd:PLN03226  14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  131 GLDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYD 210
Cdd:PLN03226  94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  211 KLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRG 290
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  291 ALIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKH 370
Cdd:PLN03226 254 GMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  371 GYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 450
Cdd:PLN03226 334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFL 413
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 25144732  451 HEGVQIAKKYNAEAGKTLKDFKSFTETNePFKKDVADLAKRVEEFSTKFEIPG 503
Cdd:PLN03226 414 HRAVTIALKIQKEHGKKLKDFKKGLESN-DFSKDIEALRAEVEEFATSFPMPG 465
SHMT pfam00464
Serine hydroxymethyltransferase;
52-450 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 728.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732    52 VEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFG 131
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   132 LDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYDK 211
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   212 LEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGA 291
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   292 LIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHG 371
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25144732   372 YALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 450
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
53-488 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: 648.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  53 EKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFGL 132
Cdd:cd00378   1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 133 DpakwGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTparKVSATSEFFQSLPYKVDPTTGLIDYDKL 212
Cdd:cd00378  81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 213 EQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGAL 292
Cdd:cd00378 154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 293 IFYRKGvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHGY 372
Cdd:cd00378 234 ILTRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 373 ALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVS-ALRPGGIRLGTPALTSRGFQEQDFEKVGDFIH 451
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 25144732 452 EGVQIAKKynaeagktlkdfksfTETNEPFKKDVADL 488
Cdd:cd00378 381 RALKDAED---------------VAVAEEVRKEVAEL 402
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
50-504 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: 583.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  50 DHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEV 129
Cdd:COG0112   3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 130 FGldpAKWgVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFftparKVSATSEFFQSLPYKVDPTTGLIDY 209
Cdd:COG0112  83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKGYNVVSYGVDPETGLIDY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 210 DKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPR 289
Cdd:COG0112 154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 290 GALIFYRKgvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKK 369
Cdd:COG0112 234 GGLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAE 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 370 HGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDV-SALRPGGIRLGTPALTSRGFQEQDFEKVGD 448
Cdd:COG0112 300 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEEIAE 379
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25144732 449 FIHEgvqiakkynaeagkTLKDFKSftetnepfKKDVADLAKRVEEFSTKFEIPGN 504
Cdd:COG0112 380 LIAD--------------VLDNPED--------EAVLAEVREEVKELCKRFPLYPD 413
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
51-503 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 25144732   51 HVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVF 130
Cdd:PLN03226  14 PLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  131 GLDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYD 210
Cdd:PLN03226  94 RLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDYD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  211 KLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRG 290
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  291 ALIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKH 370
Cdd:PLN03226 254 GMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  371 GYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 450
Cdd:PLN03226 334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFL 413
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 25144732  451 HEGVQIAKKYNAEAGKTLKDFKSFTETNePFKKDVADLAKRVEEFSTKFEIPG 503
Cdd:PLN03226 414 HRAVTIALKIQKEHGKKLKDFKKGLESN-DFSKDIEALRAEVEEFATSFPMPG 465
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
52-503 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 765.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   52 VEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFG 131
Cdd:PTZ00094  15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  132 LDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPtTGLIDYDK 211
Cdd:PTZ00094  95 LDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNE-KGLIDYDK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  212 LEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGA 291
Cdd:PTZ00094 174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  292 LIFYRKGVRStnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHG 371
Cdd:PTZ00094 254 LIFYRKKVKP----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  372 YALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFIH 451
Cdd:PTZ00094 324 YDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLD 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 25144732  452 EGVQIAKKYNAEAGKTLKDFKSFTETNEpfkkDVADLAKRVEEFSTKFEIPG 503
Cdd:PTZ00094 404 RAVKLAQEIQKQVGKKLVDFKKALEKNP----ELQKLRQEVVEFASQFPFPG 451
SHMT pfam00464
Serine hydroxymethyltransferase;
52-450 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 728.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732    52 VEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFG 131
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   132 LDPAKWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSLPYKVDPTTGLIDYDK 211
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   212 LEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGA 291
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   292 LIFYRKGVRSTNAKGVDTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHG 371
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25144732   372 YALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGDFI 450
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
53-488 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: 648.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  53 EKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFGL 132
Cdd:cd00378   1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 133 DpakwGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTparKVSATSEFFQSLPYKVDPTTGLIDYDKL 212
Cdd:cd00378  81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 213 EQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGAL 292
Cdd:cd00378 154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 293 IFYRKGvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHGY 372
Cdd:cd00378 234 ILTRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 373 ALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVS-ALRPGGIRLGTPALTSRGFQEQDFEKVGDFIH 451
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 25144732 452 EGVQIAKKynaeagktlkdfksfTETNEPFKKDVADL 488
Cdd:cd00378 381 RALKDAED---------------VAVAEEVRKEVAEL 402
PLN02271 PLN02271
serine hydroxymethyltransferase
56-503 0e+00

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 593.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   56 DPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEVFGLDPA 135
Cdd:PLN02271 133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSE 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  136 KWGVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFFTPA-RKVSATSEFFQSLPYKVDPTTGLIDYDKLEQ 214
Cdd:PLN02271 213 KWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGgKKVSGASIFFESLPYKVNPQTGYIDYDKLEE 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  215 NAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGALIF 294
Cdd:PLN02271 293 KALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIF 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  295 YRKGVRSTNAKGV------DTLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMK 368
Cdd:PLN02271 373 YRKGPKLRKQGMLlshgddNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALL 452
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  369 KHGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFQEQDFEKVGD 448
Cdd:PLN02271 453 RRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESDFETIAD 532
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 25144732  449 FIHEGVQIAKKYNAEAGKTLKDFKSFTETNepfkKDVADLAKRVEEFSTKFEIPG 503
Cdd:PLN02271 533 FLLRAAQIASAVQREHGKLQKEFLKGLQNN----KDIVELRNRVEAFASQFAMPG 583
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
50-504 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: 583.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  50 DHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEV 129
Cdd:COG0112   3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 130 FGldpAKWgVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGFftparKVSATSEFFQSLPYKVDPTTGLIDY 209
Cdd:COG0112  83 FG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGS-----PVNFSGKGYNVVSYGVDPETGLIDY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 210 DKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPR 289
Cdd:COG0112 154 DEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 290 GALIFYRKgvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKK 369
Cdd:COG0112 234 GGLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAE 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 370 HGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDV-SALRPGGIRLGTPALTSRGFQEQDFEKVGD 448
Cdd:COG0112 300 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEEIAE 379
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25144732 449 FIHEgvqiakkynaeagkTLKDFKSftetnepfKKDVADLAKRVEEFSTKFEIPGN 504
Cdd:COG0112 380 LIAD--------------VLDNPED--------EAVLAEVREEVKELCKRFPLYPD 413
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
50-504 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 571.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   50 DHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEV 129
Cdd:PRK00011   4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  130 FGldpAKWgVNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGfftpaRKVSATSEFFQSLPYKVDPTTGLIDY 209
Cdd:PRK00011  84 FG---AEY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGLIDY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  210 DKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPR 289
Cdd:PRK00011 155 DEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  290 GALIFYRKGvrstnakgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKK 369
Cdd:PRK00011 235 GGLILTNDE-------------ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAE 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  370 HGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDV-SALRPGGIRLGTPALTSRGFQEQDFEKVGD 448
Cdd:PRK00011 302 RGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPrSPFVTSGIRIGTPAITTRGFKEAEMKEIAE 381
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 25144732  449 FIHEgvqIAKKYNAEAgktlkdfksftetnepfkkDVADLAKRVEEFSTKFEIPGN 504
Cdd:PRK00011 382 LIAD---VLDNPDDEA-------------------VIEEVKEEVKELCKRFPLYKY 415
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
44-491 1.36e-176

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 502.57  E-value: 1.36e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   44 NENILVDHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQ 123
Cdd:PRK13034   1 LMFFFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  124 KRALEVFGLDPAkwgvNVQPLSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLTHGfftpaRKVSATSEFFQSLPYKVDPT 203
Cdd:PRK13034  81 ERAKQLFGCDYA----NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  204 TGLIDYDKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHK 283
Cdd:PRK13034 152 TGLIDYDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  284 SLRGPRGALIFyrkgvrsTNAKgvdtlyDLEEKINSAVFPGLQGGPHNHTIAGIAVALRQCLSEDFVQYGEQVLKNAKTL 363
Cdd:PRK13034 232 TLRGPRGGMIL-------TNDE------EIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQAL 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  364 AERMKKHGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCPGDV-SALRPGGIRLGTPALTSRGFQEQD 442
Cdd:PRK13034 299 AEVLKERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTeSPFVTSGIRIGTPAGTTRGFGEAE 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 25144732  443 FEKVGDFIHEgvqiakkynaeagkTLKDFKSfTETNEPFKKDVADLAKR 491
Cdd:PRK13034 379 FREIANWILD--------------VLDDLGN-AALEQRVRKEVKALCSR 412
PRK13580 PRK13580
glycine hydroxymethyltransferase;
50-452 1.27e-128

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 383.24  E-value: 1.27e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732   50 DHVEKVDPEVFDIMKNEKKRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMELLCQKRALEV 129
Cdd:PRK13580  28 DVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKEL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  130 FGLDPAKwgvnVQPLSGSPANFAVYTAIVG-------------------------------SNGRIMGLDLPDGGHLTHG 178
Cdd:PRK13580 108 FGAEHAY----VQPHSGADANLVAFWAILAhkvespaleklgaktvndlteedwealraelGNQRLLGMSLDSGGHLTHG 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  179 FftparKVSATSEFFQSLPYKVDPTTGLIDYDKLEQNAMLFRPKAIIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHI 258
Cdd:PRK13580 184 F-----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHF 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  259 SGLVAAGLIP---SPFEYSDVVTTTTHKSLRGPRGALIFYRKgvrstnakgvdtlyDLEEKINSAVfPGLQGGPHNHTIA 335
Cdd:PRK13580 259 AGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVLAKK--------------EYADAVDKGC-PLVLGGPLPHVMA 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732  336 GIAVALRQCLSEDFVQYGEQVLKNAKTLAERMKKHGYALATGGTDNHLLLVDLRPIGVEGARAEHVLDLAHIACNKNTCP 415
Cdd:PRK13580 324 AKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIP 403
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 25144732  416 GDVS-ALRPGGIRLGTPALTSRGFQEQDFEKVGDFIHE 452
Cdd:PRK13580 404 SDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVK 441
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
122-296 2.92e-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: 2.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 122 CQKRALEVFGldPAKWGVNVQPlSGSPANFAVYTAIVGSNGRIMGLDLPDGGHLThgfftparkVSATSEFFQSLPYKVD 201
Cdd:cd01494   5 LEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYW---------VAAELAGAKPVPVPVD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144732 202 PTT-GLIDYDKLEQNAMLFRPKAIIAGVSCYARHL--DYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVT 278
Cdd:cd01494  73 DAGyGGLDVAILEELKAKPNVALIVITPNTTSGGVlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVT 152
                       170
                ....*....|....*...
gi 25144732 279 TTTHKSLRGPRGALIFYR 296
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
200-257 4.21e-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: 4.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25144732 200 VDPTTGLIDYDKLEQnAMLFRPKAII----AGVSCyarhlDYERFRKIATKAGAYLMSDMAH 257
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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