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Conserved domains on  [gi|15236375|ref|NP_193129|]
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serine hydroxymethyltransferase 4 [Arabidopsis thaliana]

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
1-471 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 215639  Cd Length: 475  Bit Score: 1029.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    1 MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIEN 80
Cdd:PLN03226   4 MVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIET 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   81 LCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGgKKISATSIYFESLPYK 160
Cdd:PLN03226  84 LCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDG-KKISATSIYFESMPYR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  161 VNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTT 240
Cdd:PLN03226 163 LDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTT 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  241 TTHKSLRGPRAGMIFYRKGPKPPKKGQpEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKA 320
Cdd:PLN03226 243 TTHKSLRGPRGGMIFFRKGPKPPKGQG-EGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  321 NAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGL 400
Cdd:PLN03226 322 NAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGL 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236375  401 VEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNN---KDLDQLKADVEKFSASYEMPGFLMSEMKYKD 471
Cdd:PLN03226 402 VEKDFEKVAEFLHRAVTIALKIQKEHGKKLKDFKKGLESNdfsKDIEALRAEVEEFATSFPMPGFDKESMKYKE 475
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
1-471 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 1029.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    1 MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIEN 80
Cdd:PLN03226   4 MVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIET 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   81 LCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGgKKISATSIYFESLPYK 160
Cdd:PLN03226  84 LCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDG-KKISATSIYFESMPYR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  161 VNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTT 240
Cdd:PLN03226 163 LDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTT 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  241 TTHKSLRGPRAGMIFYRKGPKPPKKGQpEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKA 320
Cdd:PLN03226 243 TTHKSLRGPRGGMIFFRKGPKPPKGQG-EGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  321 NAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGL 400
Cdd:PLN03226 322 NAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGL 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236375  401 VEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNN---KDLDQLKADVEKFSASYEMPGFLMSEMKYKD 471
Cdd:PLN03226 402 VEKDFEKVAEFLHRAVTIALKIQKEHGKKLKDFKKGLESNdfsKDIEALRAEVEEFATSFPMPGFDKESMKYKE 475
SHMT pfam00464
Serine hydroxymethyltransferase;
12-412 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 682.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    12 LVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFH 91
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    92 CDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSgGKKISATSIYFESLPYKVNFTTGYIDYD 171
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVN-SKKISASSKFFESMPYGVDPETGYIDYD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   172 KLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRA 251
Cdd:pfam00464 160 QLEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   252 GMIFYRKGPKPPKKGQPEGaVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNYLMS 331
Cdd:pfam00464 240 GMIFYRKGVKSVDKTGKEI-LYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   332 KGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGLVEKDFEQIGEF 411
Cdd:pfam00464 319 RGYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398

                  .
gi 15236375   412 L 412
Cdd:pfam00464 399 I 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
15-424 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: 604.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  15 VDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFHCDp 94
Cdd:cd00378   3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  95 aawGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTsggkKISATSIYFESLPYKVNFTTGYIDYDKLE 174
Cdd:cd00378  82 ---YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT----KVSASGKLFESVPYGVDPETGLIDYDALE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 175 EKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRAGMI 254
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 255 FYRKGpkppkkgqpegavyDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNYLMSKGY 334
Cdd:cd00378 235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 335 QIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAV-FGDSSALAPGGVRIGAPAMTSRGLVEKDFEQIGEFLS 413
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLpWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                       410
                ....*....|.
gi 15236375 414 RAVTLTLDIQK 424
Cdd:cd00378 381 RALKDAEDVAV 391
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
9-463 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: 601.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   9 NTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALE 88
Cdd:COG0112   2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  89 AFHCDPAawgvNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGyytsggKKISATSIYFESLPYKVNFTTGYI 168
Cdd:COG0112  82 LFGAEHA----NVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG------SPVNFSGKGYNVVSYGVDPETGLI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 169 DYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRG 248
Cdd:COG0112 152 DYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 249 PRAGMIFYRKgpkppkkgqpegavyDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNY 328
Cdd:COG0112 232 PRGGLILCNE---------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEA 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 329 LMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDS-SALAPGGVRIGAPAMTSRGLVEKDFEQ 407
Cdd:COG0112 297 LAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEE 376
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15236375 408 IGEFLSRAVtltldiqktygkllkdfnKGLVNNKDLDQLKADVEKFSASYEMPGFL 463
Cdd:COG0112 377 IAELIADVL------------------DNPEDEAVLAEVREEVKELCKRFPLYPDL 414
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
1-471 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 1029.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    1 MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIEN 80
Cdd:PLN03226   4 MVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIET 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   81 LCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGgKKISATSIYFESLPYK 160
Cdd:PLN03226  84 LCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDG-KKISATSIYFESMPYR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  161 VNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTT 240
Cdd:PLN03226 163 LDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTT 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  241 TTHKSLRGPRAGMIFYRKGPKPPKKGQpEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKA 320
Cdd:PLN03226 243 TTHKSLRGPRGGMIFFRKGPKPPKGQG-EGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  321 NAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGL 400
Cdd:PLN03226 322 NAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGL 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236375  401 VEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNN---KDLDQLKADVEKFSASYEMPGFLMSEMKYKD 471
Cdd:PLN03226 402 VEKDFEKVAEFLHRAVTIALKIQKEHGKKLKDFKKGLESNdfsKDIEALRAEVEEFATSFPMPGFDKESMKYKE 475
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
1-462 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 815.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    1 MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIEN 80
Cdd:PTZ00094   4 SRNLVLPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   81 LCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTsGGKKISATSIYFESLPYK 160
Cdd:PTZ00094  84 LCQKRALEAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYT-AKKKVSATSIYFESLPYQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  161 VNfTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTT 240
Cdd:PTZ00094 163 VN-EKGLIDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  241 TTHKSLRGPRAGMIFYRKGPKPpkkgqpegavyDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKA 320
Cdd:PTZ00094 242 TTHKSLRGPRSGLIFYRKKVKP-----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLK 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  321 NAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGL 400
Cdd:PTZ00094 311 NAKALAAALEKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGA 390
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236375  401 VEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNNKDLDQLKADVEKFSASYEMPGF 462
Cdd:PTZ00094 391 KEKDFKFVADFLDRAVKLAQEIQKQVGKKLVDFKKALEKNPELQKLRQEVVEFASQFPFPGI 452
PLN02271 PLN02271
serine hydroxymethyltransferase
4-464 0e+00

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 773.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    4 VSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCR 83
Cdd:PLN02271 121 VRAWGNQPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCC 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   84 SRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGGKKISATSIYFESLPYKVNF 163
Cdd:PLN02271 201 ERALAAFGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGGKKVSGASIFFESLPYKVNP 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  164 TTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTH 243
Cdd:PLN02271 281 QTGYIDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTH 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  244 KSLRGPRAGMIFYRKGPKPPKKGQ-----PEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQV 318
Cdd:PLN02271 361 KSLRGPRGGIIFYRKGPKLRKQGMllshgDDNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQV 440
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  319 KANAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSR 398
Cdd:PLN02271 441 KKNAQALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSR 520
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236375  399 GLVEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNNKDLDQLKADVEKFSASYEMPGFLM 464
Cdd:PLN02271 521 GCLESDFETIADFLLRAAQIASAVQREHGKLQKEFLKGLQNNKDIVELRNRVEAFASQFAMPGFDV 586
SHMT pfam00464
Serine hydroxymethyltransferase;
12-412 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 682.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    12 LVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFH 91
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    92 CDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSgGKKISATSIYFESLPYKVNFTTGYIDYD 171
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVN-SKKISASSKFFESMPYGVDPETGYIDYD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   172 KLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRA 251
Cdd:pfam00464 160 QLEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   252 GMIFYRKGPKPPKKGQPEGaVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNYLMS 331
Cdd:pfam00464 240 GMIFYRKGVKSVDKTGKEI-LYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   332 KGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGLVEKDFEQIGEF 411
Cdd:pfam00464 319 RGYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398

                  .
gi 15236375   412 L 412
Cdd:pfam00464 399 I 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
15-424 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: 604.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  15 VDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFHCDp 94
Cdd:cd00378   3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  95 aawGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTsggkKISATSIYFESLPYKVNFTTGYIDYDKLE 174
Cdd:cd00378  82 ---YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT----KVSASGKLFESVPYGVDPETGLIDYDALE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 175 EKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRAGMI 254
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 255 FYRKGpkppkkgqpegavyDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNYLMSKGY 334
Cdd:cd00378 235 LTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 335 QIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAV-FGDSSALAPGGVRIGAPAMTSRGLVEKDFEQIGEFLS 413
Cdd:cd00378 301 KVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLpWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIA 380
                       410
                ....*....|.
gi 15236375 414 RAVTLTLDIQK 424
Cdd:cd00378 381 RALKDAEDVAV 391
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
9-463 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: 601.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   9 NTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALE 88
Cdd:COG0112   2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  89 AFHCDPAawgvNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGyytsggKKISATSIYFESLPYKVNFTTGYI 168
Cdd:COG0112  82 LFGAEHA----NVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG------SPVNFSGKGYNVVSYGVDPETGLI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 169 DYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRG 248
Cdd:COG0112 152 DYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 249 PRAGMIFYRKgpkppkkgqpegavyDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNY 328
Cdd:COG0112 232 PRGGLILCNE---------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEA 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 329 LMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDS-SALAPGGVRIGAPAMTSRGLVEKDFEQ 407
Cdd:COG0112 297 LAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEE 376
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15236375 408 IGEFLSRAVtltldiqktygkllkdfnKGLVNNKDLDQLKADVEKFSASYEMPGFL 463
Cdd:COG0112 377 IAELIADVL------------------DNPEDEAVLAEVREEVKELCKRFPLYPDL 414
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
9-463 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 588.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    9 NTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALE 88
Cdd:PRK00011   3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   89 AFHCDPAawgvNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGyytsggKKISATSIYFESLPYKVNFTTGYI 168
Cdd:PRK00011  83 LFGAEYA----NVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG------SPVNFSGKLYNVVSYGVDEETGLI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  169 DYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRG 248
Cdd:PRK00011 153 DYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  249 PRAGMIFYRKGpkppkkgqpegavyDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNY 328
Cdd:PRK00011 233 PRGGLILTNDE--------------ELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  329 LMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAV-FGDSSALAPGGVRIGAPAMTSRGLVEKDFEQ 407
Cdd:PRK00011 299 LAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVpFDPRSPFVTSGIRIGTPAITTRGFKEAEMKE 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15236375  408 IGEFLSRAVtltldiqktygkllkdfnKGLVNNKDLDQLKADVEKFSASYEMPGFL 463
Cdd:PRK00011 379 IAELIADVL------------------DNPDDEAVIEEVKEEVKELCKRFPLYKYL 416
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
9-410 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 514.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    9 NTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALE 88
Cdd:PRK13034   6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   89 AFHCDPAawgvNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGyytsggKKISATSIYFESLPYKVNFTTGYI 168
Cdd:PRK13034  86 LFGCDYA----NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG------AKVSLSGKWYNAVQYGVDRLTGLI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  169 DYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRG 248
Cdd:PRK13034 156 DYDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  249 PRAGMIFYRKGpkppkkgqpegavyDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNY 328
Cdd:PRK13034 236 PRGGMILTNDE--------------EIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  329 LMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDS-SALAPGGVRIGAPAMTSRGLVEKDFEQ 407
Cdd:PRK13034 302 LKERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTeSPFVTSGIRIGTPAGTTRGFGEAEFRE 381

                 ...
gi 15236375  408 IGE 410
Cdd:PRK13034 382 IAN 384
PRK13580 PRK13580
glycine hydroxymethyltransferase;
12-419 7.49e-123

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 367.06  E-value: 7.49e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   12 LVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFH 91
Cdd:PRK13580  30 ILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   92 CDPAAwgvnVQPYSGSPANFAAYTALL---------------QPHD----------------RIMGLDLPSGGHLTHGYy 140
Cdd:PRK13580 110 AEHAY----VQPHSGADANLVAFWAILahkvespaleklgakTVNDlteedwealraelgnqRLLGMSLDSGGHLTHGF- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  141 tsggkKISATSIYFESLPYKVNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHIS 220
Cdd:PRK13580 185 -----RPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFA 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  221 GLVAA---QEAANPFEYCDVVTTTTHKSLRGPRAGMIFYRKgpkppkkgqpegavyDFEDKINFAVfPALQGGPHNHQIG 297
Cdd:PRK13580 260 GLVAGkvfTGDEDPVPHADIVTTTTHKTLRGPRGGLVLAKK---------------EYADAVDKGC-PLVLGGPLPHVMA 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  298 ALAVALKQANTPGFKVYAKQVKANAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVF 377
Cdd:PRK13580 324 AKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIP 403
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 15236375  378 GDSS-ALAPGGVRIGAPAMTSRGLVEKDFEQIGEFLSRAVTLT 419
Cdd:PRK13580 404 SDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVKVLSNT 446
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
79-257 1.19e-26

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: 105.54  E-value: 1.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375  79 ENLCRSRALEAFhcDPAAWGVNVQPySGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHgyytsggkkiSATSIYFESLP 158
Cdd:cd01494   2 LEELEEKLARLL--QPGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV----------AAELAGAKPVP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375 159 YKVNFTTGYIDYDKLEEKALDFRPKLLIC-------GGSAYPRDwdyaRFRAIADKVGALLLCDMAHISGLVAAQEAANP 231
Cdd:cd01494  69 VPVDDAGYGGLDVAILEELKAKPNVALIVitpnttsGGVLVPLK----EIRKIAKEYGILLLVDAASAGGASPAPGVLIP 144
                       170       180
                ....*....|....*....|....*.
gi 15236375 232 FEYCDVVTTTTHKSLRGPRAGMIFYR 257
Cdd:cd01494 145 EGGADVVTFSLHKNLGGEGGGVVIVK 170
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
99-255 1.35e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 46.91  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375    99 VNVQPYSGSPAN-FAAYTALLQPHDRIMgLDLPsgghlTHGYYTSGGKKISATSIYFESLPYKvNFTtgyIDYDKLEEkA 177
Cdd:pfam00155  64 AAVVFGSGAGANiEALIFLLANPGDAIL-VPAP-----TYASYIRIARLAGGEVVRYPLYDSN-DFH---LDFDALEA-A 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236375   178 LDFRPK-LLICG-----GSAYPRDwDYARFRAIADKVGALLLCDMAHIsGLVAAQEAANPF-----EYCDVVTTTT-HKS 245
Cdd:pfam00155 133 LKEKPKvVLHTSphnptGTVATLE-ELEKLLDLAKEHNILLLVDEAYA-GFVFGSPDAVATrallaEGPNLLVVGSfSKA 210
                         170
                  ....*....|..
gi 15236375   246 --LRGPRAGMIF 255
Cdd:pfam00155 211 fgLAGWRVGYIL 222
 
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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