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Conserved domains on  [gi|530410579|ref|XP_005256824|]
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serine hydroxymethyltransferase, cytosolic isoform X1 [Homo sapiens]

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)

CATH:  3.90.1150.10|3.40.640.10
EC:  2.1.2.1
Gene Ontology:  GO:0004372|GO:0030170|GO:0070905|GO:0008270|GO:0019264|GO:0048027
PubMed:  12686103|2201683|10800595|10673430

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 24-480 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 215639  Cd Length: 475  Bit Score: 816.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 264 AGMIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALT 343
Cdd:PLN03226 253 GGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLM 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 344 ELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAH 423
Cdd:PLN03226 332 SKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAE 411

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530410579 424 FIHRGIELTLQIQSDTGVRatLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL 480
Cdd:PLN03226 412 FLHRAVTIALKIQKEHGKK--LKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGF 466
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 24-480 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 816.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 264 AGMIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALT 343
Cdd:PLN03226 253 GGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLM 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 344 ELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAH 423
Cdd:PLN03226 332 SKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAE 411

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530410579 424 FIHRGIELTLQIQSDTGVRatLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL 480
Cdd:PLN03226 412 FLHRAVTIALKIQKEHGKK--LKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGF 466
SHMT pfam00464
Serine hydroxymethyltransferase;
26-425 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 769.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579   26 LKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYK 105
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  106 LDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQ 185
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  186 LEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG 265
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  266 MIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTEL 345
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  346 GYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 425
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 27-453 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: 632.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  27 KDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKL 106
Cdd:cd00378    1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 107 DpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTdkkKISATSIFFESMPYKVNPDTGYINYDQL 186
Cdd:cd00378   81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 187 EENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGM 266
Cdd:cd00378  154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 267 IFYRKGvksvdpktgkeilyNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELG 346
Cdd:cd00378  234 ILTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERG 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 347 YKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 425
Cdd:cd00378  300 FKVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFI 379

                        410       420
                 ....*....|....*....|....*...
gi 530410579 426 HRGIeltlqiqSDTGVRATLKEFKERLA 453
Cdd:cd00378  380 ARAL-------KDAEDVAVAEEVRKEVA 400
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 21-479 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: 553.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  21 MLaQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:COG0112    1 ML-SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:COG0112   80 KELFGAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:COG0112  151 IDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLR 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 261 GCRAGMIFyrkgvksvdpkTGKEilynLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSE 340
Cdd:COG0112  231 GPRGGLIL-----------CNEE----LAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAE 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 341 ALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQ 419
Cdd:COG0112  296 ALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEME 375

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 420 KVAHFIHRGieltlqiqsdtgvratlkefkerLAGDKYQAAVQALREEVESFASLFPLPG 479
Cdd:COG0112  376 EIAELIADV-----------------------LDNPEDEAVLAEVREEVKELCKRFPLYP 412
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 24-480 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 816.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 264 AGMIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALT 343
Cdd:PLN03226 253 GGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLM 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 344 ELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAH 423
Cdd:PLN03226 332 SKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAE 411

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530410579 424 FIHRGIELTLQIQSDTGVRatLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL 480
Cdd:PLN03226 412 FLHRAVTIALKIQKEHGKK--LKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGF 466
SHMT pfam00464
Serine hydroxymethyltransferase;
26-425 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 769.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579   26 LKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYK 105
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  106 LDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQ 185
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  186 LEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG 265
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  266 MIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTEL 345
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  346 GYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 425
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
 24-480 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 737.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PTZ00094  13 QSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDtGYINY 183
Cdd:PTZ00094  93 FGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLIDY 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PTZ00094 172 DKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPR 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 264 AGMIFYRKGVKSvdpktgkeilyNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALT 343
Cdd:PTZ00094 252 SGLIFYRKKVKP-----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 344 ELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAH 423
Cdd:PTZ00094 321 KRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVAD 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530410579 424 FIHRGIELTLQIQSDTGvrATLKEFKERLAGDKyqaAVQALREEVESFASLFPLPGL 480
Cdd:PTZ00094 401 FLDRAVKLAQEIQKQVG--KKLVDFKKALEKNP---ELQKLRQEVVEFASQFPFPGI 452
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 27-453 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: 632.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  27 KDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKL 106
Cdd:cd00378    1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 107 DpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTdkkKISATSIFFESMPYKVNPDTGYINYDQL 186
Cdd:cd00378   81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 187 EENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGM 266
Cdd:cd00378  154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 267 IFYRKGvksvdpktgkeilyNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELG 346
Cdd:cd00378  234 ILTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERG 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 347 YKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 425
Cdd:cd00378  300 FKVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFI 379

                        410       420
                 ....*....|....*....|....*...
gi 530410579 426 HRGIeltlqiqSDTGVRATLKEFKERLA 453
Cdd:cd00378  380 ARAL-------KDAEDVAVAEEVRKEVA 400
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 21-479 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: 553.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  21 MLaQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:COG0112    1 ML-SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:COG0112   80 KELFGAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:COG0112  151 IDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLR 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 261 GCRAGMIFyrkgvksvdpkTGKEilynLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSE 340
Cdd:COG0112  231 GPRGGLIL-----------CNEE----LAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAE 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 341 ALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQ 419
Cdd:COG0112  296 ALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEME 375

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 420 KVAHFIHRGieltlqiqsdtgvratlkefkerLAGDKYQAAVQALREEVESFASLFPLPG 479
Cdd:COG0112  376 EIAELIADV-----------------------LDNPEDEAVLAEVREEVKELCKRFPLYP 412
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 21-479 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 552.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  21 MLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:PRK00011   1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:PRK00011  81 KELFGAE----YANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:PRK00011 152 IDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLR 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 261 GCRAGMIFyrkgvkSVDPKTGKEilynleslINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSE 340
Cdd:PRK00011 232 GPRGGLIL------TNDEELAKK--------INSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAE 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 341 ALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQ 419
Cdd:PRK00011 298 ALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMK 377

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 420 KVAHFIhrgieltlqiqsdtgvratlkefKERLAGDKYQAAVQALREEVESFASLFPLPG 479
Cdd:PRK00011 378 EIAELI-----------------------ADVLDNPDDEAVIEEVKEEVKELCKRFPLYK 414
PLN02271 PLN02271
serine hydroxymethyltransferase
 24-479 0e+00

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 542.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN02271 127 QPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAA 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMT-DKKKISATSIFFESMPYKVNPDTGYIN 182
Cdd:PLN02271 207 FGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTpGGKKVSGASIFFESLPYKVNPQTGYID 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 183 YDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGC 262
Cdd:PLN02271 287 YDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGP 366

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 263 RAGMIFYRKGVKSVDP-----KTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRA 337
Cdd:PLN02271 367 RGGIIFYRKGPKLRKQgmllsHGDDNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQA 446

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 338 LSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKD 417
Cdd:PLN02271 447 LASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESD 526

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530410579 418 FQKVAHFIHRGIELTLQIQSDTGvratlKEFKERLAGDKYQAAVQALREEVESFASLFPLPG 479
Cdd:PLN02271 527 FETIADFLLRAAQIASAVQREHG-----KLQKEFLKGLQNNKDIVELRNRVEAFASQFAMPG 583
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
 23-478 1.61e-170

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 486.39  E-value: 1.61e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  23 AQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQ 102
Cdd:PRK13034   6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 103 AYkldpQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGYIN 182
Cdd:PRK13034  86 LF----GCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLID 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 183 YDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGC 262
Cdd:PRK13034 157 YDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 263 RAGMifyrkgvksvdpktgkeILYNLESL---INSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALS 339
Cdd:PRK13034 237 RGGM-----------------ILTNDEEIakkINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALA 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 340 EALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDF 418
Cdd:PRK13034 300 EVLKERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEF 379

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410579 419 QKVAHFIhrgieltLQIQSDTGvratlkefkerlagdkyQAAVQA-LREEVESFASLFPLP 478
Cdd:PRK13034 380 REIANWI-------LDVLDDLG-----------------NAALEQrVRKEVKALCSRFPIY 416
PRK13580 PRK13580
glycine hydroxymethyltransferase;
37-480 6.74e-111

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 337.01  E-value: 6.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  37 IKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCwgvnVQ 116
Cdd:PRK13580  41 IRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAY----VQ 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 117 PYSGSPANFAVYTAL---------VEPHG----------------------RIMGLDLPDGGHLTHGFmtdKKKISatSI 165
Cdd:PRK13580 117 PHSGADANLVAFWAIlahkvespaLEKLGaktvndlteedwealraelgnqRLLGMSLDSGGHLTHGF---RPNIS--GK 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 166 FFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVV---- 241
Cdd:PRK13580 192 MFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFtgde 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 242 -PSPFEHchVVTTTTHKTLRGCRAGMIFyrkgvksvdpkTGKEilynLESLINSAVfPGLQGGPHNHAIAGVAVALKQAM 320
Cdd:PRK13580 272 dPVPHAD--IVTTTTHKTLRGPRGGLVL-----------AKKE----YADAVDKGC-PLVLGGPLPHVMAAKAVALAEAR 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 321 TLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRS-ALRPS 399
Cdd:PRK13580 334 TPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNgAWYTS 413

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 400 GLRLGTPALTSRGLLEKDFQKVAHFIHRgieltlqIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPL-P 478
Cdd:PRK13580 414 GIRLGTPALTTLGMGSDEMDEVAELIVK-------VLSNTTPGTTAEGAPSKAKYELDEGVAQEVRARVAELLARFPLyP 486


                 ..
gi 530410579 479 GL 480
Cdd:PRK13580 487 EI 488
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 92-270 6.53e-29

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: 112.09  E-value: 6.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579  92 LETLCQKRALQAYKldPQCWGVNVQPySGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHgfmtdkkkiSATSIFFESMP 171
Cdd:cd01494    1 KLEELEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 172 YKVNPDTGY-INYDQLEENARLFHPKLIIAGTSCYSRNLEYA--RLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHC 248
Cdd:cd01494   69 VPVDDAGYGgLDVAILEELKAKPNVALIVITPNTTSGGVLVPlkEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGA 148

                        170       180
                 ....*....|....*....|..
gi 530410579 249 HVVTTTTHKTLRGCRAGMIFYR 270
Cdd:cd01494  149 DVVTFSLHKNLGGEGGGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 171-404 1.78e-03

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 40.40  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 171 PYKVNPDTGYINYDQLEENARLFHPKLII-------AGTsCYSRNlEYARLRKIADENGAYLMADMAHiSGLVAAGVVPS 243
Cdd:cd00609  109 PVPLDEEGGFLLDLELLEAAKTPKTKLLYlnnpnnpTGA-VLSEE-ELEELAELAKKHGILIISDEAY-AELVYDGEPPP 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 244 PFEhcHVVTTTTHKTLRGC---------RAGMIFYRKgvksvdpktgKEILYNLESLInsavfPGLQGGPHNHAIAGVAV 314
Cdd:cd00609  186 ALA--LLDAYERVIVLRSFsktfglpglRIGYLIAPP----------EELLERLKKLL-----PYTTSGPSTLSQAAAAA 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410579 315 ALKQAMTlEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLrSKGTDGGRAEKVLEACSIACNKntcPGDRS 394
Cdd:cd00609  249 ALDDGEE-HLEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDL-PEGDDEEFLERLLLEAGVVVRP---GSAFG 323

                        250
                 ....*....|
gi 530410579 395 ALRPSGLRLG 404
Cdd:cd00609  324 EGGEGFVRLS 333
 
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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