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Conserved domains on  [gi|1147708167|dbj|BAW98523|]
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serine hydroxymethyltransferase, partial [Sulfurimonas sp. M59]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 1-215 1.72e-151

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).


The actual alignment was detected with superfamily member PRK13034:

Pssm-ID: 450240  Cd Length: 416  Bit Score: 426.68  E-value: 1.72e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGSKPSFSGKNYSSFTYGV-ELDGRINYDRVLDIAKIVHPKII 79
Cdd:PRK13034   93 NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVdRLTGLIDYDEVEELAKEHKPKLI 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  80 VCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTNDEDIAKKI 159
Cdd:PRK13034  173 IAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNDEEIAKKI 252

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147708167 160 NSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:PRK13034  253 NSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYD 308
 
Name Accession Description Interval E-value
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
 1-215 1.72e-151

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 426.68  E-value: 1.72e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGSKPSFSGKNYSSFTYGV-ELDGRINYDRVLDIAKIVHPKII 79
Cdd:PRK13034   93 NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVdRLTGLIDYDEVEELAKEHKPKLI 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  80 VCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTNDEDIAKKI 159
Cdd:PRK13034  173 IAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNDEEIAKKI 252

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147708167 160 NSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:PRK13034  253 NSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYD 308
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 1-215 2.52e-128

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: 367.82  E-value: 2.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGSKPSFSGKNYSSFTYGVELD-GRINYDRVLDIAKIVHPKII 79
Cdd:COG0112    89 NVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPEtGLIDYDEVRKLALEHKPKLI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  80 VCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTNdEDIAKKI 159
Cdd:COG0112   169 IAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCN-EELAKKI 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147708167 160 NSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:COG0112   248 DSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFR 303
SHMT pfam00464
Serine hydroxymethyltransferase;
1-215 6.38e-111

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 323.24  E-value: 6.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGS-----KPSFSGKNYSSFTYGVE-LDGRINYDRVLDIAKIV 74
Cdd:pfam00464  89 NVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYpvnskKISASSKFFESMPYGVDpETGYIDYDQLEKNAKLF 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  75 HPKIIVCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTND-- 152
Cdd:pfam00464 169 RPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIFYRKgv 248

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1147708167 153 -----------EDIAKKINSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:pfam00464 249 ksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYK 322
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 1-215 1.30e-107

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: 314.91  E-value: 1.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGS--KPSFSGKNYSSFTYGVELD-GRINYDRVLDIAKIVHPK 77
Cdd:cd00378    84 NVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSftKVSASGKLFESVPYGVDPEtGLIDYDALEKMALEFKPK 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  78 IIVCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTNDEDIAK 157
Cdd:cd00378   164 LIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGELAK 243

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1147708167 158 KINSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:cd00378   244 KINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFK 301
 
Name Accession Description Interval E-value
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
 1-215 1.72e-151

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 426.68  E-value: 1.72e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGSKPSFSGKNYSSFTYGV-ELDGRINYDRVLDIAKIVHPKII 79
Cdd:PRK13034   93 NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVdRLTGLIDYDEVEELAKEHKPKLI 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  80 VCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTNDEDIAKKI 159
Cdd:PRK13034  173 IAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNDEEIAKKI 252

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147708167 160 NSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:PRK13034  253 NSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYD 308
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 1-215 1.62e-132

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 378.65  E-value: 1.62e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGSKPSFSGKNYSSFTYGVELD-GRINYDRVLDIAKIVHPKII 79
Cdd:PRK00011   90 NVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEEtGLIDYDEVEKLALEHKPKLI 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  80 VCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTNDEDIAKKI 159
Cdd:PRK00011  170 IAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNDEELAKKI 249

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147708167 160 NSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:PRK00011  250 NSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFR 305
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 1-215 2.52e-128

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: 367.82  E-value: 2.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGSKPSFSGKNYSSFTYGVELD-GRINYDRVLDIAKIVHPKII 79
Cdd:COG0112    89 NVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPEtGLIDYDEVRKLALEHKPKLI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  80 VCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTNdEDIAKKI 159
Cdd:COG0112   169 IAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCN-EELAKKI 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147708167 160 NSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:COG0112   248 DSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFR 303
SHMT pfam00464
Serine hydroxymethyltransferase;
1-215 6.38e-111

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 323.24  E-value: 6.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGS-----KPSFSGKNYSSFTYGVE-LDGRINYDRVLDIAKIV 74
Cdd:pfam00464  89 NVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYpvnskKISASSKFFESMPYGVDpETGYIDYDQLEKNAKLF 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  75 HPKIIVCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTND-- 152
Cdd:pfam00464 169 RPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIFYRKgv 248

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1147708167 153 -----------EDIAKKINSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:pfam00464 249 ksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYK 322
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 1-215 1.30e-107

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: 314.91  E-value: 1.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHGS--KPSFSGKNYSSFTYGVELD-GRINYDRVLDIAKIVHPK 77
Cdd:cd00378    84 NVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSftKVSASGKLFESVPYGVDPEtGLIDYDALEKMALEFKPK 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  78 IIVCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTNDEDIAK 157
Cdd:cd00378   164 LIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGELAK 243

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1147708167 158 KINSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:cd00378   244 KINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFK 301
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
 1-215 3.36e-96

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 287.26  E-value: 3.36e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHG-----SKPSFSGKNYSSFTYGVELDGRINYDRVLDIAKIVH 75
Cdd:PTZ00094  103 NVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKGLIDYDKLEELAKAFR 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  76 PKIIVCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTN---D 152
Cdd:PTZ00094  183 PKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSGLIFYRkkvK 262

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147708167 153 EDIAKKINSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:PTZ00094  263 PDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYD 325
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 1-214 4.84e-82

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 251.82  E-value: 4.84e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHG-----SKPSFSGKNYSSFTYGVELD-GRINYDRVLDIAKIV 74
Cdd:PLN03226  103 NVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgKKISATSIYFESMPYRLDEStGLIDYDKLEKKAMLF 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  75 HPKIIVCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIM----- 149
Cdd:PLN03226  183 RPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMIFfrkgp 262

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147708167 150 --------TNDEDIAKKINSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGY 214
Cdd:PLN03226  263 kppkgqgeGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKGY 335
PRK13580 PRK13580
glycine hydroxymethyltransferase;
2-213 2.82e-67

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 214.13  E-value: 2.82e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   2 VQPHSGSQANGAVYAALL----------KAG---------------------DKLLGMDLSHGGHLTHGSKPSFSGKNYS 50
Cdd:PRK13580  115 VQPHSGADANLVAFWAILahkvespaleKLGaktvndlteedwealraelgnQRLLGMSLDSGGHLTHGFRPNISGKMFH 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  51 SFTYGVELD-GRINYDRVLDIAKIVHPKIIVCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAG---EHPSPF 126
Cdd:PRK13580  195 QRSYGVDPDtGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKvftGDEDPV 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167 127 PHAHVVTTTTHKTLAGPRGGMIMTNDEdIAKKINSAIfPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLA 206
Cdd:PRK13580  275 PHADIVTTTTHKTLRGPRGGLVLAKKE-YADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALA 352


                  ....*..
gi 1147708167 207 EVLMKRG 213
Cdd:PRK13580  353 EGFLKRG 359
PLN02271 PLN02271
serine hydroxymethyltransferase
 1-212 2.62e-62

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 203.50  E-value: 2.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQANGAVYAALLKAGDKLLGMDLSHGGHLTHG-SKPSfsGKNYS-------SFTYGVE-LDGRINYDRVLDIA 71
Cdd:PLN02271  217 NVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyYTPG--GKKVSgasiffeSLPYKVNpQTGYIDYDKLEEKA 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  72 KIVHPKIIVCGASAYAREIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIM-- 149
Cdd:PLN02271  295 LDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIFyr 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167 150 -----------------TNDEDIAKKINSAIFPALQGGPLVHVIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKR 212
Cdd:PLN02271  375 kgpklrkqgmllshgddNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALLRR 454
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 5-151 5.00e-11

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: 58.93  E-value: 5.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   5 HSGSQANGAVYAALLKAGDKLLGMDLSHGGHltHGSKPSFSGKNYSSFTYGVELDGRINYDRVLDIAKIVHPKIIVCGAS 84
Cdd:cd01494    24 PSGTGANEAALLALLGPGDEVIVDANGHGSR--YWVAAELAGAKPVPVPVDDAGYGGLDVAILEELKAKPNVALIVITPN 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1147708167  85 AYAR--EIDFAKFREIADEVGAILFADIAHIAGLVAAGEHPSPFPHAHVVTTTTHKTLAGPRGGMIMTN 151
Cdd:cd01494   102 TTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGVVIVK 170
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
1-215 2.69e-04

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 41.14  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   1 NVQPHSGSQAN-GAVYAALLKAGDKLLGMDLSHGGHLT----HGSKPsFSGKNYSSFTYGVELDGrinYDRVLDIAKIVh 75
Cdd:pfam00155  65 AVVFGSGAGANiEALIFLLANPGDAILVPAPTYASYIRiarlAGGEV-VRYPLYDSNDFHLDFDA---LEAALKEKPKV- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  76 pkIIVCGAS-----AYAREiDFAKFREIADEVGAILFADIAHIAGlvaAGEHPSPFPHAHVVTTTTHKT----------L 140
Cdd:pfam00155 140 --VLHTSPHnptgtVATLE-ELEKLLDLAKEHNILLLVDEAYAGF---VFGSPDAVATRALLAEGPNLLvvgsfskafgL 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1147708167 141 AGPRGGMIMTNDE--DIAKKINSAIFPALQGGPlvhvIAAKAVGFKHNLSPEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:pfam00155 214 AGWRVGYILGNAAviSQLRKLARPFYSSTHLQA----AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLS 286
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 5-215 2.95e-04

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: 40.79  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167   5 HSGSQANGAVYAALLKAGDKLLGMDLSHGGHLT----HGSKPsfsgknyssftYGVELD---GRINYDRVLDIAKIVHPK 77
Cdd:cd00609    66 NGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAaarlAGAEV-----------VPVPLDeegGFLLDLELLEAAKTPKTK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147708167  78 IIV-------CGAsAYAREiDFAKFREIADEVGAILFADIAHiAGLVAAGEHPSPFPHAHVVTTTT-------HKTLAGP 143
Cdd:cd00609   135 LLYlnnpnnpTGA-VLSEE-ELEELAELAKKHGILIISDEAY-AELVYDGEPPPALALLDAYERVIvlrsfskTFGLPGL 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1147708167 144 RGGMIMTNDEDIAKKINSAIfPALQGGPLVHVIAAKAVGFKHNLSpEWKDYAQQVKKNASVLAEVLMKRGYD 215
Cdd:cd00609   212 RIGYLIAPPEELLERLKKLL-PYTTSGPSTLSQAAAAAALDDGEE-HLEELRERYRRRRDALLEALKELGPL 281
 
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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