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Conserved domains on  [gi|1598816386|gb|TEH13995|]
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aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme, partial [Pseudomonas aeruginosa]

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) ...
 1-230 2.72e-172

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: 480.22  E-value: 2.72e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386   1 MFSKHDQIRGYDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAID 80
Cdd:PRK13034    2 MFFFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  81 RARQLFGADYANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGAKVSSSGKLYNAVQYGLDTATGLIDYDEVE 160
Cdd:PRK13034   82 RAKQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386 161 RLAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:PRK13034  162 ELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHK 231
 
Name Accession Description Interval E-value
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
 1-230 2.72e-172

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 480.22  E-value: 2.72e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386   1 MFSKHDQIRGYDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAID 80
Cdd:PRK13034    2 MFFFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  81 RARQLFGADYANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGAKVSSSGKLYNAVQYGLDTATGLIDYDEVE 160
Cdd:PRK13034   82 RAKQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386 161 RLAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:PRK13034  162 ELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHK 231
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 5-230 1.97e-167

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: 467.58  E-value: 1.97e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386   5 HDQIRGYDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQ 84
Cdd:COG0112     2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  85 LFGADYANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGAKVSSSGKLYNAVQYGLDTATGLIDYDEVERLAV 164
Cdd:COG0112    82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1598816386 165 EHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:COG0112   162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHK 227
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 11-230 5.09e-131

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: 375.00  E-value: 5.09e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  11 YDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQLFGADY 90
Cdd:cd00378     3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  91 ANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGA--KVSSSGKLYNAVQYGLDTATGLIDYDEVERLAVEHKP 168
Cdd:cd00378    83 ANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSftKVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1598816386 169 KMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:cd00378   163 KLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHK 224
SHMT pfam00464
Serine hydroxymethyltransferase;
11-230 3.52e-128

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 367.54  E-value: 3.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  11 YDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQLFGAD- 89
Cdd:pfam00464   4 SDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  90 ---YANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGAKV-----SSSGKLYNAVQYGLDTATGLIDYDEVER 161
Cdd:pfam00464  84 akwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVnskkiSASSKFFESMPYGVDPETGYIDYDQLEK 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1598816386 162 LAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:pfam00464 164 NAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHK 232
 
Name Accession Description Interval E-value
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
 1-230 2.72e-172

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 480.22  E-value: 2.72e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386   1 MFSKHDQIRGYDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAID 80
Cdd:PRK13034    2 MFFFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  81 RARQLFGADYANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGAKVSSSGKLYNAVQYGLDTATGLIDYDEVE 160
Cdd:PRK13034   82 RAKQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386 161 RLAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:PRK13034  162 ELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHK 231
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 4-230 4.44e-169

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 471.87  E-value: 4.44e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386   4 KHDQIRGYDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRAR 83
Cdd:PRK00011    2 FMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  84 QLFGADYANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGAKVSSSGKLYNAVQYGLDTATGLIDYDEVERLA 163
Cdd:PRK00011   82 ELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1598816386 164 VEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:PRK00011  162 LEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHK 228
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 5-230 1.97e-167

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: 467.58  E-value: 1.97e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386   5 HDQIRGYDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQ 84
Cdd:COG0112     2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  85 LFGADYANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGAKVSSSGKLYNAVQYGLDTATGLIDYDEVERLAV 164
Cdd:COG0112    82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1598816386 165 EHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:COG0112   162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHK 227
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 11-230 5.09e-131

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: 375.00  E-value: 5.09e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  11 YDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQLFGADY 90
Cdd:cd00378     3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  91 ANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGA--KVSSSGKLYNAVQYGLDTATGLIDYDEVERLAVEHKP 168
Cdd:cd00378    83 ANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSftKVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1598816386 169 KMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:cd00378   163 KLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHK 224
SHMT pfam00464
Serine hydroxymethyltransferase;
11-230 3.52e-128

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 367.54  E-value: 3.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  11 YDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQLFGAD- 89
Cdd:pfam00464   4 SDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  90 ---YANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHGAKV-----SSSGKLYNAVQYGLDTATGLIDYDEVER 161
Cdd:pfam00464  84 akwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVnskkiSASSKFFESMPYGVDPETGYIDYDQLEK 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1598816386 162 LAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:pfam00464 164 NAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHK 232
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
 1-230 4.36e-109

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 320.78  E-value: 4.36e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386   1 MFSKHDQIRGYDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAID 80
Cdd:PTZ00094    8 VLPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  81 RARQLFGADY----ANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHG-----AKVSSSGKLYNAVQYGLDtAT 151
Cdd:PTZ00094   88 RALEAFGLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVN-EK 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1598816386 152 GLIDYDEVERLAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:PTZ00094  167 GLIDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHK 245
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 12-230 2.67e-103

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 306.91  E-value: 2.67e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  12 DDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQLFGADYA 91
Cdd:PLN03226   19 DPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFRLDPE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  92 ----NVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHG-----AKVSSSGKLYNAVQYGLDTATGLIDYDEVERL 162
Cdd:PLN03226   99 kwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgKKISATSIYFESMPYRLDESTGLIDYDKLEKK 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1598816386 163 AVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:PLN03226  179 AMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHK 246
PRK13580 PRK13580
glycine hydroxymethyltransferase;
6-230 7.03e-94

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 283.47  E-value: 7.03e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386   6 DQIRGYDDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQL 85
Cdd:PRK13580   28 DVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKEL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  86 FGADYANVQPHSGSSANAAVYLALLNA------------------------------GD-TILGMSLAHGGHLTHGAKVS 134
Cdd:PRK13580  108 FGAEHAYVQPHSGADANLVAFWAILAHkvespaleklgaktvndlteedwealraelGNqRLLGMSLDSGGHLTHGFRPN 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386 135 SSGKLYNAVQYGLDTATGLIDYDEVERLAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLY 214
Cdd:PRK13580  188 ISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVF 267

                         250
                  ....*....|....*....
gi 1598816386 215 P---NPIPFADVVTTTTHK 230
Cdd:PRK13580  268 TgdeDPVPHADIVTTTTHK 286
PLN02271 PLN02271
serine hydroxymethyltransferase
 12-230 2.41e-75

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 238.17  E-value: 2.41e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  12 DDELLAAMDAEEARQEDHLELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIDRARQLFGADYA 91
Cdd:PLN02271  133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSE 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  92 ----NVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHLTHG------AKVSSSGKLYNAVQYGLDTATGLIDYDEVER 161
Cdd:PLN02271  213 kwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyytpggKKVSGASIFFESLPYKVNPQTGYIDYDKLEE 292

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1598816386 162 LAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:PLN02271  293 KALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHK 361
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 75-230 9.67e-22

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: 87.82  E-value: 9.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  75 EQLAIDRARQLF--GADYANVQPhSGSSANAAVYLALLNAGDTILGMSLAHGGHltHGAKVSSSGKLYNAVQYGLDTAtG 152
Cdd:cd01494     2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSR--YWVAAELAGAKPVPVPVDDAGY-G 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386 153 LIDYDEVERLAVEHKPKMIVAGFSAYSKTL--DFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHK 230
Cdd:cd01494    78 GLDVAILEELKAKPNVALIVITPNTTSGGVlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHK 157
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 78-230 4.85e-07

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 49.17  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  78 AIDRARQLFGADYANVQPHSGSSANAAVYLALLNAGDTILGMSLAHGGHlTHGAKVSSSGKLY--NAVQYGLDTATGlID 155
Cdd:cd00615    64 AQELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSV-INGLVLSGAVPVYlkPERNPYYGIAGG-IP 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1598816386 156 YDEVERLAVEHK-PKMIVAGFSAYSKTL-DFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPF--ADVVTTTTHK 230
Cdd:cd00615   142 PETFKKALIEHPdAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSSAAMagADIVVQSTHK 220
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
65-222 7.67e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 45.76  E-value: 7.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  65 YGGCEHVDKVEQLAIDRARQLFGADY---ANVQPHSGSSAN-AAVYLALLNAGDTILGMSLAHGGHLT----HGAKVSSs 136
Cdd:pfam00155  35 YGPTDGHPELREALAKFLGRSPVLKLdreAAVVFGSGAGANiEALIFLLANPGDAILVPAPTYASYIRiarlAGGEVVR- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386 137 gklYNAvqygLDTATGLIDYDEVERlAVEHKPKMIVAGfSAYSKT-LDFPR-----FRAIADKVGALLFVDMAHVAGLVA 210
Cdd:pfam00155 114 ---YPL----YDSNDFHLDFDALEA-ALKEKPKVVLHT-SPHNPTgTVATLeelekLLDLAKEHNILLLVDEAYAGFVFG 184

                         170
                  ....*....|..
gi 1598816386 211 AGLYPNPIPFAD 222
Cdd:pfam00155 185 SPDAVATRALLA 196
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 97-222 1.82e-05

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: 44.64  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  97 SGSS-ANAAVYLALLNAGDTILGMSLAHGGHLT----HGAKVsssgklynaVQYGLDTATGLIDYDEVERLAVEHKPKMI 171
Cdd:cd00609    66 NGAQeALSLLLRALLNPGDEVLVPDPTYPGYEAaarlAGAEV---------VPVPLDEEGGFLLDLELLEAAKTPKTKLL 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1598816386 172 V-------AGfsaysKTLDFPRFRAIAD---KVGALLFVDMAHvAGLVAAGLYPNPIPFAD 222
Cdd:cd00609   137 YlnnpnnpTG-----AVLSEEELEELAElakKHGILIISDEAY-AELVYDGEPPPALALLD 191
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 96-209 4.30e-05

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 43.70  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  96 HSGSSANAAVYLALLNAGDTILGMSLAHGGhLTHGAKVSSSGKL---YNavqygldtatgliDYDEVERLAVE----HKP 168
Cdd:cd06454    68 SSGYAANDGVLSTLAGKGDLIISDSLNHAS-IIDGIRLSGAKKRifkHN-------------DMEDLEKLLREarrpYGK 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1598816386 169 KMIVAGfSAYSKTLDF---PRFRAIADKVGALLFVDMAHVAGLV 209
Cdd:cd06454   134 KLIVTE-GVYSMDGDIaplPELVDLAKKYGAILFVDEAHSVGVY 176
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 97-224 2.39e-04

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 41.42  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598816386  97 SGSSANAAVYLALLNAGDTILGMSLAHGGhlTHgakvsssgKLYNAVQYGLDTATGLIDYDEVERL--AVEHKPKMIvag 174
Cdd:cd00614    63 SGMAAISTVLLALLKAGDHVVASDDLYGG--TY--------RLFERLLPKLGIEVTFVDPDDPEALeaAIKPETKLV--- 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1598816386 175 F-----SAYSKTLDFPRFRAIADKVGALLFVDmahvaGLVAAGLYPNPIPF-ADVV 224
Cdd:cd00614   130 YvesptNPTLKVVDIEAIAELAHEHGALLVVD-----NTFATPYLQRPLELgADIV 180
 
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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