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1BJW

ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0005737cellular_componentcytoplasm
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033853molecular_functionaspartate-prephenate aminotransferase activity
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0005737cellular_componentcytoplasm
B0006520biological_processamino acid metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0033853molecular_functionaspartate-prephenate aminotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 414
ChainResidue
AGLY39
ATRP125
AASN175
ATYR322
AARG361
AHOH558
AHOH607

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 414
ChainResidue
BTYR322
BARG361
BTRP125
BASN175

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GAAKafAMtGWRIG
ChainResidueDetails
AGLY231-GLY244

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1GCK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Important for prephenate aminotransferase activity","evidences":[{"source":"PubMed","id":"30771275","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10029535","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11432784","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1B5P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BJ4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR124
AASP203

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BALA68

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR124
BASP203

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AALA68

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP125
AASP203

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP125
BASP203

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP203
ATYR128

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP203
BTYR128

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PDB entries from 2025-12-24

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