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1AAT

OXOGLUTARATE-INDUCED CONFORMATIONAL CHANGES IN CYTOSOLIC ASPARTATE AMINOTRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0004609molecular_functionphosphatidylserine decarboxylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006103biological_process2-oxoglutarate metabolic process
A0006114biological_processglycerol biosynthetic process
A0006520biological_processamino acid metabolic process
A0006531biological_processaspartate metabolic process
A0006532biological_processaspartate biosynthetic process
A0006533biological_processL-aspartate catabolic process
A0006536biological_processglutamate metabolic process
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0032869biological_processcellular response to insulin stimulus
A0043490biological_processmalate-aspartate shuttle
A0047801molecular_functionL-cysteine transaminase activity
A0051384biological_processresponse to glucocorticoid
A0120554molecular_function2-aminobutanoate transaminase activity
A0170033biological_processL-amino acid metabolic process
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0004609molecular_functionphosphatidylserine decarboxylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006103biological_process2-oxoglutarate metabolic process
B0006114biological_processglycerol biosynthetic process
B0006520biological_processamino acid metabolic process
B0006531biological_processaspartate metabolic process
B0006532biological_processaspartate biosynthetic process
B0006533biological_processL-aspartate catabolic process
B0006536biological_processglutamate metabolic process
B0008483molecular_functiontransaminase activity
B0008652biological_processamino acid biosynthetic process
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0032869biological_processcellular response to insulin stimulus
B0043490biological_processmalate-aspartate shuttle
B0047801molecular_functionL-cysteine transaminase activity
B0051384biological_processresponse to glucocorticoid
B0120554molecular_function2-aminobutanoate transaminase activity
B0170033biological_processL-amino acid metabolic process
Functional Information from PDB Data
site_idOG
Number of Residues5
Details2-OXOGLUTARATE BINDING SITE
ChainResidue
ATRP140
AASN194
AARG386
BTYR70
BARG292

site_idPLP
Number of Residues12
DetailsPYRIDOXAL PHOSPHATE BINDING SITE
ChainResidue
AGLY107
AARG266
BTYR70
BSER296
AGLY108
ATHR109
ATRP140
AASP222
ATYR225
ASER255
ASER257
ALYS258

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKnfGLyNERVG
ChainResidueDetails
ASER255-GLY268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"499525","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP140
AASP222

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP140
BASP222

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP140
AASP222
ALYS258

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP140
BASP222
BLYS258

246704

PDB entries from 2025-12-24

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