ID   AAPAT_RHILP             Reviewed;         400 AA.
AC   O86459;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable aspartate/prephenate aminotransferase {ECO:0000250|UniProtKB:Q02635};
DE            Short=AspAT / PAT {ECO:0000250|UniProtKB:Q02635};
DE            EC=2.6.1.1 {ECO:0000250|UniProtKB:Q02635};
DE            EC=2.6.1.79 {ECO:0000250|UniProtKB:Q02635};
DE   AltName: Full=Transaminase A;
GN   Name=aspC; Synonyms=aatA;
OS   Rhizobium leguminosarum bv. phaseoli.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8002;
RA   Allaway D.;
RT   "Sequence of an aspartate aminotransferase from Rhizobium leguminosarum.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC       oxoglutarate to glutamate and oxaloacetate. Can also transaminate
CC       prephenate in the presence of glutamate.
CC       {ECO:0000250|UniProtKB:Q02635}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000250|UniProtKB:Q02635};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-arogenate = L-glutamate + prephenate;
CC         Xref=Rhea:RHEA:22880, ChEBI:CHEBI:16810, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58180; EC=2.6.1.79;
CC         Evidence={ECO:0000250|UniProtKB:Q02635};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q02635};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q02635}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q02635}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AJ006709; CAA07198.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86459; -.
DR   SMR; O86459; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033854; F:glutamate-prephenate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..400
FT                   /note="Probable aspartate/prephenate aminotransferase"
FT                   /id="PRO_0000123846"
FT   BINDING         39
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:P00509"
FT   BINDING         125
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   BINDING         175
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   BINDING         375
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   SITE            12
FT                   /note="Important for prephenate aminotransferase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   MOD_RES         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
SQ   SEQUENCE   400 AA;  43752 MW;  1375BE0A72934304 CRC64;
     MAFLADALSR VKPSATIAVS QKARELKAKG RDVIGLGAGE PDFDTPDNIK KAAIDAINRG
     ETKYTPVSGI PELRKAIAAK FKRENGLDYS WEQTIVGTGG KQILFNAFMA TLNPGDEVSI
     PAPYWVSYPE MVALCGGTRF FVSATQEHNF KLQAADLEKA ITPKTKWFIF NSPSNPTGAA
     YTHDELKALT DVLMKNPQVW VLTDDMYEHL TYGDFKFVTP VEVEPQLYDR TLTMNGVSKA
     YAMTGWRIGY AAGPIQLIKA MDMIQGQQTS GATSIAQWAA VEALNGTQDF IPENKKIFEG
     RRDLVVSMLN QAKGIVCPVP EGAFYVYPSC KGLIGKTAPS GKVIETDEDF VSELLESEGV
     AVVHGSAFGL GPNFRISYAT SEEQLEEACR RIQRFCGACK