ID   AAT_STRGR               Reviewed;         213 AA.
AC   P36692;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
DE   Flags: Fragment;
GN   Name=aspC; Synonyms=aatA;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N2-3-11;
RX   PubMed=8039667; DOI=10.1111/j.1574-6968.1994.tb06863.x;
RA   Kuberski S., Kasberg T., Distler J.;
RT   "The nusG gene of Streptomyces griseus: cloning of the gene and analysis of
RT   the A-factor binding properties of the gene product.";
RL   FEMS Microbiol. Lett. 119:33-39(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RC   STRAIN=IFO 13350 / CBS 651.72;
RX   PubMed=8286423;
RA   Miyake K., Onaka H., Horinouchi S., Beppu T.;
RT   "Organization and nucleotide sequence of the secE-nusG region of
RT   Streptomyces griseus.";
RL   Biochim. Biophys. Acta 1217:97-100(1994).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; X72787; CAA51294.1; -; Genomic_DNA.
DR   EMBL; D17464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S41059; S41059.
DR   AlphaFoldDB; P36692; -.
DR   SMR; P36692; -.
DR   STRING; 1911.GCA_001715295_02340; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
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.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..>213
FT                   /note="Probable aspartate aminotransferase"
FT                   /id="PRO_0000123852"
FT   BINDING         47
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   NON_TER         213
SQ   SEQUENCE   213 AA;  22694 MW;  C380BF59DA55A429 CRC64;
     MSAATSPSER RVSARIGAIS ESATLAVDAK AKALKAAGRP VIGFGAGEPD FPTPDYIVDA
     AVEACRNPKY HRYTPQRAPE LKAAIAEKTL RDSGYEVDAG QILVTNGGKQ AIYEAFAAIL
     DPGDEVIVPA PYWTTYPESI RLAGGVPVEV VADETTGYRV SVEQLEAART EKTKVVLFVS
     PSNPTGAVYS EADAEAIGRW AVEHGLWVMT DEI