ID   AAT_RHIML               Reviewed;         410 AA.
AC   Q06191;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000303|PubMed:8320232};
DE            Short=AAT {ECO:0000303|PubMed:8320232};
DE            Short=AspAT {ECO:0000305};
DE            EC=2.6.1.1 {ECO:0000269|PubMed:8320232};
DE   AltName: Full=Transaminase A {ECO:0000305};
GN   Name=aatB {ECO:0000303|PubMed:8320232};
OS   Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC   STRAIN=104A14;
RX   PubMed=8320232; DOI=10.1128/jb.175.13.4186-4196.1993;
RA   Alfano J.R., Kahn M.L.;
RT   "Isolation and characterization of a gene coding for a novel aspartate
RT   aminotransferase from Rhizobium meliloti.";
RL   J. Bacteriol. 175:4186-4196(1993).
CC   -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC       oxoglutarate to glutamate and oxaloacetate.
CC       {ECO:0000269|PubMed:8320232}.
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:0000269|PubMed:8320232};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P58350};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.3 mM for aspartate {ECO:0000269|PubMed:8320232};
CC         KM=0.87 mM for 2-oxoglutarate {ECO:0000269|PubMed:8320232};
CC         Vmax=2.4 umol/min/mg enzyme for oxaloacetate production
CC         {ECO:0000269|PubMed:8320232};
CC       pH dependence:
CC         Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:8320232};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P58350}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Insertion mutant is prototroph and is able to
CC       carry out symbiotic nitrogen fixation. {ECO:0000269|PubMed:8320232}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L12149; AAA71965.1; -; Unassigned_DNA.
DR   PIR; A40658; A40658.
DR   AlphaFoldDB; Q06191; -.
DR   SMR; Q06191; -.
DR   STRING; 382.DU99_17730; -.
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: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   1: Evidence at protein level;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..410
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123849"
FT   BINDING         47
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:P00509"
FT   BINDING         135
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   BINDING         185
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   BINDING         385
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   MOD_RES         249
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P58350"
SQ   SEQUENCE   410 AA;  44454 MW;  F571E8DAC31FFDEA CRC64;
     MTINATVKEA GFRPASRISS IGVSEILKIG ARAAAMKREG KPVIILGAGE PDFDTPDHVK
     QAASDAIHRG ETKYTALDGT PELKKAIREK FQRENGLAYE LDEITVATGA KQILFNAMMA
     SLDPGDEVVI PTPYWTSYSD IVQICEGKPI LIACDASSGF RLTAQKLEAA ITPRTRWVLL
     NSPSNPSGAA YSAADYRPLL DVLLKHPHVW LLVDDMYEHI VYDAFRFVTP ARLEPGLKDR
     TLTVNGVSKA YAMTGWRIGY AGGPRALIKA MAVVQSQATS CPSSVSQAAS VAALNGPQDF
     LKERTESFQR RRNLVVNGLN AIEGLDCRVP EGAFYTFSGC AGVARRVTPS GKRIESDTDF
     CAYLLEDSHV AVVPGSAFGL SPYFRISYAT SEAELKEALE RISAACKRLS