ID   ALAA_HAEIN              Reviewed;         404 AA.
AC   P71348;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Glutamate-pyruvate aminotransferase AlaA;
DE            EC=2.6.1.2 {ECO:0000250|UniProtKB:P0A959};
GN   Name=alaA; OrderedLocusNames=HI_0286;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Involved in the biosynthesis of alanine. Catalyzes the
CC       transamination of pyruvate by glutamate, leading to the formation of L-
CC       alanine and 2-oxoglutarate. Is also able to catalyze the reverse
CC       reaction. {ECO:0000250|UniProtKB:P0A959}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC         Evidence={ECO:0000250|UniProtKB:P0A959};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19455;
CC         Evidence={ECO:0000250|UniProtKB:P0A959};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P0A959};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-alanine biosynthesis.
CC       {ECO:0000250|UniProtKB:P0A959}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A959}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L42023; AAC21948.1; -; Genomic_DNA.
DR   RefSeq; NP_438453.1; NC_000907.1.
DR   AlphaFoldDB; P71348; -.
DR   SMR; P71348; -.
DR   STRING; 71421.HI_0286; -.
DR   EnsemblBacteria; AAC21948; AAC21948; HI_0286.
DR   KEGG; hin:HI_0286; -.
DR   PATRIC; fig|71421.8.peg.302; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   OrthoDB; 9803354at2; -.
DR   PhylomeDB; P71348; -.
DR   BioCyc; HINF71421:G1GJ1-304-MONOMER; -.
DR   UniPathway; UPA00133; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; ISS:UniProtKB.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..404
FT                   /note="Glutamate-pyruvate aminotransferase AlaA"
FT                   /id="PRO_0000123869"
FT   BINDING         41
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000250|UniProtKB:P0A959"
FT   BINDING         179
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000250|UniProtKB:P0A959"
FT   BINDING         378
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000250|UniProtKB:P0A959"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A959"
SQ   SEQUENCE   404 AA;  45160 MW;  7F2C3E24CC69FB46 CRC64;
     MRLFPKSDKL EHVCYDIRGP VHKEALRLEE EGNKILKLNI GNPAPFGFEA PDEILVDVLR
     NLPSAQGYCD SKGLYSARKA IVQYYQSKGI LGATVNDVYI GNGVSELITM AMQALLNDGD
     EVLVPMPDYP LWTAAVTLSG GKAVHYLCDE DANWFPTIDD IKAKVNAKTK AIVIINPNNP
     TGAVYSKELL QEIVEIARQN NLIIFADEIY DKILYDGAVH HHIAALAPDL LTVTLNGLSK
     AYRVAGFRQG WMILNGPKHN AKGYIEGLDM LASMRLCANV PMQHAIQTAL GGYQSINEFI
     LPGGRLLEQR NKAYDLITQI PGITCVKPMG AMYMFPKIDV KKFNIHSDEK MVLDLLRQEK
     VLLVHGKGFN WHSPDHFRIV TLPYVNQLEE AITKLARFLS DYRQ
//