ALAA_HAEIN
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 03-AUG-2022, entry version 122.
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; Proteobacteria; 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 RefSeq; WP_005694022.1; 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 OMA; WRMGWII; -.
DR PhylomeDB; P71348; -.
DR BioCyc; HINF71421:G1GJ1-304-MON; -.
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 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 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