ID   ALAA_ECOLI              Reviewed;         405 AA.
AC   P0A959; P77727;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=Glutamate-pyruvate aminotransferase AlaA;
DE            EC=2.6.1.2 {ECO:0000269|PubMed:20729367};
GN   Name=alaA {ECO:0000303|PubMed:20729367, ECO:0000303|PubMed:25014014};
GN   Synonyms=yfbQ {ECO:0000303|PubMed:20729367};
GN   OrderedLocusNames=b2290, JW2287;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION IN ALANINE BIOSYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, INDUCTION, AND NOMENCLATURE.
RX   PubMed=20729367; DOI=10.1128/jb.00738-10;
RA   Kim S.H., Schneider B.L., Reitzer L.;
RT   "Genetics and regulation of the major enzymes of alanine synthesis in
RT   Escherichia coli.";
RL   J. Bacteriol. 192:5304-5311(2010).
RN   [5] {ECO:0007744|PDB:4CVQ}
RP   X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP   AND A SUBSTRATE-MIMICKING ACETATE MOLECULE, SUBUNIT, AND COFACTOR.
RX   PubMed=25014014; DOI=10.1371/journal.pone.0102139;
RA   Pena-Soler E., Fernandez F.J., Lopez-Estepa M., Garces F., Richardson A.J.,
RA   Quintana J.F., Rudd K.E., Coll M., Vega M.C.;
RT   "Structural analysis and mutant growth properties reveal distinctive
RT   enzymatic and cellular roles for the three major L-alanine transaminases of
RT   Escherichia coli.";
RL   PLoS ONE 9:e102139-e102139(2014).
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:0000269|PubMed:20729367}.
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:0000269|PubMed:20729367};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19455;
CC         Evidence={ECO:0000269|PubMed:20729367};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:25014014, ECO:0000305|PubMed:20729367};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.55 mM for pyruvate (at 37 degrees Celsius and pH 8.5)
CC         {ECO:0000269|PubMed:20729367};
CC         KM=4.9 mM for alanine (at 37 degrees Celsius and pH 8.5)
CC         {ECO:0000269|PubMed:20729367};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-alanine biosynthesis.
CC       {ECO:0000269|PubMed:20729367}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20729367,
CC       ECO:0000269|PubMed:25014014}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Modestly repressed by alanine and leucine via Lrp.
CC       {ECO:0000269|PubMed:20729367}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U00096; AAC75350.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16127.1; -; Genomic_DNA.
DR   PIR; H65000; H65000.
DR   RefSeq; NP_416793.1; NC_000913.3.
DR   RefSeq; WP_000074527.1; NZ_STEB01000008.1.
DR   PDB; 4CVQ; X-ray; 2.11 A; A/B=1-405.
DR   PDBsum; 4CVQ; -.
DR   AlphaFoldDB; P0A959; -.
DR   SMR; P0A959; -.
DR   BioGRID; 4262970; 9.
DR   DIP; DIP-11970N; -.
DR   IntAct; P0A959; 11.
DR   STRING; 511145.b2290; -.
DR   jPOST; P0A959; -.
DR   PaxDb; 511145-b2290; -.
DR   EnsemblBacteria; AAC75350; AAC75350; b2290.
DR   GeneID; 75205664; -.
DR   GeneID; 946772; -.
DR   KEGG; ecj:JW2287; -.
DR   KEGG; eco:b2290; -.
DR   PATRIC; fig|1411691.4.peg.4445; -.
DR   EchoBASE; EB3854; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   InParanoid; P0A959; -.
DR   OMA; CALDLCI; -.
DR   OrthoDB; 9803354at2; -.
DR   PhylomeDB; P0A959; -.
DR   BioCyc; EcoCyc:G7184-MONOMER; -.
DR   BioCyc; MetaCyc:G7184-MONOMER; -.
DR   BRENDA; 2.6.1.2; 2026.
DR   SABIO-RK; P0A959; -.
DR   UniPathway; UPA00133; -.
DR   PRO; PR:P0A959; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR   GO; GO:0008483; F:transaminase activity; IMP:EcoliWiki.
DR   GO; GO:0006523; P:alanine biosynthetic process; IMP:EcoliWiki.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IMP:EcoCyc.
DR   GO; GO:0019272; P:L-alanine biosynthetic process from pyruvate; IMP:EcoCyc.
DR   GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..405
FT                   /note="Glutamate-pyruvate aminotransferase AlaA"
FT                   /id="PRO_0000123866"
FT   BINDING         41
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000305|PubMed:25014014,
FT                   ECO:0007744|PDB:4CVQ"
FT   BINDING         179
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000305|PubMed:25014014,
FT                   ECO:0007744|PDB:4CVQ"
FT   BINDING         378
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000305|PubMed:25014014,
FT                   ECO:0007744|PDB:4CVQ"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:25014014,
FT                   ECO:0007744|PDB:4CVQ"
FT   HELIX           8..10
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           20..30
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           52..61
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           75..86
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           104..113
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          121..127
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           130..138
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           158..163
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          169..177
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   TURN            179..181
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           187..199
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   TURN            209..212
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           223..226
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          232..238
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   TURN            239..242
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          250..256
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           259..261
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           262..274
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           281..284
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           285..290
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           297..300
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           305..319
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          329..334
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           340..343
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           348..359
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           366..369
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   STRAND          372..380
FT                   /evidence="ECO:0007829|PDB:4CVQ"
FT   HELIX           385..400
FT                   /evidence="ECO:0007829|PDB:4CVQ"
SQ   SEQUENCE   405 AA;  45517 MW;  6A5E78876CC3C388 CRC64;
     MSPIEKSSKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA PDEILVDVIR
     NLPTAQGYCD SKGLYSARKA IMQHYQARGM RDVTVEDIYI GNGVSELIVQ AMQALLNSGD
     EMLVPAPDYP LWTAAVSLSS GKAVHYLCDE SSDWFPDLDD IRAKITPRTR GIVIINPNNP
     TGAVYSKELL MEIVEIARQH NLIIFADEIY DKILYDDAEH HSIAPLAPDL LTITFNGLSK
     TYRVAGFRQG WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI
     TPGGRLYEQR NRAWELINDI PGVSCVKPRG ALYMFPKIDA KRFNIHDDQK MVLDFLLQEK
     VLLVQGTAFN WPWPDHFRIV TLPRVDDIEL SLSKFARFLS GYHQL
//