ALAA_ECOLI
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 03-AUG-2022, entry version 119.
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; Proteobacteria; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; P0A959; -.
DR PRIDE; P0A959; -.
DR EnsemblBacteria; AAC75350; AAC75350; b2290.
DR EnsemblBacteria; BAA16127; BAA16127; BAA16127.
DR GeneID; 66673827; -.
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; WRMGWII; -.
DR PhylomeDB; P0A959; -.
DR BioCyc; EcoCyc:G7184-MON; -.
DR BioCyc; MetaCyc:G7184-MON; -.
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: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:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019272; P:L-alanine biosynthetic process from pyruvate; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
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 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
