ALAC_ECOLI
ID ALAC_ECOLI Reviewed; 412 AA.
AC P77434;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Glutamate-pyruvate aminotransferase AlaC;
DE EC=2.6.1.2 {ECO:0000269|PubMed:20729367};
GN Name=alaC {ECO:0000303|PubMed:20729367};
GN Synonyms=yfdZ {ECO:0000303|PubMed:20729367};
GN OrderedLocusNames=b2379, JW2376;
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 INDUCTION BY SGRR.
RX PubMed=17209026; DOI=10.1128/jb.01689-06;
RA Vanderpool C.K., Gottesman S.;
RT "The novel transcription factor SgrR coordinates the response to glucose-
RT phosphate stress.";
RL J. Bacteriol. 189:2238-2248(2007).
RN [5]
RP FUNCTION IN ALANINE BIOSYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, SUBUNIT, INDUCTION, NOMENCLATURE, AND PATHWAY.
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 [6]
RP FUNCTION IN ALANINE BIOSYNTHESIS.
RX PubMed=21597182; DOI=10.1271/bbb.100905;
RA Yoneyama H., Hori H., Lim S.J., Murata T., Ando T., Isogai E.,
RA Katsumata R.;
RT "Isolation of a mutant auxotrophic for L-alanine and identification of
RT three major aminotransferases that synthesize L-alanine in Escherichia
RT coli.";
RL Biosci. Biotechnol. Biochem. 75:930-938(2011).
CC -!- FUNCTION: Involved in the biosynthesis of alanine (PubMed:20729367).
CC Catalyzes the transamination of pyruvate by glutamate, leading to the
CC formation of L-alanine and 2-oxoglutarate. Is also able to catalyze the
CC reverse reaction (PubMed:20729367). {ECO:0000269|PubMed:20729367,
CC ECO:0000269|PubMed:21597182}.
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:0000305|PubMed:20729367};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.94 mM for pyruvate (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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Activated by SgrR and modestly repressed by alanine and
CC leucine via Lrp. {ECO:0000269|PubMed:17209026,
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; AAC75438.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16249.1; -; Genomic_DNA.
DR PIR; H65011; H65011.
DR RefSeq; NP_416880.1; NC_000913.3.
DR RefSeq; WP_000785931.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P77434; -.
DR SMR; P77434; -.
DR BioGRID; 4260931; 48.
DR BioGRID; 851191; 3.
DR DIP; DIP-12010N; -.
DR IntAct; P77434; 8.
DR STRING; 511145.b2379; -.
DR jPOST; P77434; -.
DR PaxDb; P77434; -.
DR PRIDE; P77434; -.
DR EnsemblBacteria; AAC75438; AAC75438; b2379.
DR EnsemblBacteria; BAA16249; BAA16249; BAA16249.
DR GeneID; 66673750; -.
DR GeneID; 946850; -.
DR KEGG; ecj:JW2376; -.
DR KEGG; eco:b2379; -.
DR PATRIC; fig|1411691.4.peg.4349; -.
DR EchoBASE; EB3950; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_6; -.
DR InParanoid; P77434; -.
DR OMA; YPHMPTG; -.
DR PhylomeDB; P77434; -.
DR BioCyc; EcoCyc:G7242-MON; -.
DR BioCyc; MetaCyc:G7242-MON; -.
DR SABIO-RK; P77434; -.
DR UniPathway; UPA00133; -.
DR PRO; PR:P77434; -.
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:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IGI:EcoliWiki.
DR GO; GO:0006523; P:alanine biosynthetic process; IGI:EcoliWiki.
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 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 Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..412
FT /note="Glutamate-pyruvate aminotransferase AlaC"
FT /id="PRO_0000123926"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 412 AA; 46216 MW; F0F62F84344E588E CRC64;
MADTRPERRF TRIDRLPPYV FNITAELKMA ARRRGEDIID FSMGNPDGAT PPHIVEKLCT
VAQRPDTHGY STSRGIPRLR RAISRWYQDR YDVEIDPESE AIVTIGSKEG LAHLMLATLD
HGDTVLVPNP SYPIHIYGAV IAGAQVRSVP LVEGVDFFNE LERAIRESYP KPKMMILGFP
SNPTAQCVEL EFFEKVVALA KRYDVLVVHD LAYADIVYDG WKAPSIMQVP GARDVAVEFF
TLSKSYNMAG WRIGFMVGNK TLVSALARIK SYHDYGTFTP LQVAAIAALE GDQQCVRDIA
EQYKRRRDVL VKGLHEAGWM VEMPKASMYV WAKIPEPYAA MGSLEFAKKL LNEAKVCVSP
GIGFGDYGDT HVRFALIENR DRIRQAIRGI KAMFRADGLL PASSKHIHEN AE
