AVTA_ECOLI
ID AVTA_ECOLI Reviewed; 417 AA.
AC P09053; Q2M7N5; Q6BF21;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Valine--pyruvate aminotransferase;
DE EC=2.6.1.66;
DE AltName: Full=Alanine--valine transaminase;
DE AltName: Full=Transaminase C;
GN Name=avtA; OrderedLocusNames=b3572, JW5652;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2825136; DOI=10.1093/nar/15.22.9461;
RA Liu L., Whalen W., Das A., Berg C.M.;
RT "Rapid sequencing of cloned DNA using a transposon for bidirectional
RT priming: sequence of the Escherichia coli K-12 avtA gene.";
RL Nucleic Acids Res. 15:9461-9469(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 208.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
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 [6]
RP FUNCTION AS AN AMINOTRANSFERASE.
RX PubMed=13034817; DOI=10.1016/s0021-9258(18)71404-x;
RA Rudman D., Meister A.;
RT "Transamination in Escherichia coli.";
RL J. Biol. Chem. 200:591-604(1953).
RN [7]
RP INDUCTION.
RX PubMed=6373721; DOI=10.1128/jb.158.2.571-574.1984;
RA Whalen W.A., Berg C.M.;
RT "Gratuitous repression of avtA in Escherichia coli and Salmonella
RT typhimurium.";
RL J. Bacteriol. 158:571-574(1984).
RN [8]
RP FUNCTION IN ALANINE BIOSYNTHESIS, AND INDUCTION.
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).
CC -!- FUNCTION: Involved in the biosynthesis of alanine.
CC {ECO:0000269|PubMed:13034817, ECO:0000269|PubMed:20729367}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine;
CC Xref=Rhea:RHEA:22912, ChEBI:CHEBI:11851, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57762, ChEBI:CHEBI:57972; EC=2.6.1.66;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Modestly repressed by alanine and leucine via Lrp. Amino
CC acid limitation causes repression by promoting the accumulation of L-
CC alanine or L-leucine or both. AvtA is also repressed by L-alpha-
CC aminobutyric acid and other nonprotein amino acids which are
CC structurally similar to L-alanine. {ECO:0000269|PubMed:20729367,
CC ECO:0000269|PubMed:6373721}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68546.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=CAA68546.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; Y00490; CAA68546.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00039; AAB18549.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48193.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77721.1; -; Genomic_DNA.
DR PIR; S47793; S47793.
DR RefSeq; WP_000144363.1; NZ_LN832404.1.
DR RefSeq; YP_026231.1; NC_000913.3.
DR AlphaFoldDB; P09053; -.
DR SMR; P09053; -.
DR BioGRID; 4259371; 141.
DR IntAct; P09053; 1.
DR STRING; 511145.b3572; -.
DR jPOST; P09053; -.
DR PaxDb; P09053; -.
DR PRIDE; P09053; -.
DR EnsemblBacteria; AAT48193; AAT48193; b3572.
DR EnsemblBacteria; BAE77721; BAE77721; BAE77721.
DR GeneID; 948087; -.
DR KEGG; ecj:JW5652; -.
DR KEGG; eco:b3572; -.
DR PATRIC; fig|1411691.4.peg.3140; -.
DR EchoBASE; EB0105; -.
DR eggNOG; COG3977; Bacteria.
DR HOGENOM; CLU_053657_0_0_6; -.
DR InParanoid; P09053; -.
DR OMA; HAHQCLR; -.
DR PhylomeDB; P09053; -.
DR BioCyc; EcoCyc:VALINE-PYRUVATE-AMINOTRANSFER-MON; -.
DR BioCyc; MetaCyc:VALINE-PYRUVATE-AMINOTRANSFER-MON; -.
DR BRENDA; 2.6.1.66; 2026.
DR PRO; PR:P09053; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009042; F:valine-pyruvate transaminase activity; IDA:EcoCyc.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..417
FT /note="Valine--pyruvate aminotransferase"
FT /id="PRO_0000123941"
FT MOD_RES 249
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 208
FT /note="A -> G (in Ref. 2; AAB18549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46711 MW; 55A0CA53F0E697A2 CRC64;
MTFSLFGDKF TRHSGITLLM EDLNDGLRTP GAIMLGGGNP AQIPEMQDYF QTLLTDMLES
GKATDALCNY DGPQGKTELL TLLAGMLREK LGWDIEPQNI ALTNGSQSAF FYLFNLFAGR
RADGRVKKVL FPLAPEYIGY ADAGLEEDLF VSARPNIELL PEGQFKYHVD FEHLHIGEET
GMICVSRPTN PTGNVITDEE LLKLDALANQ HGIPLVIDNA YGVPFPGIIF SEARPLWNPN
IVLCMSLSKL GLPGSRCGII IANEKIITAI TNMNGIISLA PGGIGPAMMC EMIKRNDLLR
LSETVIKPFY YQRVQETIAI IRRYLPENRC LIHKPEGAIF LWLWFKDLPI TTKQLYQRLK
ARGVLMVPGH NFFPGLDKPW PHTHQCMRMN YVPEPEKIEA GVKILAEEIE RAWAESH
