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P09053

- AVTA_ECOLI

UniProt

P09053 - AVTA_ECOLI

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Protein

Valine--pyruvate aminotransferase

Gene

avtA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of alanine.2 Publications

Catalytic activityi

L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine.

Cofactori

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. transaminase activity Source: EcoCyc
  3. valine-pyruvate transaminase activity Source: EcoCyc

GO - Biological processi

  1. cellular amino acid catabolic process Source: EcoCyc
  2. D-alanine biosynthetic process Source: UniProtKB
  3. pyruvate metabolic process Source: EcoCyc
  4. valine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.
ECOL316407:JW5652-MONOMER.
MetaCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Valine--pyruvate aminotransferase (EC:2.6.1.66)
Alternative name(s):
Alanine--valine transaminase
Transaminase C
Gene namesi
Name:avtA
Ordered Locus Names:b3572, JW5652
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10107. avtA.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 417417Valine--pyruvate aminotransferasePRO_0000123941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei249 – 2491N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP09053.
PRIDEiP09053.

Expressioni

Inductioni

Modestly repressed by alanine and leucine via Lrp. Amino acid limitation causes repression by promoting the accumulation of L-alanine or L-leucine or both. AvtA is also repressed by L-alpha-aminobutyric acid and other nonprotein amino acids which are structurally similar to L-alanine.2 Publications

Gene expression databases

GenevestigatoriP09053.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiP09053. 1 interaction.
STRINGi511145.b3572.

Structurei

3D structure databases

ProteinModelPortaliP09053.
SMRiP09053. Positions 15-415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3977.
HOGENOMiHOG000269357.
InParanoidiP09053.
KOiK00835.
OMAiHQCLRMN.
OrthoDBiEOG6QCD62.
PhylomeDBiP09053.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

P09053-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTFSLFGDKF TRHSGITLLM EDLNDGLRTP GAIMLGGGNP AQIPEMQDYF
60 70 80 90 100
QTLLTDMLES GKATDALCNY DGPQGKTELL TLLAGMLREK LGWDIEPQNI
110 120 130 140 150
ALTNGSQSAF FYLFNLFAGR RADGRVKKVL FPLAPEYIGY ADAGLEEDLF
160 170 180 190 200
VSARPNIELL PEGQFKYHVD FEHLHIGEET GMICVSRPTN PTGNVITDEE
210 220 230 240 250
LLKLDALANQ HGIPLVIDNA YGVPFPGIIF SEARPLWNPN IVLCMSLSKL
260 270 280 290 300
GLPGSRCGII IANEKIITAI TNMNGIISLA PGGIGPAMMC EMIKRNDLLR
310 320 330 340 350
LSETVIKPFY YQRVQETIAI IRRYLPENRC LIHKPEGAIF LWLWFKDLPI
360 370 380 390 400
TTKQLYQRLK ARGVLMVPGH NFFPGLDKPW PHTHQCMRMN YVPEPEKIEA
410
GVKILAEEIE RAWAESH
Length:417
Mass (Da):46,711
Last modified:October 11, 2004 - v3
Checksum:i55A0CA53F0E697A2
GO

Sequence cautioni

The sequence CAA68546.1 differs from that shown. Reason: Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081A → G in AAB18549. (PubMed:8041620)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00490 Genomic DNA. Translation: CAA68546.1. Sequence problems.
U00039 Genomic DNA. Translation: AAB18549.1.
U00096 Genomic DNA. Translation: AAT48193.1.
AP009048 Genomic DNA. Translation: BAE77721.1.
PIRiS47793.
RefSeqiYP_026231.1. NC_000913.3.
YP_491862.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAT48193; AAT48193; b3572.
BAE77721; BAE77721; BAE77721.
GeneIDi12930377.
948087.
KEGGiecj:Y75_p3603.
eco:b3572.
PATRICi32122620. VBIEscCol129921_3687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00490 Genomic DNA. Translation: CAA68546.1 . Sequence problems.
U00039 Genomic DNA. Translation: AAB18549.1 .
U00096 Genomic DNA. Translation: AAT48193.1 .
AP009048 Genomic DNA. Translation: BAE77721.1 .
PIRi S47793.
RefSeqi YP_026231.1. NC_000913.3.
YP_491862.1. NC_007779.1.

3D structure databases

ProteinModelPortali P09053.
SMRi P09053. Positions 15-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P09053. 1 interaction.
STRINGi 511145.b3572.

Proteomic databases

PaxDbi P09053.
PRIDEi P09053.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT48193 ; AAT48193 ; b3572 .
BAE77721 ; BAE77721 ; BAE77721 .
GeneIDi 12930377.
948087.
KEGGi ecj:Y75_p3603.
eco:b3572.
PATRICi 32122620. VBIEscCol129921_3687.

Organism-specific databases

EchoBASEi EB0105.
EcoGenei EG10107. avtA.

Phylogenomic databases

eggNOGi COG3977.
HOGENOMi HOG000269357.
InParanoidi P09053.
KOi K00835.
OMAi HQCLRMN.
OrthoDBi EOG6QCD62.
PhylomeDBi P09053.

Enzyme and pathway databases

BioCyci EcoCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.
ECOL316407:JW5652-MONOMER.
MetaCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.

Miscellaneous databases

PROi P09053.

Gene expression databases

Genevestigatori P09053.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Rapid sequencing of cloned DNA using a transposon for bidirectional priming: sequence of the Escherichia coli K-12 avtA gene."
    Liu L., Whalen W., Das A., Berg C.M.
    Nucleic Acids Res. 15:9461-9469(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: SEQUENCE REVISION TO 208.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Transamination in Escherichia coli."
    Rudman D., Meister A.
    J. Biol. Chem. 200:591-604(1953) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN AMINOTRANSFERASE.
  7. "Gratuitous repression of avtA in Escherichia coli and Salmonella typhimurium."
    Whalen W.A., Berg C.M.
    J. Bacteriol. 158:571-574(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Genetics and regulation of the major enzymes of alanine synthesis in Escherichia coli."
    Kim S.H., Schneider B.L., Reitzer L.
    J. Bacteriol. 192:5304-5311(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ALANINE BIOSYNTHESIS, INDUCTION.

Entry informationi

Entry nameiAVTA_ECOLI
AccessioniPrimary (citable) accession number: P09053
Secondary accession number(s): Q2M7N5, Q6BF21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 11, 2004
Last modified: November 26, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3