P09053 (AVTA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Valine--pyruvate aminotransferase
EC=2.6.1.66

Alternative name(s):
Alanine--valine transaminase
Transaminase C

Gene names

Name:	avtA
Ordered Locus Names:	b3572, JW5652

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biosynthesis of alanine. Ref.6 Ref.8
Catalytic activity	L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Induction	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. Ref.7 Ref.8
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Sequence caution	The sequence CAA68546.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame. The sequence CAA68546.1 differs from that shown. Reason:

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	D-alanine biosynthetic process Inferred from mutant phenotype Ref.8. Source: UniProtKB cellular amino acid catabolic process Inferred from experiment Ref.6. Source: EcoCyc pyruvate metabolic process Inferred from experiment PubMed 4616947. Source: EcoCyc valine biosynthetic process Inferred from experiment Ref.6. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro valine-pyruvate transaminase activity Inferred from direct assay PubMed 4616947. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 417	417	Valine--pyruvate aminotransferase		PRO_0000123941
Amino acid modifications
	Modified residue	249	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	208	1	A → G in AAB18549. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P09053 [UniParc]. Last modified October 11, 2004. Version 3. Checksum: 55A0CA53F0E697A2	FASTA	417	46,711
	10 20 30 40 50 60 MTFSLFGDKF TRHSGITLLM EDLNDGLRTP GAIMLGGGNP AQIPEMQDYF QTLLTDMLES 70 80 90 100 110 120 GKATDALCNY DGPQGKTELL TLLAGMLREK LGWDIEPQNI ALTNGSQSAF FYLFNLFAGR 130 140 150 160 170 180 RADGRVKKVL FPLAPEYIGY ADAGLEEDLF VSARPNIELL PEGQFKYHVD FEHLHIGEET 190 200 210 220 230 240 GMICVSRPTN PTGNVITDEE LLKLDALANQ HGIPLVIDNA YGVPFPGIIF SEARPLWNPN 250 260 270 280 290 300 IVLCMSLSKL GLPGSRCGII IANEKIITAI TNMNGIISLA PGGIGPAMMC EMIKRNDLLR 310 320 330 340 350 360 LSETVIKPFY YQRVQETIAI IRRYLPENRC LIHKPEGAIF LWLWFKDLPI TTKQLYQRLK 370 380 390 400 410 ARGVLMVPGH NFFPGLDKPW PHTHQCMRMN YVPEPEKIEA GVKILAEEIE RAWAESH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005." Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L. Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S47793.
RefSeq	YP_026231.1. NC_000913.2. YP_491862.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P09053.
SMR	P09053. Positions 15-415.
ModBase	Search...
Protein-protein interaction databases
IntAct	P09053. 1 interaction.
STRING	511145.b3572.
Proteomic databases
PaxDb	P09053.
PRIDE	P09053.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT48193; AAT48193; b3572. BAE77721; BAE77721; BAE77721.
GeneID	12930377. 948087.
KEGG	ecj:Y75_p3603. eco:b3572.
PATRIC	32122620. VBIEscCol129921_3687.
Organism-specific databases
EchoBASE	EB0105.
EcoGene	EG10107. avtA.
Phylogenomic databases
eggNOG	COG3977.
HOGENOM	HOG000269357.
KO	K00835.
OMA	HQCLRMN.
ProtClustDB	PRK09440.
Enzyme and pathway databases
BioCyc	EcoCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER. ECOL316407:JW5652-MONOMER. MetaCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.
Gene expression databases
Genevestigator	P09053.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AVTA_ECOLI

Accession

Primary (citable) accession number: P09053
Secondary accession number(s): Q2M7N5, Q6BF21

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program