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P77434 (ALAC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate-pyruvate aminotransferase AlaC

EC=2.6.1.2
Gene names
Name:alaC
Synonyms:yfdZ
Ordered Locus Names:b2379, JW2376
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of alanine. Ref.5 Ref.6

Catalytic activity

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.

Cofactor

Pyridoxal phosphate Potential.

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm By similarity.

Induction

Activated by SgrR and modestly repressed by alanine and leucine via Lrp. Ref.4 Ref.5

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.94 mM for pyruvate (at 37 degrees Celsius and pH 8.5) Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Glutamate-pyruvate aminotransferase AlaC
PRO_0000123926

Amino acid modifications

Modified residue2441N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P77434 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: F0F62F84344E588E

FASTA41246,216
        10         20         30         40         50         60 
MADTRPERRF TRIDRLPPYV FNITAELKMA ARRRGEDIID FSMGNPDGAT PPHIVEKLCT 

        70         80         90        100        110        120 
VAQRPDTHGY STSRGIPRLR RAISRWYQDR YDVEIDPESE AIVTIGSKEG LAHLMLATLD 

       130        140        150        160        170        180 
HGDTVLVPNP SYPIHIYGAV IAGAQVRSVP LVEGVDFFNE LERAIRESYP KPKMMILGFP 

       190        200        210        220        230        240 
SNPTAQCVEL EFFEKVVALA KRYDVLVVHD LAYADIVYDG WKAPSIMQVP GARDVAVEFF 

       250        260        270        280        290        300 
TLSKSYNMAG WRIGFMVGNK TLVSALARIK SYHDYGTFTP LQVAAIAALE GDQQCVRDIA 

       310        320        330        340        350        360 
EQYKRRRDVL VKGLHEAGWM VEMPKASMYV WAKIPEPYAA MGSLEFAKKL LNEAKVCVSP 

       370        380        390        400        410 
GIGFGDYGDT HVRFALIENR DRIRQAIRGI KAMFRADGLL PASSKHIHEN AE 

« Hide

References

« Hide 'large scale' references
[1]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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.
[4]"The novel transcription factor SgrR coordinates the response to glucose-phosphate stress."
Vanderpool C.K., Gottesman S.
J. Bacteriol. 189:2238-2248(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY SGRR.
[5]"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 AS AN AMINOTRANSFERASE AND IN ALANINE BIOSYNTHESIS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, NOMENCLATURE.
[6]"Isolation of a mutant auxotrophic for L-alanine and identification of three major aminotransferases that synthesize L-alanine in Escherichia coli."
Yoneyama H., Hori H., Lim S.J., Murata T., Ando T., Isogai E., Katsumata R.
Biosci. Biotechnol. Biochem. 75:930-938(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ALANINE BIOSYNTHESIS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC75438.1.
AP009048 Genomic DNA. Translation: BAA16249.1.
PIRH65011.
RefSeqNP_416880.1. NC_000913.3.
YP_490621.1. NC_007779.1.

3D structure databases

ProteinModelPortalP77434.
SMRP77434. Positions 20-399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-12010N.
IntActP77434. 8 interactions.
STRING511145.b2379.

Proteomic databases

PaxDbP77434.
PRIDEP77434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75438; AAC75438; b2379.
BAA16249; BAA16249; BAA16249.
GeneID12931937.
946850.
KEGGecj:Y75_p2346.
eco:b2379.
PATRIC32120137. VBIEscCol129921_2477.

Organism-specific databases

EchoBASEEB3950.
EcoGeneEG14198. alaC.

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223051.
KOK14261.
OMAGPTPQHI.
OrthoDBEOG6W721W.
PhylomeDBP77434.
ProtClustDBPRK08175.

Enzyme and pathway databases

BioCycEcoCyc:G7242-MONOMER.
ECOL316407:JW2376-MONOMER.
MetaCyc:G7242-MONOMER.

Gene expression databases

GenevestigatorP77434.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

PROP77434.

Entry information

Entry nameALAC_ECOLI
AccessionPrimary (citable) accession number: P77434
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene