Skip Header

Contribute Send feedback
Read comments (?) or add your own

P0A959 (ALAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. 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
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 AlaA
EC=2.6.1.2
Gene names
Name:alaA
Synonyms:yfbQ
Ordered Locus Names:b2290, JW2287
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of alanine. Ref.4

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity.

Subunit structure

Homodimer. Ref.4

Subcellular location

Cytoplasm By similarity.

Induction

Modestly repressed by alanine and leucine via Lrp. Ref.4

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.55 mM for pyruvate (at 37 degrees Celsius and pH 8.5) Ref.4

KM=4.9 mM for alanine (at 37 degrees Celsius and pH 8.5)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Glutamate-pyruvate aminotransferase AlaA
PRO_0000123866

Sites

Binding site411Substrate; via amide nitrogen By similarity
Binding site1791Substrate By similarity
Binding site3781Substrate By similarity

Amino acid modifications

Modified residue2401N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A959 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 6A5E78876CC3C388

FASTA40545,517
        10         20         30         40         50         60 
MSPIEKSSKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA PDEILVDVIR 

        70         80         90        100        110        120 
NLPTAQGYCD SKGLYSARKA IMQHYQARGM RDVTVEDIYI GNGVSELIVQ AMQALLNSGD 

       130        140        150        160        170        180 
EMLVPAPDYP LWTAAVSLSS GKAVHYLCDE SSDWFPDLDD IRAKITPRTR GIVIINPNNP 

       190        200        210        220        230        240 
TGAVYSKELL MEIVEIARQH NLIIFADEIY DKILYDDAEH HSIAPLAPDL LTITFNGLSK 

       250        260        270        280        290        300 
TYRVAGFRQG WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI 

       310        320        330        340        350        360 
TPGGRLYEQR NRAWELINDI PGVSCVKPRG ALYMFPKIDA KRFNIHDDQK MVLDFLLQEK 

       370        380        390        400 
VLLVQGTAFN WPWPDHFRIV TLPRVDDIEL SLSKFARFLS GYHQL

« 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 277:1453-1474(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]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00096 Genomic DNA. Translation: AAC75350.1.
AP009048 Genomic DNA. Translation: BAA16127.1.
PIRH65000.
RefSeqNP_416793.1. NC_000913.2.
YP_490532.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A959.
SMRP0A959. Positions 7-399.
ModBaseSearch...

Protein-protein interaction databases

IntActP0A959. 10 interactions.
STRING511145.b2290.

Proteomic databases

PaxDbP0A959.
PRIDEP0A959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75350; AAC75350; b2290.
BAA16127; BAA16127; BAA16127.
GeneID12933976.
946772.
KEGGecj:Y75_p2256.
eco:b2290.
PATRIC32119949. VBIEscCol129921_2384.

Organism-specific databases

EchoBASEEB3854.
EcoGeneEG14101. alaA.

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223042.
KOK14260.
OMAYQARDMR.
ProtClustDBPRK09265.

Enzyme and pathway databases

BioCycEcoCyc:G7184-MONOMER.
ECOL316407:JW2287-MONOMER.
MetaCyc:G7184-MONOMER.

Gene expression databases

GenevestigatorP0A959.

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. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALAA_ECOLI
AccessionPrimary (citable) accession number: P0A959
Secondary accession number(s): P77727
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents