Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate-pyruvate aminotransferase AlaC

Gene

alaC

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

Functioni

Involved in the biosynthesis of alanine.2 Publications

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=0.94 mM for pyruvate (at 37 degrees Celsius and pH 8.5)1 Publication

GO - Molecular functioni

  1. L-alanine:2-oxoglutarate aminotransferase activity Source: EcoCyc
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: EcoliWiki

GO - Biological processi

  1. alanine biosynthetic process Source: EcoliWiki
  2. D-alanine biosynthetic process Source: UniProtKB
  3. L-alanine biosynthetic process from pyruvate Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-pyruvate aminotransferase AlaC (EC:2.6.1.2)
Gene namesi
Name:alaC
Synonyms:yfdZ
Ordered Locus Names:b2379, JW2376
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG14198. alaC.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Glutamate-pyruvate aminotransferase AlaCPRO_0000123926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei244 – 2441N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP77434.
PRIDEiP77434.

Expressioni

Inductioni

Activated by SgrR and modestly repressed by alanine and leucine via Lrp.2 Publications

Gene expression databases

GenevestigatoriP77434.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-12010N.
IntActiP77434. 8 interactions.
STRINGi511145.b2379.

Structurei

3D structure databases

ProteinModelPortaliP77434.
SMRiP77434. Positions 20-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0436.
HOGENOMiHOG000223051.
InParanoidiP77434.
KOiK14261.
OMAiRGSIPKP.
OrthoDBiEOG6W721W.
PhylomeDBiP77434.

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.

P77434-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADTRPERRF TRIDRLPPYV FNITAELKMA ARRRGEDIID FSMGNPDGAT
60 70 80 90 100
PPHIVEKLCT VAQRPDTHGY STSRGIPRLR RAISRWYQDR YDVEIDPESE
110 120 130 140 150
AIVTIGSKEG LAHLMLATLD HGDTVLVPNP SYPIHIYGAV IAGAQVRSVP
160 170 180 190 200
LVEGVDFFNE LERAIRESYP KPKMMILGFP SNPTAQCVEL EFFEKVVALA
210 220 230 240 250
KRYDVLVVHD LAYADIVYDG WKAPSIMQVP GARDVAVEFF TLSKSYNMAG
260 270 280 290 300
WRIGFMVGNK TLVSALARIK SYHDYGTFTP LQVAAIAALE GDQQCVRDIA
310 320 330 340 350
EQYKRRRDVL VKGLHEAGWM VEMPKASMYV WAKIPEPYAA MGSLEFAKKL
360 370 380 390 400
LNEAKVCVSP GIGFGDYGDT HVRFALIENR DRIRQAIRGI KAMFRADGLL
410
PASSKHIHEN AE
Length:412
Mass (Da):46,216
Last modified:February 1, 1997 - v1
Checksum:iF0F62F84344E588E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75438.1.
AP009048 Genomic DNA. Translation: BAA16249.1.
PIRiH65011.
RefSeqiNP_416880.1. NC_000913.3.
YP_490621.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75438; AAC75438; b2379.
BAA16249; BAA16249; BAA16249.
GeneIDi12931937.
946850.
KEGGiecj:Y75_p2346.
eco:b2379.
PATRICi32120137. VBIEscCol129921_2477.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75438.1.
AP009048 Genomic DNA. Translation: BAA16249.1.
PIRiH65011.
RefSeqiNP_416880.1. NC_000913.3.
YP_490621.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP77434.
SMRiP77434. Positions 20-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-12010N.
IntActiP77434. 8 interactions.
STRINGi511145.b2379.

Proteomic databases

PaxDbiP77434.
PRIDEiP77434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75438; AAC75438; b2379.
BAA16249; BAA16249; BAA16249.
GeneIDi12931937.
946850.
KEGGiecj:Y75_p2346.
eco:b2379.
PATRICi32120137. VBIEscCol129921_2477.

Organism-specific databases

EchoBASEiEB3950.
EcoGeneiEG14198. alaC.

Phylogenomic databases

eggNOGiCOG0436.
HOGENOMiHOG000223051.
InParanoidiP77434.
KOiK14261.
OMAiRGSIPKP.
OrthoDBiEOG6W721W.
PhylomeDBiP77434.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP77434.

Gene expression databases

GenevestigatoriP77434.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiALAC_ECOLI
AccessioniPrimary (citable) accession number: P77434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: January 7, 2015
This is version 108 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.