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Protein

Glutamate-pyruvate aminotransferase AlaA

Gene

alaA

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

Functioni

Involved in the biosynthesis of alanine.1 Publication

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=0.55 mM for pyruvate (at 37 degrees Celsius and pH 8.5)1 Publication
  2. KM=4.9 mM for alanine (at 37 degrees Celsius and pH 8.5)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411Substrate; via amide nitrogenBy similarity
Binding sitei179 – 1791SubstrateBy similarity
Binding sitei378 – 3781SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. alanine biosynthetic process Source: EcoliWiki
  2. cellular response to DNA damage stimulus Source: EcoCyc
  3. D-alanine biosynthetic process Source: UniProtKB
  4. L-alanine biosynthetic process from pyruvate Source: EcoCyc
  5. response to antibiotic Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-pyruvate aminotransferase AlaA (EC:2.6.1.2)
Gene namesi
Name:alaA
Synonyms:yfbQ
Ordered Locus Names:b2290, JW2287
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14101. alaA.

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 – 405405Glutamate-pyruvate aminotransferase AlaAPRO_0000123866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei240 – 2401N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP0A959.
PRIDEiP0A959.

Expressioni

Inductioni

Modestly repressed by alanine and leucine via Lrp.1 Publication

Gene expression databases

GenevestigatoriP0A959.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-11970N.
IntActiP0A959. 10 interactions.
STRINGi511145.b2290.

Structurei

Secondary structure

1
405
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Helixi20 – 3011Combined sources
Helixi44 – 463Combined sources
Helixi52 – 6110Combined sources
Helixi62 – 643Combined sources
Helixi75 – 8612Combined sources
Turni87 – 893Combined sources
Helixi95 – 973Combined sources
Beta strandi98 – 1036Combined sources
Helixi104 – 11310Combined sources
Beta strandi121 – 1277Combined sources
Helixi130 – 1389Combined sources
Beta strandi142 – 1487Combined sources
Helixi150 – 1523Combined sources
Helixi158 – 1636Combined sources
Beta strandi169 – 1779Combined sources
Turni179 – 1813Combined sources
Helixi187 – 19913Combined sources
Beta strandi203 – 2075Combined sources
Turni209 – 2124Combined sources
Helixi223 – 2264Combined sources
Beta strandi232 – 2387Combined sources
Turni239 – 2424Combined sources
Helixi245 – 2473Combined sources
Beta strandi250 – 2567Combined sources
Helixi259 – 2613Combined sources
Helixi262 – 27413Combined sources
Helixi281 – 2844Combined sources
Helixi285 – 2906Combined sources
Helixi297 – 3004Combined sources
Helixi305 – 31915Combined sources
Beta strandi329 – 3346Combined sources
Helixi340 – 3434Combined sources
Helixi348 – 35912Combined sources
Beta strandi360 – 3623Combined sources
Helixi366 – 3694Combined sources
Beta strandi372 – 3809Combined sources
Helixi385 – 40016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CVQX-ray2.11A/B1-405[»]
SMRiP0A959. Positions 1-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0436.
HOGENOMiHOG000223042.
InParanoidiP0A959.
KOiK14260.
OMAiQRNRTWE.
OrthoDBiEOG6X9MJ6.
PhylomeDBiP0A959.

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.

P0A959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPIEKSSKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA
60 70 80 90 100
PDEILVDVIR NLPTAQGYCD SKGLYSARKA IMQHYQARGM RDVTVEDIYI
110 120 130 140 150
GNGVSELIVQ AMQALLNSGD EMLVPAPDYP LWTAAVSLSS GKAVHYLCDE
160 170 180 190 200
SSDWFPDLDD IRAKITPRTR GIVIINPNNP TGAVYSKELL MEIVEIARQH
210 220 230 240 250
NLIIFADEIY DKILYDDAEH HSIAPLAPDL LTITFNGLSK TYRVAGFRQG
260 270 280 290 300
WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI
310 320 330 340 350
TPGGRLYEQR NRAWELINDI PGVSCVKPRG ALYMFPKIDA KRFNIHDDQK
360 370 380 390 400
MVLDFLLQEK VLLVQGTAFN WPWPDHFRIV TLPRVDDIEL SLSKFARFLS

GYHQL
Length:405
Mass (Da):45,517
Last modified:July 18, 2005 - v1
Checksum:i6A5E78876CC3C388
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75350.1.
AP009048 Genomic DNA. Translation: BAA16127.1.
PIRiH65000.
RefSeqiNP_416793.1. NC_000913.3.
YP_490532.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75350; AAC75350; b2290.
BAA16127; BAA16127; BAA16127.
GeneIDi12933976.
946772.
KEGGiecj:Y75_p2256.
eco:b2290.
PATRICi32119949. VBIEscCol129921_2384.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75350.1.
AP009048 Genomic DNA. Translation: BAA16127.1.
PIRiH65000.
RefSeqiNP_416793.1. NC_000913.3.
YP_490532.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CVQX-ray2.11A/B1-405[»]
SMRiP0A959. Positions 1-404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-11970N.
IntActiP0A959. 10 interactions.
STRINGi511145.b2290.

Proteomic databases

PaxDbiP0A959.
PRIDEiP0A959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75350; AAC75350; b2290.
BAA16127; BAA16127; BAA16127.
GeneIDi12933976.
946772.
KEGGiecj:Y75_p2256.
eco:b2290.
PATRICi32119949. VBIEscCol129921_2384.

Organism-specific databases

EchoBASEiEB3854.
EcoGeneiEG14101. alaA.

Phylogenomic databases

eggNOGiCOG0436.
HOGENOMiHOG000223042.
InParanoidiP0A959.
KOiK14260.
OMAiQRNRTWE.
OrthoDBiEOG6X9MJ6.
PhylomeDBiP0A959.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP0A959.

Gene expression databases

GenevestigatoriP0A959.

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(1996) [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(2005) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN AMINOTRANSFERASE AND IN ALANINE BIOSYNTHESIS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, NOMENCLATURE.

Entry informationi

Entry nameiALAA_ECOLI
AccessioniPrimary (citable) accession number: P0A959
Secondary accession number(s): P77727
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 18, 2005
Last sequence update: July 18, 2005
Last modified: March 31, 2015
This is version 81 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.