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Protein

2-iminobutanoate/2-iminopropanoate deaminase

Gene

ridA

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

Functioni

Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity).By similarity

Catalytic activityi

2-iminobutanoate + H2O = 2-oxobutanoate + NH3.
2-iminopropanoate + H2O = pyruvate + NH3.

Pathwayi: L-isoleucine biosynthesis

This protein is involved in the subpathway that synthesizes 2-oxobutanoate from L-threonine. This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei17 – 171Stabilizes the substrateBy similarity
Binding sitei105 – 1051SubstrateSequence analysis
Sitei120 – 1201Important for catalytic activity at high pHBy similarity

GO - Molecular functioni

  • deaminase activity Source: UniProtKB
  • hydrolase activity Source: UniProtKB-KW
  • identical protein binding Source: EcoCyc
  • unfolded protein binding Source: EcoCyc

GO - Biological processi

  • isoleucine biosynthetic process Source: UniProtKB-KW
  • response to toxic substance Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Detoxification, Isoleucine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:G7877-MONOMER.
ECOL316407:JW5755-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-iminobutanoate/2-iminopropanoate deaminase (EC:3.5.99.10)
Alternative name(s):
Enamine/imine deaminase
Gene namesi
Name:ridA
Synonyms:yjgF
Ordered Locus Names:b4243, JW5755
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12524. ridA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 1281272-iminobutanoate/2-iminopropanoate deaminasePRO_0000170321Add
BLAST

Proteomic databases

EPDiP0AF93.
PaxDbiP0AF93.
PRIDEiP0AF93.

2D gel databases

SWISS-2DPAGEP0AF93.

Interactioni

Subunit structurei

Homotrimer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • unfolded protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262720. 8 interactions.
DIPiDIP-36232N.
STRINGi511145.b4243.

Structurei

Secondary structure

1
128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi18 – 225Combined sources
Beta strandi24 – 296Combined sources
Turni37 – 393Combined sources
Helixi46 – 6318Combined sources
Helixi68 – 703Combined sources
Beta strandi71 – 799Combined sources
Helixi81 – 833Combined sources
Helixi84 – 9714Combined sources
Beta strandi104 – 1096Combined sources
Helixi114 – 1163Combined sources
Beta strandi118 – 1269Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QU9X-ray1.20A/B/C1-128[»]
ProteinModelPortaliP0AF93.
SMRiP0AF93. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AF93.

Family & Domainsi

Sequence similaritiesi

Belongs to the RutC family.Curated

Phylogenomic databases

eggNOGiENOG4105KME. Bacteria.
COG0251. LUCA.
HOGENOMiHOG000267215.
InParanoidiP0AF93.
KOiK09022.
OMAiAGMDFNN.
OrthoDBiEOG6QVRPF.
PhylomeDBiP0AF93.

Family and domain databases

Gene3Di3.30.1330.40. 1 hit.
InterProiIPR013813. Endoribo_LPSP/chorism_mut-like.
IPR006056. RidA.
IPR019897. RidA_CS.
IPR006175. YjgF/YER057c/UK114.
[Graphical view]
PANTHERiPTHR11803. PTHR11803. 1 hit.
PfamiPF01042. Ribonuc_L-PSP. 1 hit.
[Graphical view]
SUPFAMiSSF55298. SSF55298. 1 hit.
TIGRFAMsiTIGR00004. TIGR00004. 1 hit.
PROSITEiPS01094. UPF0076. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AF93-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTIATENA PAAIGPYVQG VDLGNMIITS GQIPVNPKTG EVPADVAAQA
60 70 80 90 100
RQSLDNVKAI VEAAGLKVGD IVKTTVFVKD LNDFATVNAT YEAFFTEHNA
110 120
TFPARSCVEV ARLPKDVKIE IEAIAVRR
Length:128
Mass (Da):13,612
Last modified:January 23, 2007 - v2
Checksum:i4696BE30BAA71A15
GO

Sequence cautioni

The sequence AAA97140.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97140.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77200.2.
AP009048 Genomic DNA. Translation: BAE78242.1.
RefSeqiNP_418664.2. NC_000913.3.
WP_000047539.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77200; AAC77200; b4243.
BAE78242; BAE78242; BAE78242.
GeneIDi948771.
KEGGiecj:JW5755.
eco:b4243.
PATRICi32124063. VBIEscCol129921_4376.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97140.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77200.2.
AP009048 Genomic DNA. Translation: BAE78242.1.
RefSeqiNP_418664.2. NC_000913.3.
WP_000047539.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QU9X-ray1.20A/B/C1-128[»]
ProteinModelPortaliP0AF93.
SMRiP0AF93. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262720. 8 interactions.
DIPiDIP-36232N.
STRINGi511145.b4243.

2D gel databases

SWISS-2DPAGEP0AF93.

Proteomic databases

EPDiP0AF93.
PaxDbiP0AF93.
PRIDEiP0AF93.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77200; AAC77200; b4243.
BAE78242; BAE78242; BAE78242.
GeneIDi948771.
KEGGiecj:JW5755.
eco:b4243.
PATRICi32124063. VBIEscCol129921_4376.

Organism-specific databases

EchoBASEiEB2415.
EcoGeneiEG12524. ridA.

Phylogenomic databases

eggNOGiENOG4105KME. Bacteria.
COG0251. LUCA.
HOGENOMiHOG000267215.
InParanoidiP0AF93.
KOiK09022.
OMAiAGMDFNN.
OrthoDBiEOG6QVRPF.
PhylomeDBiP0AF93.

Enzyme and pathway databases

BioCyciEcoCyc:G7877-MONOMER.
ECOL316407:JW5755-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AF93.
PROiP0AF93.

Family and domain databases

Gene3Di3.30.1330.40. 1 hit.
InterProiIPR013813. Endoribo_LPSP/chorism_mut-like.
IPR006056. RidA.
IPR019897. RidA_CS.
IPR006175. YjgF/YER057c/UK114.
[Graphical view]
PANTHERiPTHR11803. PTHR11803. 1 hit.
PfamiPF01042. Ribonuc_L-PSP. 1 hit.
[Graphical view]
SUPFAMiSSF55298. SSF55298. 1 hit.
TIGRFAMsiTIGR00004. TIGR00004. 1 hit.
PROSITEiPS01094. UPF0076. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  5. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
    Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
    Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: B / BL21.
  7. "A test case for structure-based functional assignment: the 1.2-A crystal structure of the yjgF gene product from Escherichia coli."
    Volz K.
    Protein Sci. 8:2428-2437(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, PUTATIVE SUBSTRATE BINDING SITE.

Entry informationi

Entry nameiRIDA_ECOLI
AccessioniPrimary (citable) accession number: P0AF93
Secondary accession number(s): P39330, P76806, Q2M664
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.