Enamine/imine deaminase - Escherichia coli (strain K12)

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P0AF93 (RIDA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Enamine/imine deaminase
EC=3.5.4.-

Gene names

Name:	ridA
Synonyms:	yjgF
Ordered Locus Names:	b4243, JW5755

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	128 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	Iminobutyrate + H₂O = 2-oxobutanoate + NH₃.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine.
Subunit structure	Homotrimer. Ref.7
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the RutC family.
Sequence caution	The sequence AAA97140.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Detoxification Isoleucine biosynthesis
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	deaminase activity Inferred from sequence or structural similarity. Source: UniProtKB hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4 Ref.5

Chain

2 – 128

127

Enamine/imine deaminase

PRO_0000170321

Sites

Binding site

105

Substrate Potential

Site

Stabilizes the substrate By similarity

Site

120

Role at high pH By similarity

Secondary structure

128

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AF93 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4696BE30BAA71A15
Show »

FASTA

128

13,612

        10         20         30         40         50         60 
MSKTIATENA PAAIGPYVQG VDLGNMIITS GQIPVNPKTG EVPADVAAQA RQSLDNVKAI 

        70         80         90        100        110        120 
VEAAGLKVGD IVKTTVFVKD LNDFATVNAT YEAFFTEHNA TFPARSCVEV ARLPKDVKIE 


IEAIAVRR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U14003 Genomic DNA. Translation: AAA97140.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77200.2.
AP009048 Genomic DNA. Translation: BAE78242.1.

RefSeq

NP_418664.2. NC_000913.2.
YP_492383.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QU9	X-ray	1.20	A/B/C	1-128	[»]

ProteinModelPortal

P0AF93.

SMR

P0AF93. Positions 2-128.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36232N.

STRING

511145.b4243.

2D gel databases

SWISS-2DPAGE

P0AF93.

Proteomic databases

PaxDb

P0AF93.

PRIDE

P0AF93.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77200; AAC77200; b4243.
BAE78242; BAE78242; BAE78242.

GeneID

12933726.
948771.

KEGG

ecj:Y75_p4128.
eco:b4243.

PATRIC

32124063. VBIEscCol129921_4376.

Organism-specific databases

EchoBASE

EB2415.

EcoGene

EG12524. ridA.

Phylogenomic databases

eggNOG

COG0251.

HOGENOM

HOG000267215.

K09022.

OMA

AGNTIYL.

ProtClustDB

CLSK950280.

Enzyme and pathway databases

BioCyc

EcoCyc:G7877-MONOMER.
ECOL316407:JW5755-MONOMER.

Gene expression databases

Genevestigator

P0AF93.

Family and domain databases

Gene3D

3.30.1330.40. 1 hit.

InterPro

IPR013813. Endoribo_LPSP/chorism_mut-like.
IPR006056. YjgF-like.
IPR019897. YjgF-like_CS.
IPR006175. YjgF/Yer057p/UK114.
[Graphical view]

PANTHER

PTHR11803. PTHR11803. 1 hit.

Pfam

PF01042. Ribonuc_L-PSP. 1 hit.
[Graphical view]

SUPFAM

SSF55298. YjgF/chorismate_mutase-like. 1 hit.

TIGRFAMs

TIGR00004. TIGR00004. 1 hit.

PROSITE

PS01094. UPF0076. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AF93.

Entry information

Entry name

RIDA_ECOLI

Accession

Primary (citable) accession number: P0AF93
Secondary accession number(s): P39330, P76806, Q2M664

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents