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O53163 (ECH12_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable enoyl-CoA hydratase echA12
EC=4.2.1.17
Gene names
Name:echA12
Synonyms:fadB2
Ordered Locus Names:Rv1472, MT1518
ORF Names:MTV007.19
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Could possibly oxidize fatty acids using specific components By similarity.

Catalytic activity

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from direct assay. Source: MTBBASE

   Molecular functionenoyl-CoA hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Probable enoyl-CoA hydratase echA12
PRO_0000109341

Sequences

Sequence LengthMass (Da)Tools
O53163 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 6542FC79E7164F1C

FASTA28530,575
        10         20         30         40         50         60 
MPHRCAAQVV AGYRSTVSLV LVEHPRPEIA QITLNRPERM NSMAFDVMVP LKEALAQVSY 

        70         80         90        100        110        120 
DNSVRVVVLT GAGRGFSPGA DHKSAGVVPH VENLTRPTYA LRSMELLDDV ILMLRRLHQP 

       130        140        150        160        170        180 
VIAAVNGPAI GGGLCLALAA DIRVASSSAY FRAAGINNGL TASELGLSYL LPRAIGSSRA 

       190        200        210        220        230        240 
FEIMLTGRDV SAEEAERIGL VSRQVPDEQL LDACYAIAAR MAGFSRPGIE LTKRTLWSGL 

       250        260        270        280 
DAASLEAHMQ AEGLGQLFVR LLTANFEEAV AARAEQRAPV FTDDT

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842576 Genomic DNA. Translation: CAA16000.1.
AE000516 Genomic DNA. Translation: AAK45783.1.
PIRC70873.
RefSeqNP_215988.1. NC_000962.2.
NP_335969.1. NC_002755.2.

3D structure databases

ProteinModelPortalO53163.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001564; EBMYCP00000001564; EBMYCG00000001564.
EBMYCT00000069161; EBMYCP00000067220; EBMYCG00000069156.
GeneID886547.
924454.
GenomeReviewsGene locus MT1518 in contig AE000516_GR.
Gene locus Rv1472 in contig AL123456_GR.
KEGGmtc:MT1518.
mtu:Rv1472.
PATRIC18125104. VBIMycTub22151_1667.
TIGRMT1518.

Organism-specific databases

TubercuListRv1472.

Phylogenomic databases

GeneTreeEBGT00050000015506.
HOGENOMHBG748731.
OMALEGHMQA.
PhylomeDBO53163.
ProtClustDBPRK05864.

Family and domain databases

InterProIPR001753. Crotonase_core.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
KOK01692.
PfamPF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECH12_MYCTU
AccessionPrimary (citable) accession number: O53163
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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