P96807 (ECH1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable enoyl-CoA hydratase 1
EC=4.2.1.17

Alternative name(s):
N-related protein
Nodulation protein

Gene names

Ordered Locus Names:

Rv0130, MT0138

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in the hydration of fatty acids for production of polyhydroxylalkanoates. Ref.3
Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. Ref.3
Subunit structure	Homodimer. Ref.3
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family. Contains 1 MaoC-like domain.
Biophysicochemical properties	Kinetic parameters: KM=55 µM for 2-butenoyl-CoA Ref.3

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from mutant phenotype PubMed 18375556. Source: MTBBASE oxidation-reduction process Inferred from electronic annotation. Source: GOC
Molecular_function	3-hydroxyacyl-CoA dehydratase activity Inferred from direct assay PubMed 18375556. Source: MTBBASE enoyl-CoA hydratase activity Inferred from direct assay Ref.3. Source: MTBBASE oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 151

151

Probable enoyl-CoA hydratase 1

PRO_0000262761

Regions

Domain

11 – 132

122

MaoC-like

Region

60 – 63

4

Substrate-binding Probable Ref.3

Region

86 – 89

4

Substrate-binding (in homodimeric partner) Probable Ref.3

Region

97 – 99

3

Substrate-binding Probable Ref.3

Compositional bias

11 – 14

4

Poly-Ala

Sites

Binding site

124

1

Substrate; in homodimeric partner Probable Ref.3

Binding site

148

1

Substrate; in homodimeric partner Probable Ref.3

Site

40

1

Important for catalytic activity

Site

42

1

Transition state stabilizer Potential

Site

45

1

Important for catalytic activity

Experimental info

Mutagenesis

40

1

D → N: 27% loss of activity. Ref.3

Mutagenesis

45

1

H → Q: Total loss of activity. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

151

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Helix

7 – 12

6

Turn

13 – 15

3

Beta strand

16 – 20

5

Helix

28 – 38

11

Helix

43 – 46

4

Helix

48 – 52

5

Helix

63 – 68

6

Helix

70 – 75

6

Beta strand

79 – 82

4

Beta strand

84 – 95

12

Beta strand

105 – 119

15

Beta strand

122 – 133

12

Beta strand

140 – 150

11

Sequences

	Sequence		Length	Mass (Da)
	P96807 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 7A2613466BBFCD57	FASTA	151	16,007
	10 20 30 40 50 60 MRTFESVADL AAAAGEKVGQ SDWVTITQEE VNLFADATGD HQWIHVDPER AAAGPFGTTI 70 80 90 100 110 120 AHGFMTLALL PRLQHQMYTV KGVKLAINYG LNKVRFPAPV PVGSRVRATS SLVGVEDLGN 130 140 150 GTVQATVSTT VEVEGSAKPA CVAESIVRYV A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis." Johansson P., Castell A., Jones T.A., Backbro K. Protein Sci. 15:2300-2309(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-40 AND HIS-45. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842572 Genomic DNA. Translation: CAB07036.1.
AE000516 Genomic DNA. Translation: AAK44362.1.
AL123456 Genomic DNA. Translation: CCP42855.1.

PIR

E70615.

RefSeq

NP_214644.1. NC_000962.3.
NP_334548.1. NC_002755.2.
YP_006513449.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C2I	X-ray	1.80	A/B	1-151	[»]

ProteinModelPortal

P96807.

SMR

P96807. Positions 2-150.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv0130.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK44362; AAK44362; MT0138.

GeneID

13316113.
886876.
923002.

KEGG

mtc:MT0138.
mtu:Rv0130.
mtv:RVBD_0130.

PATRIC

18122032. VBIMycTub22151_0151.

Organism-specific databases

TubercuList

Rv0130.

Phylogenomic databases

eggNOG

COG2030.

HOGENOM

HOG000242265.

OMA

DWITITQ.

ProtClustDB

CLSK790285.

Enzyme and pathway databases

SABIO-RK

P96807.

Family and domain databases

InterPro

IPR002539. MaoC_dom.
[Graphical view]

Pfam

PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P96807.

Entry information

Entry name

ECH1_MYCTU

Accession

Primary (citable) accession number: P96807
Secondary accession number(s): L0T2P7, Q7DAF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program