Reviewed, UniProtKB/Swiss-Prot P96807 (ECH1_MYCTU)

Names and origin

Protein names

Recommended name:
    Probable enoyl-CoA hydratase 1
    EC=4.2.1.17
Alternative name(s):
    Nodulation protein
    N-related protein

Gene names

Ordered Locus Names:

Rv0130, MT0138

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	enoyl-CoA hydratase activity Inferred from electronic annotation. Source: EC 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

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

.

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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

Sequences

	Sequence		Length	Mass (Da)
	P96807-1 [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: 9634230] [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: 12218036] [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: 16963641] [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

EMBLGenBankDDBJ

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

PIR

E70615.

RefSeq

NP_214644.1.
NP_334548.1.

3D structure databases

PDBPDBe

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

ModBase

Search...

Genome annotation databases

GeneID

886876.
923002.

GenomeReviews

Gene locus MT0138 in contig AE000516_GR.
Gene locus Rv0130 in contig AL123456_GR.

KEGG

mtc:MT0138.
mtu:Rv0130.

TIGR

MT0138.

Organism-specific databases

TubercuList

Rv0130.

Phylogenomic databases

HOGENOM

P96807.

OMA

IPFWGEL.

Enzyme and pathway databases

BRENDA

4.2.1.17. 809.

Family and domain databases

InterPro

IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR002539. MaoC_deHydtase.
[Graphical view]

Pfam

PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ECH1_MYCTU

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	May 1, 1997
Last modified:	November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)