Q1ZXF1 (ECHM_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable enoyl-CoA hydratase, mitochondrial
EC=4.2.1.17

Alternative name(s):
Enoyl-CoA hydratase 1
Short-chain enoyl-CoA hydratase
Short name=SCEH

Gene names

Name:	echs1
ORF Names:	DDB_G0285071

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate By similarity.
Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Homohexamer; dimer of trimers By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Domain	The monomer is folded into a right-handed spiral of four turns, followed by two small domains which are involved in trimerization By similarity.
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from sequence or structural similarity. Source: dictyBase
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	enoyl-CoA hydratase activity Inferred from sequence or structural similarity. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 42	42	Mitochondrion
	Chain	43 – 277	235	Probable enoyl-CoA hydratase, mitochondrial		PRO_0000331592
Regions
	Region	85 – 88	4	Substrate binding By similarity
Sites
	Binding site	128	1	Substrate; via amide nitrogen By similarity
	Site	151	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1ZXF1 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: 69C207F4D78F792B	FASTA	277	30,187
	10 20 30 40 50 60 MLKQVIKTVS SSQAPKKYFF KQFCTSTTEK KGRVGLVTLN RPKSLNALSD GLISEINSAV 70 80 90 100 110 120 KLFQEDKDVG SIIITGSEKA FAAGADIKEM EKVTLPDAYN NDLLAQWHDL TKIRKPIIAA 130 140 150 160 170 180 VNGYALGGGC ELAMMCDIII AGEKAVFGQP EIKLGTIPGC GGTQRLIRAI GKSKAMELVL 190 200 210 220 230 240 TGNNLTAVEA EKAGLVSKVV PVEELLTEAT KMAEKIASYS QLTVAMAKEA VNASYELTLQ 250 260 270 EGIRFERRMF HSTFGTHDQK EGMNAFVEKR TPTWHNK

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000073 Genomic DNA. Translation: EAS66856.1.
RefSeq	XP_001134539.1. XM_001134539.1.
3D structure databases
ProteinModelPortal	Q1ZXF1.
SMR	Q1ZXF1. Positions 28-270.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1ZXF1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0232942; DDB0232942; DDB_G0285071.
GeneID	8624884.
GenomeReviews	Gene locus echs1 in contig CM000153_GR.
KEGG	ddi:DDB_G0285071.
Organism-specific databases
dictyBase	DDB_G0285071. echs1.
Phylogenomic databases
eggNOG	KOG1680.
GeneTree	EPrGT00050000004514.
HOGENOM	HBG748731.
OMA	TGNMINA.
PhylomeDB	Q1ZXF1.
Family and domain databases
InterPro	IPR014748. Crontonase_C. IPR001753. Crotonase_core. IPR018376. Enoyl-CoA_hyd/isom_CS. [Graphical view]
Gene3D	G3DSA:1.10.12.10. Crontonase_C. 1 hit.
KO	K07511.
Pfam	PF00378. ECH. 1 hit. [Graphical view]
PROSITE	PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ECHM_DICDI

Accession

Primary (citable) accession number: Q1ZXF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 2, 2006
Last modified:	November 16, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)