Reviewed, UniProtKB/Swiss-Prot Q10488 (ETR1_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable trans-2-enoyl-CoA reductase, mitochondrial
    EC=1.3.1.38

Gene names

Name:	etr1
ORF Names:	SPAC26F1.04c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA. May have a role in the mitochondrial synthesis of fatty acids By similarity.
Catalytic activity	Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to stress Inferred from expression pattern. Source: GeneDB_SPombe fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	trans-2-enoyl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 372		Probable trans-2-enoyl-CoA reductase, mitochondrial		PRO_0000000903

Sequences

	Sequence		Length	Mass (Da)
	Q10488-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: F0ECE4624829A428	FASTA	372	41,230
	10 20 30 40 50 60 MSFFKTAVRR FSSTSITRGM AKAIAYSEYG NPKEVLRAVS YNVPKCSKNQ VNVRFLASPI 70 80 90 100 110 120 NPSDINQIQG VYPSKPPFTN DVCSSKPSAV AGNEGLVEVV DVGDQFKGTF SPGQWAILGS 130 140 150 160 170 180 VNLGSWRTEM NIDGRSLVPV DKSAFPSIAE AATLSVNPCT AYCLLQHVVQ LNKGDWFIQD 190 200 210 220 230 240 GANSMVGIAT IQLAKHFGYK SINVVRNRPD IEKLKEQLKS LGATIVITDE ELMDRKTMKQ 250 260 270 280 290 300 KVPEWIQGGE VKLGIDCVSG RVAAEMAKYM SKGATMATFG GMSRQPLPVP VSLLIFKNLK 310 320 330 340 350 360 FHGFWVTKWK SEHPEEFLKI IHKVEDFYRN GTLKTVNTEL VSLKEDADEK TFLDTFLNAI 370 EGHGKKIIKF EH

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA97361.1.
PIR	T38416.
RefSeq	NP_594891.1.
3D structure databases
HSSP	HSSP built from PDB template 1GYR based on UniProtKB Q8WZM3.
ModBase	Search...
Genome annotation databases
GeneID	2542100.
KEGG	spo:SPAC26F1.04c.
NMPDR	fig|4896.1.peg.4861.
Organism-specific databases
GeneDB_Spombe	SPAC26F1.04c.
Phylogenomic databases
OMA	Q10488. AYLMLTH.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002959-MON.
BRENDA	1.3.1.38. 653.
Gene expression databases
ArrayExpress	Q10488.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ETR1_SCHPO

Accession

Primary (citable) accession number: Q10488

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)