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Protein

Putative enoyl reductase C646.07c

Gene

SPBC646.07c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_350968. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative enoyl reductase C646.07c (EC:1.3.1.38)
Gene namesi
ORF Names:SPBC646.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC646.07c.
PomBaseiSPBC646.07c.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8484CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei85 – 10521HelicalSequence AnalysisAdd
BLAST
Topological domaini106 – 15752LumenalSequence AnalysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence AnalysisAdd
BLAST
Topological domaini179 – 1868CytoplasmicSequence Analysis
Transmembranei187 – 20721HelicalSequence AnalysisAdd
BLAST
Topological domaini208 – 22316LumenalSequence AnalysisAdd
BLAST
Transmembranei224 – 24623HelicalSequence AnalysisAdd
BLAST
Topological domaini247 – 2504CytoplasmicSequence Analysis
Transmembranei251 – 26818HelicalSequence AnalysisAdd
BLAST
Topological domaini269 – 29527LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Putative enoyl reductase C646.07cPRO_0000317698Add
BLAST

Proteomic databases

MaxQBiO94511.
PaxDbiO94511.

Interactioni

Protein-protein interaction databases

BioGridi277585. 2 interactions.
MINTiMINT-4684798.
STRINGi4896.SPBC646.07c.1.

Family & Domainsi

Sequence similaritiesi

Belongs to the steroid 5-alpha reductase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG306265.
HOGENOMiHOG000190918.
InParanoidiO94511.
KOiK10258.
OMAiFTKSHPQ.
OrthoDBiEOG74XSHP.
PhylomeDBiO94511.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSITLSSRGR KIRKLPKSLE FPLDGSIDKL RDEVSSVTRL PVERLRFSTA
60 70 80 90 100
DGTTLLPNTT LRKYGVGPGA TIWVKDLGPQ IGWRTVFMIE YLGPLVIHLF
110 120 130 140 150
FILNYKWIYR KDYNLCLNQK IAFVLVMLHF MKREYESIFV HRFSLATMPL
160 170 180 190 200
RNIFKNCAHY HLLSGLFLAY FIYGPWHAND YIKPNHLLFL IVGWAFAVLS
210 220 230 240 250
NFRTHIILRD LRPAGSKKRV IPTGYGFNLV SFPNYFFESL GWLFFALLTK
260 270 280 290
SWASWIFLFV GSAQMFVWAK KKHARYLKEF PNYPRSRKIM IPFFL
Length:295
Mass (Da):34,640
Last modified:May 1, 1999 - v1
Checksum:iB4181D13E0F3C333
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22811.1.
PIRiT40583.
RefSeqiNP_595365.1. NM_001021273.2.

Genome annotation databases

EnsemblFungiiSPBC646.07c.1; SPBC646.07c.1:pep; SPBC646.07c.
GeneIDi2541070.
KEGGispo:SPBC646.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22811.1.
PIRiT40583.
RefSeqiNP_595365.1. NM_001021273.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277585. 2 interactions.
MINTiMINT-4684798.
STRINGi4896.SPBC646.07c.1.

Proteomic databases

MaxQBiO94511.
PaxDbiO94511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC646.07c.1; SPBC646.07c.1:pep; SPBC646.07c.
GeneIDi2541070.
KEGGispo:SPBC646.07c.

Organism-specific databases

EuPathDBiFungiDB:SPBC646.07c.
PomBaseiSPBC646.07c.

Phylogenomic databases

eggNOGiNOG306265.
HOGENOMiHOG000190918.
InParanoidiO94511.
KOiK10258.
OMAiFTKSHPQ.
OrthoDBiEOG74XSHP.
PhylomeDBiO94511.

Enzyme and pathway databases

ReactomeiREACT_350968. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi20802184.
PROiO94511.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYN67_SCHPO
AccessioniPrimary (citable) accession number: O94511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 1999
Last modified: June 24, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.