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Reviewed, UniProtKB/Swiss-Prot O42866 (FABG_SCHPO)

Last modified September 22, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-oxoacyl-[acyl-carrier-protein] reductase
    EC=1.1.1.100
Alternative name(s):
    3-ketoacyl-acyl carrier protein reductase
Gene names
Name: oar2
ORF Names: SPAC3G9.02
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved in biosynthesis of fatty acids in mitochondria By similarity.

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Mitochondrion. Ref.2

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentMitochondrion
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular function3-oxoacyl-[acyl-carrier-protein] reductase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2362363-oxoacyl-[acyl-carrier-protein] reductase
PRO_0000374026

Regions

Nucleotide binding5 – 2925NAD or NADP By similarity

Sites

Active site1511Proton acceptor By similarity
Binding site1381Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O42866-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 7F28C25E0C9251D9

FASTA23625,601
        10         20         30         40         50         60 
MRKVLITGGS SGLGKRIAQI WSQKGHQCHI VGRNEFHLKE TLQSLSVAKG QQHTLTIADV 

        70         80         90        100        110        120 
QSDMKNLKSI FESVEIDTVV HAAGVLQSSL CVRTSEKEID SIICTNLVSA IKLSKMAILE 

       130        140        150        160        170        180 
WFRNKNSERD RLILNISSRL STYALPGTSV YAASKAGLES FTKVLAAEVA SKGIRVNAIS 

       190        200        210        220        230 
PGYVDTPMLS SQIRAIAEKK VPIGRLASTD EIVDACTFLL DNRYTTGTIL PITGGL 

« Hide

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. expand/collapse author list , 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.
[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: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAA15911.1.
PIRT11638.
RefSeqNP_594074.1.

3D structure databases

HSSPHSSP built from PDB template 1Q7B based on UniProtKB P25716.
ModBaseSearch...

Protein-protein interaction databases

STRINGO42866.

Genome annotation databases

GeneID2543512.
GenomeReviewsGene locus oar2 in contig CU329670_GR.
KEGGspo:SPAC3G9.02.
NMPDRfig|4896.1.peg.4044.

Organism-specific databases

GeneDB_SpombeSPAC3G9.02.

Gene expression databases

ArrayExpressO42866.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG_SCHPO
AccessionPrimary (citable) accession number: O42866
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 1, 1998
Last modified: September 22, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents