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Q02207 (FOX2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal hydratase-dehydrogenase-epimerase

Short name=HDE
Alternative name(s):
Multifunctional beta-oxidation protein
Short name=MFP

Including the following 2 domains:

  1. 2-enoyl-CoA hydratase
    EC=4.2.1.119
  2. (3R)-3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.n12
Gene names
Name:FOX2
Ordered Locus Names:YKR009C
ORF Names:YK108
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length900 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.

Catalytic activity

(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O.

(R)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Monomer By similarity.

Subcellular location

Peroxisome.

Domain

Contains two SDR domains.

Sequence similarities

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

Contains 1 MaoC-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 900900Peroxisomal hydratase-dehydrogenase-epimerase
PRO_0000054700

Regions

Domain775 – 887113MaoC-like
Nucleotide binding13 – 3725NAD By similarity
Nucleotide binding75 – 762NAD By similarity
Nucleotide binding165 – 1695NAD By similarity
Nucleotide binding197 – 2004NAD By similarity
Nucleotide binding326 – 35025NAD By similarity
Region6 – 230225Short-chain dehydrogenase like 1
Region319 – 535217Short-chain dehydrogenase like 2
Region689 – 6902(3R)-3-hydroxydecanoyl-CoA binding By similarity
Region803 – 8086(3R)-3-hydroxydecanoyl-CoA binding By similarity
Motif898 – 9003Microbody targeting signal Potential

Sites

Active site1651Proton acceptor By similarity
Active site4691Proton acceptor By similarity
Binding site211NAD; via amide nitrogen By similarity
Binding site401NAD By similarity
Binding site1001NAD; via carbonyl oxygen By similarity
Binding site1521Substrate By similarity
Binding site4561Substrate By similarity
Binding site7191(3R)-3-hydroxydecanoyl-CoA By similarity
Binding site8261(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen By similarity
Binding site8511(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02207 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 66FFD0D49C673788

FASTA90098,703
        10         20         30         40         50         60 
MPGNLSFKDR VVVITGAGGG LGKVYALAYA SRGAKVVVND LGGTLGGSGH NSKAADLVVD 

        70         80         90        100        110        120 
EIKKAGGIAV ANYDSVNENG EKIIETAIKE FGRVDVLINN AGILRDVSFA KMTEREFASV 

       130        140        150        160        170        180 
VDVHLTGGYK LSRAAWPYMR SQKFGRIINT ASPAGLFGNF GQANYSAAKM GLVGLAETLA 

       190        200        210        220        230        240 
KEGAKYNINV NSIAPLARSR MTENVLPPHI LKQLGPEKIV PLVLYLTHES TKVSNSIFEL 

       250        260        270        280        290        300 
AAGFFGQLRW ERSSGQIFNP DPKTYTPEAI LNKWKEITDY RDKPFNKTQH PYQLSDYNDL 

       310        320        330        340        350        360 
ITKAKKLPPN EQGSVKIKSL CNKVVVVTGA GGGLGKSHAI WFARYGAKVV VNDIKDPFSV 

       370        380        390        400        410        420 
VEEINKLYGE GTAIPDSHDV VTEAPLIIQT AISKFQRVDI LVNNAGILRD KSFLKMKDEE 

       430        440        450        460        470        480 
WFAVLKVHLF STFSLSKAVW PIFTKQKSGF IINTTSTSGI YGNFGQANYA AAKAAILGFS 

       490        500        510        520        530        540 
KTIALEGAKR GIIVNVIAPH AETAMTKTIF SEKELSNHFD ASQVSPLVVL LASEELQKYS 

       550        560        570        580        590        600 
GRRVIGQLFE VGGGWCGQTR WQRSSGYVSI KETIEPEEIK ENWNHITDFS RNTINPSSTE 

       610        620        630        640        650        660 
ESSMATLQAV QKAHSSKELD DGLFKYTTKD CILYNLGLGC TSKELKYTYE NDPDFQVLPT 

       670        680        690        700        710        720 
FAVIPFMQAT ATLAMDNLVD NFNYAMLLHG EQYFKLCTPT MPSNGTLKTL AKPLQVLDKN 

       730        740        750        760        770        780 
GKAALVVGGF ETYDIKTKKL IAYNEGSFFI RGAHVPPEKE VRDGKRAKFA VQNFEVPHGK 

       790        800        810        820        830        840 
VPDFEAEIST NKDQAALYRL SGDFNPLHID PTLAKAVKFP TPILHGLCTL GISAKALFEH 

       850        860        870        880        890        900 
YGPYEELKVR FTNVVFPGDT LKVKAWKQGS VVVFQTIDTT RNVIVLDNAA VKLSQAKSKL 

« Hide

References

« Hide 'large scale' references
[1]"Peroxisomal multifunctional beta-oxidation protein of Saccharomyces cerevisiae. Molecular analysis of the fox2 gene and gene product."
Hiltunen J.K., Wenzel B., Beyer A., Erdmann R., Fossa A., Kunau W.H.
J. Biol. Chem. 267:6646-6653(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"DNA sequencing and analysis of a 24.7 kb segment encompassing centromere CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open reading frames."
Duesterhoeft A., Philippsen P.
Yeast 8:749-759(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86456 mRNA. Translation: AAA34779.1.
X65124 Genomic DNA. Translation: CAA46243.1.
Z28234 Genomic DNA. Translation: CAA82079.1.
BK006944 Genomic DNA. Translation: DAA09165.1.
PIRS25322.
RefSeqNP_012934.1. NM_001179799.1.

3D structure databases

ProteinModelPortalQ02207.
SMRQ02207. Positions 5-893.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34141. 34 interactions.
IntActQ02207. 1 interaction.
MINTMINT-2787193.
STRING4932.YKR009C.

Proteomic databases

PaxDbQ02207.
PeptideAtlasQ02207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR009C; YKR009C; YKR009C.
GeneID853878.
KEGGsce:YKR009C.

Organism-specific databases

CYGDYKR009c.
SGDS000001717. FOX2.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00530000062928.
HOGENOMHOG000170895.
KOK14729.
OMALVTEMWK.
OrthoDBEOG7HQNM0.

Enzyme and pathway databases

BioCycMetaCyc:YKR009C-MONOMER.
YEAST:YKR009C-MONOMER.
UniPathwayUPA00659.

Gene expression databases

GenevestigatorQ02207.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 2 hits.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio975163.
PROQ02207.

Entry information

Entry nameFOX2_YEAST
AccessionPrimary (citable) accession number: Q02207
Secondary accession number(s): D6VX75
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways