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Protein

Peroxisomal hydratase-dehydrogenase-epimerase

Gene

FOX2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211NAD; via amide nitrogenBy similarity
Binding sitei40 – 401NADBy similarity
Binding sitei100 – 1001NAD; via carbonyl oxygenBy similarity
Binding sitei152 – 1521SubstrateBy similarity
Active sitei165 – 1651Proton acceptorPROSITE-ProRule annotation
Binding sitei456 – 4561SubstrateBy similarity
Active sitei469 – 4691Proton acceptorPROSITE-ProRule annotation
Binding sitei719 – 7191(3R)-3-hydroxydecanoyl-CoABy similarity
Binding sitei826 – 8261(3R)-3-hydroxydecanoyl-CoA; via amide nitrogenBy similarity
Binding sitei851 – 8511(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 3725NADBy similarityAdd
BLAST
Nucleotide bindingi75 – 762NADBy similarity
Nucleotide bindingi165 – 1695NADBy similarity
Nucleotide bindingi197 – 2004NADBy similarity
Nucleotide bindingi326 – 35025NADBy similarityAdd
BLAST

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: SGD
  2. enoyl-CoA hydratase activity Source: SGD
  3. isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid beta-oxidation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:YKR009C-MONOMER.
YEAST:YKR009C-MONOMER.
ReactomeiREACT_188947. alpha-linolenic acid (ALA) metabolism.
REACT_240301. Beta-oxidation of pristanoyl-CoA.
REACT_240498. Beta-oxidation of very long chain fatty acids.
REACT_257005. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal hydratase-dehydrogenase-epimerase
Short name:
HDE
Alternative name(s):
Multifunctional beta-oxidation protein
Short name:
MFP
Including the following 2 domains:
2-enoyl-CoA hydratase (EC:4.2.1.119)
(3R)-3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.n12)
Gene namesi
Name:FOX2
Ordered Locus Names:YKR009C
ORF Names:YK108
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKR009c.
SGDiS000001717. FOX2.

Subcellular locationi

GO - Cellular componenti

  1. peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 900900Peroxisomal hydratase-dehydrogenase-epimerasePRO_0000054700Add
BLAST

Proteomic databases

MaxQBiQ02207.
PaxDbiQ02207.
PeptideAtlasiQ02207.

Expressioni

Gene expression databases

GenevestigatoriQ02207.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi34141. 34 interactions.
IntActiQ02207. 1 interaction.
MINTiMINT-2787193.
STRINGi4932.YKR009C.

Structurei

3D structure databases

ProteinModelPortaliQ02207.
SMRiQ02207. Positions 5-893.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini775 – 887113MaoC-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 230225Short-chain dehydrogenase like 1Add
BLAST
Regioni319 – 535217Short-chain dehydrogenase like 2Add
BLAST
Regioni689 – 6902(3R)-3-hydroxydecanoyl-CoA bindingBy similarity
Regioni803 – 8086(3R)-3-hydroxydecanoyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi898 – 9003Microbody targeting signalSequence Analysis

Domaini

Contains two SDR domains.

Sequence similaritiesi

Contains 1 MaoC-like domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
InParanoidiQ02207.
KOiK14729.
OMAiTETIMPP.
OrthoDBiEOG7HQNM0.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.40.50.720. 2 hits.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 2 hits.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF54637. SSF54637. 2 hits.
PROSITEiPS00061. ADH_SHORT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02207-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGNLSFKDR VVVITGAGGG LGKVYALAYA SRGAKVVVND LGGTLGGSGH
60 70 80 90 100
NSKAADLVVD EIKKAGGIAV ANYDSVNENG EKIIETAIKE FGRVDVLINN
110 120 130 140 150
AGILRDVSFA KMTEREFASV VDVHLTGGYK LSRAAWPYMR SQKFGRIINT
160 170 180 190 200
ASPAGLFGNF GQANYSAAKM GLVGLAETLA KEGAKYNINV NSIAPLARSR
210 220 230 240 250
MTENVLPPHI LKQLGPEKIV PLVLYLTHES TKVSNSIFEL AAGFFGQLRW
260 270 280 290 300
ERSSGQIFNP DPKTYTPEAI LNKWKEITDY RDKPFNKTQH PYQLSDYNDL
310 320 330 340 350
ITKAKKLPPN EQGSVKIKSL CNKVVVVTGA GGGLGKSHAI WFARYGAKVV
360 370 380 390 400
VNDIKDPFSV VEEINKLYGE GTAIPDSHDV VTEAPLIIQT AISKFQRVDI
410 420 430 440 450
LVNNAGILRD KSFLKMKDEE WFAVLKVHLF STFSLSKAVW PIFTKQKSGF
460 470 480 490 500
IINTTSTSGI YGNFGQANYA AAKAAILGFS KTIALEGAKR GIIVNVIAPH
510 520 530 540 550
AETAMTKTIF SEKELSNHFD ASQVSPLVVL LASEELQKYS GRRVIGQLFE
560 570 580 590 600
VGGGWCGQTR WQRSSGYVSI KETIEPEEIK ENWNHITDFS RNTINPSSTE
610 620 630 640 650
ESSMATLQAV QKAHSSKELD DGLFKYTTKD CILYNLGLGC TSKELKYTYE
660 670 680 690 700
NDPDFQVLPT FAVIPFMQAT ATLAMDNLVD NFNYAMLLHG EQYFKLCTPT
710 720 730 740 750
MPSNGTLKTL AKPLQVLDKN GKAALVVGGF ETYDIKTKKL IAYNEGSFFI
760 770 780 790 800
RGAHVPPEKE VRDGKRAKFA VQNFEVPHGK VPDFEAEIST NKDQAALYRL
810 820 830 840 850
SGDFNPLHID PTLAKAVKFP TPILHGLCTL GISAKALFEH YGPYEELKVR
860 870 880 890 900
FTNVVFPGDT LKVKAWKQGS VVVFQTIDTT RNVIVLDNAA VKLSQAKSKL
Length:900
Mass (Da):98,703
Last modified:July 1, 1993 - v1
Checksum:i66FFD0D49C673788
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86456 mRNA. Translation: AAA34779.1.
X65124 Genomic DNA. Translation: CAA46243.1.
Z28234 Genomic DNA. Translation: CAA82079.1.
BK006944 Genomic DNA. Translation: DAA09165.1.
PIRiS25322.
RefSeqiNP_012934.1. NM_001179799.1.

Genome annotation databases

EnsemblFungiiYKR009C; YKR009C; YKR009C.
GeneIDi853878.
KEGGisce:YKR009C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86456 mRNA. Translation: AAA34779.1.
X65124 Genomic DNA. Translation: CAA46243.1.
Z28234 Genomic DNA. Translation: CAA82079.1.
BK006944 Genomic DNA. Translation: DAA09165.1.
PIRiS25322.
RefSeqiNP_012934.1. NM_001179799.1.

3D structure databases

ProteinModelPortaliQ02207.
SMRiQ02207. Positions 5-893.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34141. 34 interactions.
IntActiQ02207. 1 interaction.
MINTiMINT-2787193.
STRINGi4932.YKR009C.

Proteomic databases

MaxQBiQ02207.
PaxDbiQ02207.
PeptideAtlasiQ02207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR009C; YKR009C; YKR009C.
GeneIDi853878.
KEGGisce:YKR009C.

Organism-specific databases

CYGDiYKR009c.
SGDiS000001717. FOX2.

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
InParanoidiQ02207.
KOiK14729.
OMAiTETIMPP.
OrthoDBiEOG7HQNM0.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:YKR009C-MONOMER.
YEAST:YKR009C-MONOMER.
ReactomeiREACT_188947. alpha-linolenic acid (ALA) metabolism.
REACT_240301. Beta-oxidation of pristanoyl-CoA.
REACT_240498. Beta-oxidation of very long chain fatty acids.
REACT_257005. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.

Miscellaneous databases

NextBioi975163.
PROiQ02207.

Gene expression databases

GenevestigatoriQ02207.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.40.50.720. 2 hits.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 2 hits.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF54637. SSF54637. 2 hits.
PROSITEiPS00061. ADH_SHORT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.

Entry informationi

Entry nameiFOX2_YEAST
AccessioniPrimary (citable) accession number: Q02207
Secondary accession number(s): D6VX75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: January 7, 2015
This is version 120 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, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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.