Q02207 (FOX2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	900 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Domain	Repeat
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from mutant phenotype PubMed 10497229Ref.1. Source: SGD
Cellular_component	peroxisome Inferred from sequence model Ref.1. Source: SGD
Molecular_function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from direct assay Ref.1. Source: SGD enoyl-CoA hydratase activity Inferred from direct assay Ref.1. Source: SGD isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW nucleotide 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
	Chain	1 – 900	900	Peroxisomal hydratase-dehydrogenase-epimerase		PRO_0000054700
Regions
	Domain	775 – 887	113	MaoC-like
	Nucleotide binding	13 – 37	25	NAD By similarity
	Nucleotide binding	75 – 76	2	NAD By similarity
	Nucleotide binding	165 – 169	5	NAD By similarity
	Nucleotide binding	197 – 200	4	NAD By similarity
	Nucleotide binding	326 – 350	25	NAD By similarity
	Region	6 – 230	225	Short-chain dehydrogenase like 1
	Region	319 – 535	217	Short-chain dehydrogenase like 2
	Region	689 – 690	2	(3R)-3-hydroxydecanoyl-CoA binding By similarity
	Region	803 – 808	6	(3R)-3-hydroxydecanoyl-CoA binding By similarity
	Motif	898 – 900	3	Microbody targeting signal Potential
Sites
	Active site	165	1	Proton acceptor By similarity
	Active site	469	1	Proton acceptor By similarity
	Binding site	21	1	NAD; via amide nitrogen By similarity
	Binding site	40	1	NAD By similarity
	Binding site	100	1	NAD; via carbonyl oxygen By similarity
	Binding site	152	1	Substrate By similarity
	Binding site	456	1	Substrate By similarity
	Binding site	719	1	(3R)-3-hydroxydecanoyl-CoA By similarity
	Binding site	826	1	(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen By similarity
	Binding site	851	1	(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q02207 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 66FFD0D49C673788	FASTA	900	98,703
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	S25322.
RefSeq	NP_012934.1. NM_001179799.1.
3D structure databases
ProteinModelPortal	Q02207.
SMR	Q02207. Positions 5-893.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-2787193.
STRING	4932.YKR009C.
Proteomic databases
PaxDb	Q02207.
PeptideAtlas	Q02207.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKR009C; YKR009C; YKR009C.
GeneID	853878.
KEGG	sce:YKR009C.
Organism-specific databases
CYGD	YKR009c.
SGD	S000001717. FOX2.
Phylogenomic databases
eggNOG	COG1028.
GeneTree	ENSGT00530000062928.
HOGENOM	HOG000170895.
KO	K14729.
OMA	PHAETAM.
OrthoDB	EOG4PRWZX.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16868.
UniPathway	UPA00659.
Gene expression databases
Genevestigator	Q02207.
GermOnline	YKR009C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.50.720. 2 hits.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR002539. MaoC_dom. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 2 hits. PF01575. MaoC_dehydratas. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	975163.

Entry information

Entry name

FOX2_YEAST

Accession

Primary (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:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program