FOX2_YEAST
ID FOX2_YEAST Reviewed; 900 AA.
AC Q02207; D6VX75;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Peroxisomal hydratase-dehydrogenase-epimerase;
DE Short=HDE;
DE AltName: Full=Multifunctional beta-oxidation protein;
DE Short=MFP;
DE Includes:
DE RecName: Full=2-enoyl-CoA hydratase;
DE EC=4.2.1.119;
DE Includes:
DE RecName: Full=(3R)-3-hydroxyacyl-CoA dehydrogenase;
DE EC=1.1.1.n12;
GN Name=FOX2; OrderedLocusNames=YKR009C; ORFNames=YK108;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1551874; DOI=10.1016/s0021-9258(19)50476-8;
RA Hiltunen J.K., Wenzel B., Beyer A., Erdmann R., Fossa A., Kunau W.H.;
RT "Peroxisomal multifunctional beta-oxidation protein of Saccharomyces
RT cerevisiae. Molecular analysis of the fox2 gene and gene product.";
RL J. Biol. Chem. 267:6646-6653(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441752; DOI=10.1002/yea.320080908;
RA Duesterhoeft A., Philippsen P.;
RT "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT reading frames.";
RL Yeast 8:749-759(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
CC -!- FUNCTION: Second trifunctional enzyme acting on the beta-oxidation
CC pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase
CC activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-
CC ketoacyl-CoA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:58856; EC=4.2.1.119;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:32711, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726;
CC EC=1.1.1.n12;
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- DOMAIN: Contains two SDR domains.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; M86456; AAA34779.1; -; mRNA.
DR EMBL; X65124; CAA46243.1; -; Genomic_DNA.
DR EMBL; Z28234; CAA82079.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09165.1; -; Genomic_DNA.
DR PIR; S25322; S25322.
DR RefSeq; NP_012934.1; NM_001179799.1.
DR AlphaFoldDB; Q02207; -.
DR SMR; Q02207; -.
DR BioGRID; 34141; 65.
DR IntAct; Q02207; 1.
DR MINT; Q02207; -.
DR STRING; 4932.YKR009C; -.
DR MaxQB; Q02207; -.
DR PaxDb; Q02207; -.
DR PRIDE; Q02207; -.
DR EnsemblFungi; YKR009C_mRNA; YKR009C; YKR009C.
DR GeneID; 853878; -.
DR KEGG; sce:YKR009C; -.
DR SGD; S000001717; FOX2.
DR VEuPathDB; FungiDB:YKR009C; -.
DR eggNOG; KOG1206; Eukaryota.
DR GeneTree; ENSGT00940000158343; -.
DR HOGENOM; CLU_010194_18_0_1; -.
DR InParanoid; Q02207; -.
DR OMA; LITEMWK; -.
DR BioCyc; MetaCyc:YKR009C-MON; -.
DR BioCyc; YEAST:YKR009C-MON; -.
DR BRENDA; 4.2.1.119; 984.
DR Reactome; R-SCE-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-SCE-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-SCE-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-SCE-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q02207; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q02207; protein.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0106386; F:(3R)-hydroxyacyl-CoA dehydrogenase (NAD) activity; IEA:RHEA.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:SGD.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:SGD.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:SGD.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 2.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS00061; ADH_SHORT; 2.
PE 2: Evidence at transcript level;
KW Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase;
KW Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome;
KW Reference proteome; Repeat.
FT CHAIN 1..900
FT /note="Peroxisomal hydratase-dehydrogenase-epimerase"
FT /id="PRO_0000054700"
FT DOMAIN 775..887
FT /note="MaoC-like"
FT REGION 6..230
FT /note="Short-chain dehydrogenase like 1"
FT REGION 319..535
FT /note="Short-chain dehydrogenase like 2"
FT MOTIF 898..900
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 469
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 75..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 197..200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 326..350
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 689..690
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 803..808
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 826
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 851
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
SQ SEQUENCE 900 AA; 98703 MW; 66FFD0D49C673788 CRC64;
MPGNLSFKDR VVVITGAGGG LGKVYALAYA SRGAKVVVND LGGTLGGSGH NSKAADLVVD
EIKKAGGIAV ANYDSVNENG EKIIETAIKE FGRVDVLINN AGILRDVSFA KMTEREFASV
VDVHLTGGYK LSRAAWPYMR SQKFGRIINT ASPAGLFGNF GQANYSAAKM GLVGLAETLA
KEGAKYNINV NSIAPLARSR MTENVLPPHI LKQLGPEKIV PLVLYLTHES TKVSNSIFEL
AAGFFGQLRW ERSSGQIFNP DPKTYTPEAI LNKWKEITDY RDKPFNKTQH PYQLSDYNDL
ITKAKKLPPN EQGSVKIKSL CNKVVVVTGA GGGLGKSHAI WFARYGAKVV VNDIKDPFSV
VEEINKLYGE GTAIPDSHDV VTEAPLIIQT AISKFQRVDI LVNNAGILRD KSFLKMKDEE
WFAVLKVHLF STFSLSKAVW PIFTKQKSGF IINTTSTSGI YGNFGQANYA AAKAAILGFS
KTIALEGAKR GIIVNVIAPH AETAMTKTIF SEKELSNHFD ASQVSPLVVL LASEELQKYS
GRRVIGQLFE VGGGWCGQTR WQRSSGYVSI KETIEPEEIK ENWNHITDFS RNTINPSSTE
ESSMATLQAV QKAHSSKELD DGLFKYTTKD CILYNLGLGC TSKELKYTYE NDPDFQVLPT
FAVIPFMQAT ATLAMDNLVD NFNYAMLLHG EQYFKLCTPT MPSNGTLKTL AKPLQVLDKN
GKAALVVGGF ETYDIKTKKL IAYNEGSFFI RGAHVPPEKE VRDGKRAKFA VQNFEVPHGK
VPDFEAEIST NKDQAALYRL SGDFNPLHID PTLAKAVKFP TPILHGLCTL GISAKALFEH
YGPYEELKVR FTNVVFPGDT LKVKAWKQGS VVVFQTIDTT RNVIVLDNAA VKLSQAKSKL
