ID   Q9UVH9_FUNMO            Unreviewed;      1015 AA.
AC   Q9UVH9;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Fox2 protein {ECO:0000313|EMBL:CAB55552.1};
GN   Name=fox2 {ECO:0000313|EMBL:CAB55552.1};
OS   Funneliformis mosseae (Endomycorrhizal fungus) (Glomus mosseae).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Funneliformis.
OX   NCBI_TaxID=27381 {ECO:0000313|EMBL:CAB55552.1};
RN   [1] {ECO:0000313|EMBL:CAB55552.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BEG 12 {ECO:0000313|EMBL:CAB55552.1};
RX   PubMed=10517033; DOI=10.1094/MPMI.1999.12.10.934;
RA   Requena N., Petra F., Philipp F.;
RT   "Molecular characterization of GmFOX2, an evolutionarily highly conserved
RT   gene from the mycorrhizal fungus Glomus mosseae, down-regulated during
RT   interaction with rhizobacteria.";
RL   Mol. Plant Microbe Interact. 12:934-942(1999).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; AJ243538; CAB55552.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9UVH9; -.
DR   UniPathway; UPA00659; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd03448; HDE_HSD; 1.
DR   CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 2.
DR   Gene3D; 1.10.287.4290; -; 2.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
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; IPR003033; SCP2_sterol-bd_dom.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 2.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   Pfam; PF02036; SCP2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55718; SCP-like; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT   DOMAIN          747..860
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000259|Pfam:PF01575"
FT   DOMAIN          910..1006
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   1015 AA;  108898 MW;  F6A66FA50EE4D51B CRC64;
     MAQELRFDGR TVIVTGAGGV DEIIKAGGKA VSNYNSVEDG DKIVETAMKA FGRVDILINN
     AGILRDKSFA RITDSDWDLI QAVHVRGSYK VTKAAWDIFR KQKFGRIINT ASAAGIYGNF
     GQANYTKLAL VSFTETLAKE GAKANIHANV IAPIAASRMT ESVMPPDVLA ALKPDYVAPL
     VMYLCHESTQ ENGSLFEVGA GFVAKLRWER SKGAVFKADD TFLPGTVAVK WNEITEFTNP
     TYPTSPGDAD FVGLLEKAKA LPSNPKSEDL KFDGKVAIVT GAGGGLGRAY ALLLGKLGAS
     VVVNDLGVSA HGQGATSSAA DKVVEEIRQA GGKAVANYDS VEDGEKIVET AIKAFGRVDI
     IINNAGILRD KSFARMTDQD WDLVQRVHLR GTYKVTKAAW PYLTKQKYGR IINTASSVGL
     YGNFGQANYS TAKLGILGFS NTLALEGRKN NIFVNTIAPN AGTRMTATIW PPDMVEAFKP
     DYVAPFVSFL AHEACPSTGN VFEVGGGWVA QVRWQRAGGI GFPTSKALTP EDIASKIDII
     TNFDDGRATH PTTTQQALQQ FFENFANAQK SESGQSKSKS NNSKIDVEAA KKRKFEPHVF
     EYKERDVMLY ALGIGATRKD LQWVYENSDN FSVIPTFGVI PAIILSNTLP LSEVLGDFNV
     MMLLHGEQYL ELKKPIPTSG KLISTPYVID ILDKGKGVSF IFGITTTDEK GEVIFENQTT
     LFIRGIGGFG GKKTGDDRGA ATASNIPPKR APDVVVKEKT NENQAALYRL SGDYNPLHID
     PSMSAMGGFD VPILHGMCTF GISGKHIFST FGKNDPNTFK SIKARLAAPV FPGETLETQM
     WKDGDKVIFQ TRVVERDVIC IASAAVELRG SSASGASMGA PSATPSAGIS VPGFQSSSVF
     EQLKAGLDAA SPAERQAQVK KVKGSFQLNI KNAEGKEQSW YIDFKTGDGA VGIGPSPKKA
     DATIGVSDAD FMELASGKLN AQKAFMSGKL KIKGNMMLAT KLGDVLAGGK SKSKL
//