ID A0A066WG62_TILAU Unreviewed; 909 AA.
AC A0A066WG62;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative multifunctional beta-oxidation protein {ECO:0000313|EMBL:KDN52771.1};
GN ORFNames=K437DRAFT_253693 {ECO:0000313|EMBL:KDN52771.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN52771.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN52771.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN52771.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDN52771.1}.
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DR EMBL; JMSN01000006; KDN52771.1; -; Genomic_DNA.
DR RefSeq; XP_013245610.1; XM_013390156.1.
DR AlphaFoldDB; A0A066WG62; -.
DR STRING; 1037660.A0A066WG62; -.
DR GeneID; 25263651; -.
DR HOGENOM; CLU_010194_18_1_1; -.
DR InParanoid; A0A066WG62; -.
DR OMA; WATKVHT; -.
DR OrthoDB; 2140828at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000027361; Unassembled WGS sequence.
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; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 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 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; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR PROSITE; PS00061; ADH_SHORT; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027361}.
FT DOMAIN 790..901
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
FT REGION 607..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 97710 MW; FB73405CB83CC634 CRC64;
MSEFPEIENG KISFKGRTAI VSGAGNGLGR AYAIMLAQRG CKVLVNDLGP SMTDKSRKAA
DVVVEEIKKA GGEAVANYDS NVEGHKLVKQ AIDTWGRIDI VINNAGILRD KSFKSMTDAE
FDAIVAVHIT GSYAIAHAAW PYMRKQKYGR IINISSAAGI YGNFGQANYS AAKLAMNSFS
KTLAIEGAKY NIIANTVAPI AASQMLATIM PPEVLEQLKP EFVSPLVAYL VSAANKDVTG
QLVEAGAGFM AGLRRERSKG AVFRADDTFT PSAVRARIDE ILNFENDPQY PEKLTDANHL
EFLERAKGAK ANDQGDVKVR YDGKTVLVTG AGAGLGKAYA LMFAKLGANV VVNDFSEKAA
AAVVEEIKKA GGKAAPAIGS VEDGAKIVKA ATDAYGGLHV IINNAGILRD KSFASMNDDD
WHAVVKVHLR GTYAVCKAAW PIFLQQKYGR IVNTTSAVGI YGNFGQANYS AAKGAILGLT
QTLAIEGKKY NILANTIAPN AGTAMTATIW PQEMVDAFKP DFVAPVVGFL ASEANTEVSK
QLFEVSGGWV AAVRWQRSGG HAFSHAKIPQ PEAVQRKIGR ILDFDSERAS WPQDNQEAMQ
QVMANIGQEG EGDDDGDDDG DHIDPEDPAI VKEAKKQKVE STEFAYSERD VILYNLGLGA
KATDLNLTYE QADDFHALPT FGVIPQFAAS SSIPLDWLPN FSPMMLLHGE QYLAIKKPIP
TSATLVNKPR LLEVLDKGKA AAVTTVTHTV DKESGDVIFE NQSTVFIRGA GGFGGKKNGK
DRGDATALNK PPTRKPDAVI EEKTSEDQAA LYRLSGDYNP LHIDPEFSKV GGFERPILHG
LCFFGISGKH VFQKYGAFSS IKVRFASTVL PGQTLVTEMW KEGNKVIFQS KVKESGSIVL
SNAACTFSS
//
