ID M7WTH0_RHOT1 Unreviewed; 368 AA.
AC M7WTH0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=(R,R)-butanediol dehydrogenase / diacetyl reductase {ECO:0000313|EMBL:EMS21376.1};
GN ORFNames=RHTO_01842 {ECO:0000313|EMBL:EMS21376.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS21376.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS21376.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS21376.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; KB722656; EMS21376.1; -; Genomic_DNA.
DR RefSeq; XP_016272495.1; XM_016415521.1.
DR AlphaFoldDB; M7WTH0; -.
DR GeneID; 27365855; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_0_1; -.
DR OrthoDB; 1692576at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08233; butanediol_DH_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..358
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 368 AA; 39194 MW; E472E7A3AD373089 CRC64;
MPHVEQQTMK AAMYYGPHDL RIEEVAKPVP REGEVLVKVA WCGICGTAGP ILVPNKQPHP
ITRSSLSQGP VRLGHEFSGT VEEVGPGVEG DWKMGDRVVI EAVISCHKCY ACRSGCNNAC
TSLGFVGLSG PSGGLAEYFS SPASFLHRLP PNVSLKAGAM CEPLAVAIHA VKRAGFEKGM
KVLVCGAGPI GVFLTVVLKA MGADLIVVSE PSTTRRKFAT LAGATQTVSP LEDPGNLLSS
LRAMTGENEG FDIAFEAAGV ESALALAISA VRTRGVVLNV SVWSKEPKID MNQLVFGEKS
IRGASCYFED HPEVMRALGA EEIKLDQYVT STIPLDQLIE GGFEQLLRNA ENHVKILVSP
SGNLDQPF
//
