ID A0A1E3IVE3_9TREE Unreviewed; 434 AA.
AC A0A1E3IVE3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Xylitol dehydrogenase {ECO:0000313|EMBL:ODN92415.1};
GN ORFNames=L203_00691 {ECO:0000313|EMBL:ODN92415.1};
OS Cryptococcus depauperatus CBS 7841.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN92415.1, ECO:0000313|Proteomes:UP000094043};
RN [1] {ECO:0000313|EMBL:ODN92415.1, ECO:0000313|Proteomes:UP000094043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN92415.1,
RC ECO:0000313|Proteomes:UP000094043};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ODN92415.1}.
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DR EMBL; AWGK01000003; ODN92415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3IVE3; -.
DR STRING; 1295531.A0A1E3IVE3; -.
DR VEuPathDB; FungiDB:L203_00691; -.
DR OrthoDB; 2247176at2759; -.
DR Proteomes; UP000094043; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05285; sorbitol_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 InterPro; IPR045306; SDH-like.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; 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 Reference proteome {ECO:0000313|Proteomes:UP000094043};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 31..426
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 434 AA; 46848 MW; 73FA010CC19BAE17 CRC64;
MAEYHFLNKT QPPQVTCLNL PENTSCVLVK KRTIEVRSTP MPILQPDGVL VKVIATDESY
FSYFWRCCVE CGVGGRPVTQ PIVMGHESSG KVIAVGDRVK THKVGDRVAI EPGLPCRRCI
NCKEGKVNIC PSMRYCGAPG SVGSLSRFFA LPADMAPHIP DHLSWEEAGC IQPLAVGVQM
GKRVDLGPHK TVAVFGCGPI GLIAGAVAHA YSARKIIGFD NNPSRVEFAK HYMSPLTGKP
IFDHVFLTKD LPTTSLKNPS SGHSKNKLIP LSETGSTAAI EDGEVVDEEQ VTPGDRKWEW
AKKVAAEFIE KAGLVSEEGV DRVIEATGAE DCMFMGIAIV KRGGNYLAVG LGHIQTNLFP
TLAVTNKEIN VMGITRYTAS CFPSALDMLS RGVVNVKPLI TKCFPLTHST NAFEAVAAGG
DIKVVIKNQE GFEN
//
