ID   M7S6P7_EUTLA            Unreviewed;       361 AA.
AC   M7S6P7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=D-xylulose reductase {ECO:0000256|ARBA:ARBA00026119};
DE            EC=1.1.1.9 {ECO:0000256|ARBA:ARBA00026119};
DE   AltName: Full=Xylitol dehydrogenase A {ECO:0000256|ARBA:ARBA00030139};
GN   ORFNames=UCREL1_11318 {ECO:0000313|EMBL:EMR61749.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR61749.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
CC   -!- FUNCTION: Xylitol dehydrogenase which catalyzes the conversion of
CC       xylitol to D-xylulose. Xylose is a major component of hemicelluloses
CC       such as xylan. Most fungi utilize D-xylose via three enzymatic
CC       reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and
CC       xylulokinase, to form xylulose 5-phosphate, which enters pentose
CC       phosphate pathway. {ECO:0000256|ARBA:ARBA00024843}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC       step 4/5. {ECO:0000256|ARBA:ARBA00025713}.
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; KB707557; EMR61749.1; -; Genomic_DNA.
DR   RefSeq; XP_007799156.1; XM_007800965.1.
DR   AlphaFoldDB; M7S6P7; -.
DR   STRING; 1287681.M7S6P7; -.
DR   KEGG; ela:UCREL1_11318; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_5_1; -.
DR   OMA; DVFKVMI; -.
DR   OrthoDB; 3017546at2759; -.
DR   Proteomes; UP000012174; 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; 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   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:UP000012174};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          9..352
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   361 AA;  39072 MW;  7BBCCE5055113B5A CRC64;
     MTNPSFVLRA VKDVAIEDRP KPKMRDDHDV IVHVSQTGIC GSDVHYWQRG RIGPYVLTAP
     MVLGHESSGI VVEVGADVTH LQPGDRVAME PGIPCRRCSY CRSGSYHLCG KMIFAATPPW
     DGTLARYYVN AGDFCYKIPE AMDLEEGAMV EPVSVAVAIA KTADIRPHQT VVVMGCGPIG
     ILCQAVVKIY GAKKVVGVDV VRSRLDIAKS YGADETFMPA KPAPDVDAIE HAEKVANEMK
     DKLGLGEGAD VVLECSGAEA CVQIGVYVAR RGGMFVQAGM GKENVMFPIT AVCTQGLTIK
     GSIRYLAGCY PAAIDLISSG KINVKKLITN RFKFEESEEA FELVRQGRSD VFKVMIEGVR
     D
//