ID W2S6U0_9EURO Unreviewed; 381 AA.
AC W2S6U0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=HMPREF1541_02818 {ECO:0000313|EMBL:ETN43659.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN43659.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN43659.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN43659.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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; KB822718; ETN43659.1; -; Genomic_DNA.
DR RefSeq; XP_008715395.1; XM_008717173.1.
DR AlphaFoldDB; W2S6U0; -.
DR STRING; 1220924.W2S6U0; -.
DR GeneID; 19970157; -.
DR VEuPathDB; FungiDB:HMPREF1541_02818; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; W2S6U0; -.
DR OrthoDB; 3017546at2759; -.
DR Proteomes; UP000030752; 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; 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 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:UP000030752};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 36..148
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 190..325
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 381 AA; 40228 MW; E13B31EBC9B9D207 CRC64;
MSIRGAANPS IYLYGPGKAK IVDHPTPTLD APEDAGRIIV RVAFVGVCGS DVHFWNHGGI
NGKNVSESQP LIMGHEASGT VHAVGSAVQD LKVGDEVAIE PSDPCRSCPH CKRGAYHLCP
HMKFGACPPD TPGCLTHFYK MPADFAYPLP PSISLREGAL TEPLAVGAHA VRGVNVRPGQ
SVVVMGAGTV GVCAAVVARW FGATNVVCMD LQAGKLEGAR AVLGGADGFE TLMPRQGEAP
MELAARIVRE CGLGEGADAV VEATGAESCV QTGVYVLRKG GQYIQTGLGK VMIQFPIVDV
SEKELHFHGA FRYGPEDFAV ALDVLRSGRW EVAKLITKVW EFENTTEAWE ATKRGEGVKN
MIRVGGKEEA GVGTNGVARS T
//
