ID   XYL2_ARTOC              Reviewed;         356 AA.
AC   C5FTT1;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Probable D-xylulose reductase A;
DE            EC=1.1.1.9;
DE   AltName: Full=Xylitol dehydrogenase A;
GN   Name=xdhA; ORFNames=MCYG_06103;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + xylitol = D-xylulose + H(+) + NADH;
CC         Xref=Rhea:RHEA:20433, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC         ChEBI:CHEBI:17151, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.9;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC       step 4/5.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; DS995705; EEQ33284.1; -; Genomic_DNA.
DR   RefSeq; XP_002846234.1; XM_002846188.1.
DR   AlphaFoldDB; C5FTT1; -.
DR   SMR; C5FTT1; -.
DR   STRING; 63405.XP_002846234.1; -.
DR   EnsemblFungi; EEQ33284; EEQ33284; MCYG_06103.
DR   GeneID; 9228403; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_5_1; -.
DR   OMA; ETWYAMS; -.
DR   OrthoDB; 1019156at2759; -.
DR   UniPathway; UPA00146; UER00577.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
DR   CDD; cd05285; sorbitol_DH; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_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   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW   Reference proteome; Xylose metabolism; Zinc.
FT   CHAIN           1..356
FT                   /note="Probable D-xylulose reductase A"
FT                   /id="PRO_0000393514"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   356 AA;  37948 MW;  F84A1ED6FE6C4135 CRC64;
     MAADEPKNLS FVLEGIKKVK FEDRPVPVLK DAHDVLVNVR YTGICGSDVH YWDHGSIGPF
     VLTEPMVLGH ESSGVVTEIG PAVKSLKVGD RVALEPGICC RRCEPCKSGK YNLCVDMVFA
     ATPPYDGTLA KYYVLPEDFC YKLPSAMDLK DGALMEPLGV AVHITRQAEV KPGDTVVVFG
     AGPVGLLCCA ASRAFGAIKI ISVDIQPERL DFAKKYAATG VFLPEKASAV ENAERLRSGH
     GLGRGADVVI DASGAEQSVH TGIYVARPGG TYVQGGMGRD EISFPIMAAC TKELNMKGSF
     RYNSGDYKLA LELVGSGRLS VKELVTKVVA FTDAEQAFEE VKAGKGIKTL IAGVDG