ID   ARDH_CANAW              Reviewed;         281 AA.
AC   P43066;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=D-arabinitol 2-dehydrogenase [ribulose-forming];
DE            Short=ARDH;
DE            EC=1.1.1.250;
GN   Name=ARD1; Synonyms=ARDH;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=8407803; DOI=10.1128/jb.175.19.6314-6320.1993;
RA   Wong B., Murray J.S., Castellanos M., Croen K.D.;
RT   "D-arabitol metabolism in Candida albicans: studies of the biosynthetic
RT   pathway and the gene that encodes NAD-dependent D-arabitol dehydrogenase.";
RL   J. Bacteriol. 175:6314-6320(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinitol + NAD(+) = D-ribulose + H(+) + NADH;
CC         Xref=Rhea:RHEA:17389, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC         ChEBI:CHEBI:18333, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.250;
CC   -!- PATHWAY: Carbohydrate metabolism; D-arabinitol metabolism.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; L16227; AAC37430.1; -; Genomic_DNA.
DR   EMBL; CM000312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P43066; -.
DR   SMR; P43066; -.
DR   STRING; 5476.P43066; -.
DR   PRIDE; P43066; -.
DR   VEuPathDB; FungiDB:CAWG_05342; -.
DR   UniPathway; UPA00380; -.
DR   Proteomes; UP000001429; Chromosome 6.
DR   GO; GO:0047038; F:D-arabinitol 2-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0051161; P:arabitol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..281
FT                   /note="D-arabinitol 2-dehydrogenase [ribulose-forming]"
FT                   /id="PRO_0000054517"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         25..47
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   281 AA;  30643 MW;  B302A6411691F892 CRC64;
     MDSAYWSYDN IVPSFRLDGK LVILTGGSGG LAAVVSRALL AKGADVALVD MNLERTQQAA
     RDVLQWGEEQ MKGKYESPIG QVSAWSCNIG DAEAVDLTFK AINEHHGKIS SVLVNTAGYA
     ENFPAEEYPA KNAENLMKVN GLGSFYVSQA FARPLIQNNM TGSIILIGSM SGTIVNDPQP
     QCMYNMSKAG VIHLARSLAC EWAKYNIRVN TLSPGYILTP LTRNVISGHT EMKTEWESKI
     PMKRMAEPKE FVGSILYLAS ESASSYTTGH NLVVDGGYEC W