ID   ARDH_CANTR              Reviewed;         282 AA.
AC   P50166;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=D-arabinitol 2-dehydrogenase [ribulose-forming];
DE            Short=ARDH;
DE            EC=1.1.1.250 {ECO:0000269|PubMed:7698655, ECO:0000269|PubMed:8250887};
GN   Name=ARD;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 110-129; 198-209 AND
RP   225-234, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX   PubMed=7698655; DOI=10.1016/0378-1119(94)00900-d;
RA   Murray J.S., Wong M.L., Miyada C.G., Switchenko A.C., Goodman T.C.,
RA   Wong B.;
RT   "Isolation, characterization and expression of the gene that encodes D-
RT   arabinitol dehydrogenase in Candida tropicalis.";
RL   Gene 155:123-128(1995).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8250887; DOI=10.1006/bbrc.1993.2397;
RA   Quong M.W., Miyada C.G., Switchenko A.C., Goodman T.C.;
RT   "Identification, purification, and characterization of a D-arabinitol-
RT   specific dehydrogenase from Candida tropicalis.";
RL   Biochem. Biophys. Res. Commun. 196:1323-1329(1993).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of D-arabinitol at
CC       carbon 4 to produce D-ribulose. {ECO:0000269|PubMed:7698655,
CC       ECO:0000269|PubMed:8250887}.
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; Evidence={ECO:0000269|PubMed:7698655,
CC         ECO:0000269|PubMed:8250887};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17390;
CC         Evidence={ECO:0000305|PubMed:8250887};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.2 mM for D-arabinitol (at pH 9.5 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:8250887};
CC         KM=39.8 mM for NAD(+) (at pH 9.5 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:8250887};
CC   -!- PATHWAY: Carbohydrate metabolism; D-arabinitol metabolism.
CC       {ECO:0000305|PubMed:7698655, ECO:0000305|PubMed:8250887}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; U00675; AAA66355.1; -; Genomic_DNA.
DR   PIR; JC4041; JC4041.
DR   AlphaFoldDB; P50166; -.
DR   SMR; P50166; -.
DR   VEuPathDB; FungiDB:CTMYA2_042940; -.
DR   VEuPathDB; FungiDB:CTRG_03026; -.
DR   UniPathway; UPA00380; -.
DR   GO; GO:0047038; F:D-arabinitol 2-dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0051161; P:arabitol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA: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   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..282
FT                   /note="D-arabinitol 2-dehydrogenase [ribulose-forming]"
FT                   /id="PRO_0000054518"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         26..48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   282 AA;  30748 MW;  A82A3DA4E771EF0D CRC64;
     MDSSSYWSYD NIVPSFRLDG KLVIITGGSG GLSAVVSRAL LAKGADIALI DMNLERTQQA
     ARDVLQWGEE QMKGKHESPI GQVSAWSCNI GDAEAVELTF KAINEHHGKV ASVLINTAGY
     AENFPAEEYP AKNAENIMKV NGLGSFYVSQ AFARPLIQNN MTGSIILIGS MSGTIVNDPQ
     PQCMYNMSKA GVIHLARSLA CEWAKYNIRV NTLSPGYILT PLTRNVISGH TEMKTEWESK
     IPMKRMAEPK EFVGSILYLA SDSASSYTTG HNLVVDGGYE CW