ARDH_PICST
ID ARDH_PICST Reviewed; 278 AA.
AC P50167; A3LUR3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=D-arabinitol 2-dehydrogenase [ribulose-forming];
DE Short=ARDH;
DE EC=1.1.1.250;
GN Name=ARDH; Synonyms=ARD2; ORFNames=PICST_65696;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=7483848; DOI=10.1002/yea.320110906;
RA Hallborn J., Walfridsson M., Penttilae M., Keraenen S., Hahn-Haegerdal B.;
RT "A short-chain dehydrogenase gene from Pichia stipitis having D-arabinitol
RT dehydrogenase activity.";
RL Yeast 11:839-847(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; Z46866; CAA86939.1; -; mRNA.
DR EMBL; CP000499; ABN67006.1; -; Genomic_DNA.
DR PIR; S57351; S57351.
DR RefSeq; XP_001385035.1; XM_001384998.1.
DR AlphaFoldDB; P50167; -.
DR SMR; P50167; -.
DR STRING; 4924.XP_001385035.1; -.
DR EnsemblFungi; ABN67006; ABN67006; PICST_65696.
DR GeneID; 4839199; -.
DR KEGG; pic:PICST_65696; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; P50167; -.
DR OMA; QHGKIDN; -.
DR OrthoDB; 1051625at2759; -.
DR BioCyc; MetaCyc:MON-21870; -.
DR UniPathway; UPA00380; -.
DR Proteomes; UP000002258; Chromosome 5.
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 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..278
FT /note="D-arabinitol 2-dehydrogenase [ribulose-forming]"
FT /id="PRO_0000054519"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 22..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 278 AA; 30003 MW; 36869165F23964F6 CRC64;
MDYSYANVVP NFRLDGRLAI ITGGSGGLAA VISRALLAQG ADVALIDMNL ERTKSAAKEV
LGWGEETLKG EHASAIGQVS AWSCNIGDAE AVDATFSSIN EHHGKIADLL INTAGYCENF
PAETYPATNA ESIMKVNGLG SFYVSQSFAR PLIQNNLRGS IILIGSMSGT IVNDPQPQCM
YNMSKAGVIH LVRSLACEWA KYNIRVNTLS PGYILTPLTR NVISGHTEMK EAWESKIPMK
RMAEPKEFVG SILYLASETA SSYTTGHNLV VDGGYECW
