XYL2_PICST
ID XYL2_PICST Reviewed; 363 AA.
AC P22144; A3GIB4; Q549G5;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=D-xylulose reductase;
DE EC=1.1.1.9;
DE AltName: Full=Xylitol dehydrogenase;
DE Short=XDH;
GN Name=XYL2; ORFNames=PICST_86924;
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 [GENOMIC DNA].
RC STRAIN=ATCC 62970 / CBS 5774 / NRRL Y-11542;
RX PubMed=2127555; DOI=10.1007/bf00327019;
RA Koetter P., Amore R., Hollenberg C.P., Ciriacy M.;
RT "Isolation and characterization of the Pichia stipitis xylitol
RT dehydrogenase gene, XYL2, and construction of a xylose-utilizing
RT Saccharomyces cerevisiae transformant.";
RL Curr. Genet. 18:493-500(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=10849789; DOI=10.1385/abab:84-86:1-9:201;
RA Shi N.-Q., Prahl K., Hendrick J., Cruz J., Lu P., Cho J.-Y., Jones S.,
RA Jeffries T.W.;
RT "Characterization and complementation of a Pichia stipitis mutant unable to
RT grow on D-xylose or L-arabinose.";
RL Appl. Biochem. Biotechnol. 84:201-216(2000).
RN [3]
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).
RN [4]
RP SIMILARITY TO OTHER ZINC-ALCOHOL DEHYDROGENASES.
RX PubMed=8504864; DOI=10.1016/0014-5793(93)81522-2;
RA Persson B., Hallborn J., Walfridsson M., Hahn-Haegerdal B., Keraenen S.,
RA Penttilae M., Joernvall H.;
RT "Dual relationships of xylitol and alcohol dehydrogenases in families of
RT two protein types.";
RL FEBS Lett. 324:9-14(1993).
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 -!- INDUCTION: By xylose. Repressed by glucose.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X55392; CAA39066.1; -; Genomic_DNA.
DR EMBL; AF127801; AAD28251.1; -; Genomic_DNA.
DR EMBL; AAVQ01000002; EAZ62959.1; -; Genomic_DNA.
DR PIR; S13529; S13529.
DR RefSeq; XP_001386982.1; XM_001386945.1.
DR AlphaFoldDB; P22144; -.
DR SMR; P22144; -.
DR STRING; 4924.XP_001386982.1; -.
DR EnsemblFungi; EAZ62959; EAZ62959; PICST_86924.
DR GeneID; 4852013; -.
DR KEGG; pic:PICST_86924; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; P22144; -.
DR OMA; EYKSGHY; -.
DR OrthoDB; 1019156at2759; -.
DR BRENDA; 1.1.1.9; 4832.
DR BRENDA; 1.1.1.B19; 4832.
DR UniPathway; UPA00146; UER00577.
DR Proteomes; UP000002258; Chromosome 1.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Xylose metabolism; Zinc.
FT CHAIN 1..363
FT /note="D-xylulose reductase"
FT /id="PRO_0000160883"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 183..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 363 AA; 38521 MW; 39E16FD087160248 CRC64;
MTANPSLVLN KIDDISFETY DAPEISEPTD VLVQVKKTGI CGSDIHFYAH GRIGNFVLTK
PMVLGHESAG TVVQVGKGVT SLKVGDNVAI EPGIPSRFSD EYKSGHYNLC PHMAFAATPN
SKEGEPNPPG TLCKYFKSPE DFLVKLPDHV SLELGALVEP LSVGVHASKL GSVAFGDYVA
VFGAGPVGLL AAAVAKTFGA KGVIVVDIFD NKLKMAKDIG AATHTFNSKT GGSEELIKAF
GGNVPNVVLE CTGAEPCIKL GVDAIAPGGR FVQVGNAAGP VSFPITVFAM KELTLFGSFR
YGFNDYKTAV GIFDTNYQNG RENAPIDFEQ LITHRYKFKD AIEAYDLVRA GKGAVKCLID
GPE
