XYL2_YEAST
ID XYL2_YEAST Reviewed; 356 AA.
AC Q07993; D6VY71;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=D-xylulose reductase;
DE EC=1.1.1.9 {ECO:0000269|PubMed:10486580};
DE AltName: Full=Xylitol dehydrogenase;
DE Short=XDH;
GN Name=XYL2; OrderedLocusNames=YLR070C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=10486580; DOI=10.1016/s0014-5793(99)01016-9;
RA Richard P., Toivari M.H., Penttilae M.;
RT "Evidence that the gene YLR070c of Saccharomyces cerevisiae encodes a
RT xylitol dehydrogenase.";
RL FEBS Lett. 457:135-138(1999).
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 Evidence={ECO:0000269|PubMed:10486580};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for D-xylose {ECO:0000269|PubMed:10486580};
CC KM=240 uM for NADH {ECO:0000269|PubMed:10486580};
CC KM=25 mM for xylitol {ECO:0000269|PubMed:10486580};
CC KM=100 uM for NAD {ECO:0000269|PubMed:10486580};
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. {ECO:0000269|PubMed:10486580}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z73242; CAA97627.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09387.1; -; Genomic_DNA.
DR PIR; S64902; S64902.
DR RefSeq; NP_013171.1; NM_001181957.1.
DR AlphaFoldDB; Q07993; -.
DR SMR; Q07993; -.
DR BioGRID; 31344; 74.
DR DIP; DIP-4533N; -.
DR IntAct; Q07993; 2.
DR STRING; 4932.YLR070C; -.
DR PaxDb; Q07993; -.
DR PRIDE; Q07993; -.
DR EnsemblFungi; YLR070C_mRNA; YLR070C; YLR070C.
DR GeneID; 850759; -.
DR KEGG; sce:YLR070C; -.
DR SGD; S000004060; XYL2.
DR VEuPathDB; FungiDB:YLR070C; -.
DR eggNOG; KOG0024; Eukaryota.
DR GeneTree; ENSGT00390000004074; -.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; Q07993; -.
DR OMA; ETWYAMS; -.
DR BioCyc; YEAST:YLR070C-MON; -.
DR BRENDA; 1.1.1.9; 984.
DR Reactome; R-SCE-5652227; Fructose biosynthesis.
DR Reactome; R-SCE-5661270; Formation of xylulose-5-phosphate.
DR SABIO-RK; Q07993; -.
DR UniPathway; UPA00146; UER00577.
DR PRO; PR:Q07993; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07993; protein.
DR GO; GO:0046526; F:D-xylulose reductase activity; IDA:SGD.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IBA:GO_Central.
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 GO; GO:0006062; P:sorbitol catabolic process; IBA:GO_Central.
DR GO; GO:0005999; P:xylulose biosynthetic process; IDA:SGD.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Xylose metabolism; Zinc.
FT CHAIN 1..356
FT /note="D-xylulose reductase"
FT /id="PRO_0000270925"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 179..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 356 AA; 38600 MW; 5DFD19BDB2E0AE00 CRC64;
MTDLTTQEAI VLERPGKITL TNVSIPKISD PNEVIIQIKA TGICGSDIHY YTHGRIANYV
VESPMVLGHE SSGIVALIGE NVKTLKVGDR VALEPGIPDR FSPEMKEGRY NLDPNLKFAA
TPPFDGTLTK YYKTMKDFVY KLPDDVSFEE GALIEPLSVA IHANKLAKIK FGARCVVFGA
GPIGLLAGKV ASVFGAADVV FVDLLENKLE TARQFGATHI VNSGDLPHGV TVDSVIKKAI
GKKGADVVFE CSGAEPCVRA GIEVCKAGGT IVQVGMGQEE IQFPISIIPT KELTFQGCFR
YCQGDYSDSI ELVSSRKLSL KPFITHRYSF KDAVEAFEET SHHPLNNIKT IIEGPE
