XDH_SCHPO
ID XDH_SCHPO Reviewed; 368 AA.
AC Q9UT60;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Probable D-xylose 1-dehydrogenase (NADP(+)) {ECO:0000305};
DE Short=XDH;
DE EC=1.1.1.179 {ECO:0000250|UniProtKB:A0A024SMV2};
DE AltName: Full=D-xylose-NADP dehydrogenase;
DE AltName: Full=Dimeric dihydrodiol dehydrogenase homolog;
DE AltName: Full=NADP(+)-dependent D-xylose dehydrogenase;
GN Name=dhd1 {ECO:0000312|PomBase:SPAC513.06c};
GN ORFNames=SPAC513.06c {ECO:0000312|PomBase:SPAC513.06c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: NADP-dependent D-xylose dehydrogenase catalyzing the
CC oxydation of D-xylose into D-xylonolactone (By similarity). May also
CC display activity with other sugars. May play a role in the regeneration
CC of NADP(+) in the presence of these sugars (Probable).
CC {ECO:0000250|UniProtKB:A0A024SMV2, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH;
CC Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.179; Evidence={ECO:0000250|UniProtKB:A0A024SMV2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; CU329670; CAB58729.1; -; Genomic_DNA.
DR PIR; T38901; T38901.
DR RefSeq; NP_593980.1; NM_001019406.2.
DR AlphaFoldDB; Q9UT60; -.
DR SMR; Q9UT60; -.
DR BioGRID; 279893; 4.
DR STRING; 4896.SPAC513.06c.1; -.
DR MaxQB; Q9UT60; -.
DR PaxDb; Q9UT60; -.
DR EnsemblFungi; SPAC513.06c.1; SPAC513.06c.1:pep; SPAC513.06c.
DR GeneID; 2543473; -.
DR KEGG; spo:SPAC513.06c; -.
DR PomBase; SPAC513.06c; dhd1.
DR VEuPathDB; FungiDB:SPAC513.06c; -.
DR eggNOG; KOG2741; Eukaryota.
DR HOGENOM; CLU_023194_7_2_1; -.
DR InParanoid; Q9UT60; -.
DR OMA; NVRWGIM; -.
DR PhylomeDB; Q9UT60; -.
DR PRO; PR:Q9UT60; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; ISS:PomBase.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0042843; P:D-xylose catabolic process; ISS:PomBase.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NADP; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..368
FT /note="Probable D-xylose 1-dehydrogenase (NADP(+))"
FT /id="PRO_0000316231"
SQ SEQUENCE 368 AA; 41531 MW; F374256D882FF899 CRC64;
MTSMSGASPV IHWGFLGAGS IAAVFAKDLV GVPERHKVQH EIVAVATRDS EHRASSFAKN
HCAPCKPKAY GSYEELVKDD KVDIVYISST HPQHYEVVKL ALLNDKAVLC EKPLTINYPE
ALELVELARA RNLFFAEGFW IRFYPIVKAA KTLLHEDRVC GDHFRLFVDF SQDFRFRELP
SESRLRTVSL GAGVLLDMGV YPLTWSRLLL YDDPKNEKQE PTVSSNALTF EDHNGDIGDY
TTAVTLVFPK TESIAMLCTS MDRGKMSDDF LKLDGENGNQ LFISGDCYRP QSIKLIRASG
ETEVFDFSFD DATGFFYEQD AVAECLLKNM KEAPEIPHEE TLKMMQLTDQ IRRQINVTYP
ADLRYTTA
