XDH_HYPJR
ID XDH_HYPJR Reviewed; 391 AA.
AC A0A024SMV2; A8BT09;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=D-xylose 1-dehydrogenase (NADP(+)) {ECO:0000305|PubMed:18031347};
DE Short=XDH;
DE EC=1.1.1.179 {ECO:0000269|PubMed:18031347};
DE AltName: Full=D-xylose-NADP dehydrogenase;
DE AltName: Full=NADP(+)-dependent D-xylose dehydrogenase {ECO:0000303|PubMed:18031347};
GN Name=xyd1 {ECO:0000303|PubMed:18031347}; ORFNames=M419DRAFT_31971;
OS Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1344414;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=18031347; DOI=10.1111/j.1574-6968.2007.00969.x;
RA Berghall S., Hilditch S., Penttila M., Richard P.;
RT "Identification in the mould Hypocrea jecorina of a gene encoding an
RT NADP(+): d-xylose dehydrogenase.";
RL FEMS Microbiol. Lett. 277:249-253(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1089/ind.2013.0015;
RA Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT "Comparative genomics analysis of Trichoderma reesei strains.";
RL Ind. Biotechnol. 9:352-367(2013).
CC -!- FUNCTION: NADP-dependent D-xylose dehydrogenase catalyzing the
CC oxydation of D-xylose into D-xylonolactone. Also displays some, albeit
CC lower activity with D-glucose, D-galactose and L-arabinose as
CC substrate. Probably not involved in D-xylose degradation, as it has
CC been shown that H.jecorina assimilates D-xylose via D-xylose reductase
CC and xylitol dehydrogenase, and it is unable to grow on D-xylonic acid
CC as sole carbon source. May play a role in the regeneration of NADP(+)
CC in the presence of D-xylose. {ECO:0000269|PubMed:18031347}.
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:0000269|PubMed:18031347};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=250 uM for NADP(+) {ECO:0000269|PubMed:18031347};
CC KM=43 mM for D-xylose {ECO:0000269|PubMed:18031347};
CC KM=24 mM for D-glucose {ECO:0000269|PubMed:18031347};
CC KM=60 mM for L-arabinose {ECO:0000269|PubMed:18031347};
CC KM=100 mM for D-galactose {ECO:0000269|PubMed:18031347};
CC KM=145 mM for D-ribose {ECO:0000269|PubMed:18031347};
CC KM=390 mM for D-arabinose {ECO:0000269|PubMed:18031347};
CC Vmax=510 nmol/sec/mg enzyme toward NADP(+)
CC {ECO:0000269|PubMed:18031347};
CC Vmax=500 nmol/sec/mg enzyme toward D-xylose
CC {ECO:0000269|PubMed:18031347};
CC Vmax=130 nmol/sec/mg enzyme toward D-glucose
CC {ECO:0000269|PubMed:18031347};
CC Vmax=117 nmol/sec/mg enzyme toward L-arabinose
CC {ECO:0000269|PubMed:18031347};
CC Vmax=205 nmol/sec/mg enzyme toward D-galactose
CC {ECO:0000269|PubMed:18031347};
CC Vmax=141 nmol/sec/mg enzyme toward D-ribose
CC {ECO:0000269|PubMed:18031347};
CC Vmax=100 nmol/sec/mg enzyme toward D-arabinose
CC {ECO:0000269|PubMed:18031347};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; EF136590; ABO33081.1; -; mRNA.
DR EMBL; KI911139; ETS06670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024SMV2; -.
DR SMR; A0A024SMV2; -.
DR EnsemblFungi; ETS06670; ETS06670; M419DRAFT_31971.
DR KEGG; trr:M419DRAFT_31971; -.
DR HOGENOM; CLU_023194_7_2_1; -.
DR OrthoDB; 943656at2759; -.
DR BRENDA; 1.1.1.179; 6451.
DR SABIO-RK; A0A024SMV2; -.
DR Proteomes; UP000024376; Unassembled WGS sequence.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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 1: Evidence at protein level;
KW NADP; Oxidoreductase.
FT CHAIN 1..391
FT /note="D-xylose 1-dehydrogenase (NADP(+))"
FT /id="PRO_0000435965"
SQ SEQUENCE 391 AA; 42787 MW; 6814B67C0C37024A CRC64;
MASGNPYTLK WGIMATGGIA ETFCKDLLCN PAIRGADDVR HEIVAVASSS SSKRAEEFLQ
RIDGAFDAKT YGSYPELVAD PNVDIVYVAT PHSHHFQNTM LALEAGKNVL CEKAFTVTAA
QARKLVETAK AKKLFLMEAV WTRYFPLSIK IRELIAAGEI GTVFRTIADL SINANSEQGQ
ALKFADSHRM VNPDLAGGAT LDLGVYPLTW VFQTLYHLQP EEDKEAPTVV ASSNKYTTGA
DENTAIICSF PRHNSIGIAS TTMRADTDPE KDTIPAVRIQ GSKGEIQVFF PTYRPLKYKV
VKTNGEAQTV DCPIPGDPAR KGSGHGMFWE ADECARCLRD GKLESATLPW KESIVIMETM
EEALRQGGVT YPELITTDVY DPKSPLNTGN Q
