ID A0A1V6ZAY7_PENNA Unreviewed; 325 AA.
AC A0A1V6ZAY7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=D-xylose reductase [NAD(P)H] {ECO:0000256|ARBA:ARBA00012845};
DE EC=1.1.1.307 {ECO:0000256|ARBA:ARBA00012845};
GN ORFNames=PENNAL_c0001G09538 {ECO:0000313|EMBL:OQE96644.1},
GN PNAL_LOCUS53 {ECO:0000313|EMBL:CAG7936041.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE96644.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|EMBL:OQE96644.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|EMBL:OQE96644.1};
RA Nielsen J.C., Nielsen J.;
RT "Uncovering the secondary metabolism of Penicillium species provides
RT insights into the evolution of 6-MSA pathways.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
RN [3] {ECO:0000313|EMBL:CAG7936041.1}
RP NUCLEOTIDE SEQUENCE.
RA Branca A.L. A.;
RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the initial reaction in the xylose utilization
CC pathway by reducing D-xylose into xylitol. Xylose is a major component
CC of hemicelluloses such as xylan. Most fungi utilize D-xylose via three
CC enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase
CC (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters
CC pentose phosphate pathway. {ECO:0000256|ARBA:ARBA00025065}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + xylitol = D-xylose + H(+) + NADH;
CC Xref=Rhea:RHEA:27441, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.307; Evidence={ECO:0000256|ARBA:ARBA00000578};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + xylitol = D-xylose + H(+) + NADPH;
CC Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.307; Evidence={ECO:0000256|ARBA:ARBA00001334};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE96644.1}.
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DR EMBL; CAJVNV010000002; CAG7936041.1; -; Genomic_DNA.
DR EMBL; MOOB01000001; OQE96644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6ZAY7; -.
DR STRING; 60175.A0A1V6ZAY7; -.
DR OMA; ACATNQV; -.
DR OrthoDB; 5305445at2759; -.
DR Proteomes; UP000191691; Unassembled WGS sequence.
DR Proteomes; UP001153461; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR PANTHER; PTHR11732:SF449; D-XYLOSE REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000191691}.
FT DOMAIN 18..296
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 53
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 83
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 325 AA; 36477 MW; 74E450B087C1CC43 CRC64;
MSSGKTFTLN NGVTIPAVGF GTFASEGSKG ETYAAVTAAL NIGYRHLDCA WFYLNEDEVG
DGIRDFLKAN PSVKRSDIFV TTKVWNHLHR YDDVLWSVNN SLERMKLDYV DLFLVHWPIA
AEKDGQEKPK IGPDGKYVIL KDLTENHEET WRAMEKLYAD GKAKAIGVSN WTIPQLEAMA
KFAKVQPMVN QIEIHPFLAN DELVQYCFSH NILPQAYSPL GSQNQVPTTG ERVSENKTLN
DIAEKGGNTL AQVLIAWGLR RGYSVLPKSS NPKRIESNFK SIELNDADFE AVNEVAKTHH
CRFVNMRDTF GYDVWPEETA SGLSI
//