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Database: UniProt
Entry: A0A1V6ZAY7_PENNA
LinkDB: A0A1V6ZAY7_PENNA
Original site: A0A1V6ZAY7_PENNA 
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
//
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