ID S7ZDZ0_PENO1 Unreviewed; 313 AA.
AC S7ZDZ0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=PDE_03786 {ECO:0000313|EMBL:EPS28840.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS28840.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS28840.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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};
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DR EMBL; KB644411; EPS28840.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZDZ0; -.
DR STRING; 933388.S7ZDZ0; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR OrthoDB; 5305445at2759; -.
DR PhylomeDB; S7ZDZ0; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF504; GLYCEROL 2-DEHYDROGENASE (NADP(+))-RELATED; 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.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT DOMAIN 19..285
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 52
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 81
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 313 AA; 34646 MW; 9B4472B916C3C967 CRC64;
MAAADVRFKL NTGAEIPALG LGTWQSAPGE VARAVYHAIK VGYRHIDGAM CYGNENEVGQ
GIKQAIDEGI VTREDLFVTT KLWCTYHARV QEGLDESLQN LGLDYVDLYL MHWPLAMNPN
GNHPMFPKLE DGSRDIVHDH SHVTTWKSME KLVGSGKVRA IGVSNYSVKY LEELLPQATV
VPAVNQIENH PSLPQQEIVD FCKQKGIHIT AYSPLGSTGN VLFKAKPIVE VSEKRGVSPA
SILLSWHIAR GSSVLAKSVN PDRIEANRKD LIHLDSEDMA TIQKYIDELA ATNSFQRLVF
PPFGKTFGFP DKE
//
