ID G7XPD7_ASPKW Unreviewed; 319 AA.
AC G7XPD7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=AKAW_06797 {ECO:0000313|EMBL:GAA88683.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA88683.1};
RN [1] {ECO:0000313|EMBL:GAA88683.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA88683.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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 -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC {ECO:0000256|ARBA:ARBA00004722}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC {ECO:0000256|ARBA:ARBA00007905}.
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DR EMBL; DF126464; GAA88683.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XPD7; -.
DR STRING; 1033177.G7XPD7; -.
DR VEuPathDB; FungiDB:AKAW_06797; -.
DR eggNOG; KOG1577; Eukaryota.
DR InParanoid; G7XPD7; -.
DR UniPathway; UPA00810; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0032866; F:D-xylose:NADP reductase activity; IEA:InterPro.
DR GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd19115; AKR_AKR2D1; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044487; AKR2D.
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:SF218; NADPH-DEPENDENT ALDOSE REDUCTASE GRE3; 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.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629}.
FT DOMAIN 18..300
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 50
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 79
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 319 AA; 36023 MW; 1FE65165F737F149 CRC64;
MASPTVKLNS GYDMPLVGFG LWKVNNDTCA DQIYHAIKEG YRLFDGACDY GNEVEAGQGV
ARAIKDGLVK REELFIVSKL WNSFHDGDRV EPICRKQLAD WGIDYFDLYI VHFPISLKYV
DPAVRYPPGW MSENDKLEFG NATIQETWTA MESLVDKKLA RSIGISNFSA QLVMDLLRYA
RIRPATLQIE HHPYLTQTRL VEYAQKEGLT VTAYSSFGPL SFLELSVQNA VDTPPLFEHQ
LVKGIAEKHG RTPAQVLLRW ATQRGVAVIP KSNNPQRLKQ NLDVTGWNLE EEEIKAIAGL
DRGLRFNDPL GYGLYAPIF
//
