ID B8NCC8_ASPFN Unreviewed; 337 AA.
AC B8NCC8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=AFLA_041030 {ECO:0000313|EMBL:EED52401.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED52401.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED52401.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963476; EED52401.1; -; Genomic_DNA.
DR RefSeq; XP_002377565.1; XM_002377524.1.
DR AlphaFoldDB; B8NCC8; -.
DR STRING; 332952.B8NCC8; -.
DR EnsemblFungi; EED52401; EED52401; AFLA_041030.
DR VEuPathDB; FungiDB:AFLA_007669; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR OMA; RICAFSA; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd19071; AKR_AKR1-5-like; 1.
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.
PE 4: Predicted;
FT DOMAIN 27..291
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 67
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 92
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 337 AA; 37697 MW; 2010ED23E6368B8F CRC64;
MMADEYSDSP QGSTIFELNN GMKIPALGFG AMKKGLVLPE EERDYVRSLI VQAIKAGYRL
IDTSKIYATE DLVGEAIKES GVPRSEITVL TKLSSDDHHD VRAAFERSRR LLDTYIDIYI
MHWPQGFTKD VSRPLAPEES PTYIEVYKEM EKLVGPDCRG IGVGNLTQRT LDMLLKETEI
KPVVNEIEIH PGNPNTKLVP YCLERGIRPV AWGPLAGGPT SHYSDTSSIY ESSVLTSLSS
RYELSVGTII LSWLVQRGIV VIPHSSSLAR LSENRRLARL TDLEIQEINS LHEEIGRTRL
IDSVPQVWME VPGKGKTIMG WTVQEIGWVD DKGECLV
//
