ID D4AJM6_ARTBC Unreviewed; 314 AA.
AC D4AJM6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=ARB_04476 {ECO:0000313|EMBL:EFE36949.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE36949.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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 -!- 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:EFE36949.1}.
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DR EMBL; ABSU01000001; EFE36949.1; -; Genomic_DNA.
DR RefSeq; XP_003017594.1; XM_003017548.1.
DR AlphaFoldDB; D4AJM6; -.
DR STRING; 663331.D4AJM6; -.
DR GeneID; 9522439; -.
DR KEGG; abe:ARB_04476; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_1_1; -.
DR OMA; PVCWDPT; -.
DR OrthoDB; 5305445at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; PTHR43827; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 1.
DR PANTHER; PTHR43827:SF3; ALDO-KETO 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; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT DOMAIN 83..292
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 108
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 314 AA; 35511 MW; 4FFB534E4E25C810 CRC64;
MATNLVRLSM VMSISSTPSF VGILSQNARK VATMAARSNI QSTKKMNSGY EIPVVGFGVS
GQLPSRTVWL LTTLNRCTKP KAYHNEAECG EAIRKSGLKR SEVFFTTKVP WRSLGYEPTR
EAIESSLKEA KVDYFDLVLL HAPYGGKEKR EGSWKALVEA QKEGKVRSIG VSNYGVHHLD
ELEEYNKAIG GKIDVGQYEL HPWLTRSDIV EWLQKRNIVI EAYSPLVQAK KMDDPKLQEI
AKKHNKSPAQ VLVRWSLQKG FVPLPKSATE KRILENSDIF DFELSQDDMR ALHTDEYHHV
CWDPTTHKDG DNIP
//
