ID A0A0N0NJQ4_9EURO Unreviewed; 364 AA.
AC A0A0N0NJQ4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AB675_3632 {ECO:0000313|EMBL:KPI37158.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI37158.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI37158.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI37158.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) 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:KPI37158.1}.
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DR EMBL; LFJN01000026; KPI37158.1; -; Genomic_DNA.
DR RefSeq; XP_017997121.1; XM_018143700.1.
DR AlphaFoldDB; A0A0N0NJQ4; -.
DR STRING; 1664694.A0A0N0NJQ4; -.
DR GeneID; 28735580; -.
DR OrthoDB; 5305445at2759; -.
DR Proteomes; UP000038010; 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:SF507; ALDO_KET_RED DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00248; Aldo_ket_red; 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:UP000038010};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..364
FT /note="D-xylose reductase [NAD(P)H]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005856813"
FT DOMAIN 54..326
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
SQ SEQUENCE 364 AA; 40625 MW; E6F8656F426564CF CRC64;
MLNTLTAALT CCLLLTIPAH TFSLPPILTS NEDHDHQKPI KHPKHHPPLD IPFIGLGLWN
SKGSDATHAV DAAFGTGYIH FDSAAAYSNE EYVGSGLTNV SIPRSSYWIT SKLWNTAHQP
SLVEPALRKT LSDLQTPYLD LYLMHWPVAF VPNPPKGRNS IIDQDTSILN TWRAMESLVH
KNLTRYIGVS NFSPRQLDTI LAACKTEKGG ICPYAHEFET HPYLQQTEFV EWHLKHDIKV
IAYSPLANLN PTYNGTHSDV PSILEDPFWQ DLAANKSITV PQAVLGWGIQ RGTVVIPKSV
HAKRIKENLG AVDVNFTGLE MARIAEEDRR VRFNDPTKGW GVEPPLFEGL DGGSNRFVVE
QEEL
//
