ID W9Y7E6_9EURO Unreviewed; 398 AA.
AC W9Y7E6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming) {ECO:0000256|ARBA:ARBA00038984};
DE EC=1.1.1.179 {ECO:0000256|ARBA:ARBA00038984};
DE AltName: Full=D-xylose-NADP dehydrogenase {ECO:0000256|ARBA:ARBA00042988};
GN ORFNames=A1O3_01831 {ECO:0000313|EMBL:EXJ88767.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ88767.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ88767.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ88767.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH;
CC Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.179; Evidence={ECO:0000256|ARBA:ARBA00036678};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC {ECO:0000256|ARBA:ARBA00010928}.
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:EXJ88767.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMGY01000002; EXJ88767.1; -; Genomic_DNA.
DR RefSeq; XP_007730164.1; XM_007731974.1.
DR AlphaFoldDB; W9Y7E6; -.
DR STRING; 1182542.W9Y7E6; -.
DR GeneID; 19165964; -.
DR eggNOG; KOG2741; Eukaryota.
DR HOGENOM; CLU_023194_7_2_1; -.
DR OrthoDB; 2898964at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR22604:SF115; DIHYDRODIOL DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G07520)-RELATED; 1.
DR PANTHER; PTHR22604; OXIDOREDUCTASES; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019478}.
FT DOMAIN 7..134
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT REGION 308..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 43795 MW; 4F77BCD68570C17E CRC64;
MAPKLIRWGI LATGGIAETF TRDLLVDPTT RNVHEIKHTV VAAASSSSTS RAQEFLKSVN
APSSAVAYGS YEELVKNQDV DIVYVATPHS HHYQNVMLCL DAGKNVLCEK AFTVNAAQAR
KLIETAREKN LFLMEAVWTR YFPLSIYARE AITSGRLGTV TRVYSDNSSA QDPEKQWPDG
KHRMINPDLA GGALLDMGIY SLTWVFQTLY TTQPPHSRKA PRVVSSVKKY LPTGVDEMTT
MLLTFPRDAD LGGDIHAIAT TSFRTTNNVD GTGTAGPAVR IQGTEGELQV WPPIYRPTRT
RLILKDGTTE DKSWPQPGPG AGSGWHNGFG GGNNAEGEGH GMFWEADEAA LALVEGRKEG
RFESLDESLV IMEVMDEVRR QNGLDYPEKI ETTDRIPL
//