ID A0A0C9YEN8_9AGAR Unreviewed; 394 AA.
AC A0A0C9YEN8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=K443DRAFT_84097 {ECO:0000313|EMBL:KIK08907.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK08907.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK08907.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK08907.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN838540; KIK08907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9YEN8; -.
DR STRING; 1095629.A0A0C9YEN8; -.
DR HOGENOM; CLU_023194_5_2_1; -.
DR OrthoDB; 2898964at2759; -.
DR Proteomes; UP000054477; 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; OXIDOREDUCTASES; 1.
DR PANTHER; PTHR22604:SF105; TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT DOMAIN 27..148
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
SQ SEQUENCE 394 AA; 43492 MW; 5DE9C4A9B13A0FDC CRC64;
MAWCLDFVKR VSNPSVDPVT TASQPVKFGI LGAAAIAPPA LISPAKSHPE VQVYAVAARD
QKRAEAFAKK HGIEKAYGGS TGYQQLLDDP EVEAVYNPLP NSLHYECTMK ALAAGKHVLL
EKPGADTAEE TREMFKLAES KGLILMEAFH YRFHPAVQRL KAIVDGGELG AVKHISTSLT
VPKGIMRPGD IRYEYELGGG ALMDMGCYTL SCLRYLSSSE PVSIESAMHE VYVPPSPPSD
YVRNVDRRTV ADLLFPKGVT GTITCDLAMP PTLGVIPKMP QISAVVKCEN GEVELFNFVA
PAIYHWIKVK VVDGNGKAKT RVEKVYRFDG EEKGKEWSTY RYQLEGFVDQ LKGRKPQTWI
TKEDSVANME WIEKIYEKTG LGSRRKSSYV AVTS
//
