ID A0A0F4YF88_TALEM Unreviewed; 391 AA.
AC A0A0F4YF88;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=T310_9605 {ECO:0000313|EMBL:KKA16785.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA16785.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA16785.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA16785.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-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}.
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:KKA16785.1}.
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DR EMBL; LASV01000734; KKA16785.1; -; Genomic_DNA.
DR RefSeq; XP_013323397.1; XM_013467943.1.
DR AlphaFoldDB; A0A0F4YF88; -.
DR STRING; 1408163.A0A0F4YF88; -.
DR GeneID; 25321537; -.
DR OrthoDB; 2898964at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:KKA16785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT DOMAIN 8..135
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
SQ SEQUENCE 391 AA; 43444 MW; 52C76EBC825C101E CRC64;
MASPFNARWG ILATGGIAAT FVKDLLKNPK LRGTNDVTHT VTAVASSSSK ARAEQFIAET
KIPGPCAAYG SYAELVKDPN VDIIYVATPH SHHYQNTMLA LEAGKHVLCE KAFTVNAAQA
KILCETAKKK NLFLMEAVWT RYFPLSIKVR ELIQKGEIGE VLRVIADNSF GEDVETVWGT
QHRMVNKDLA GGALLDLGIY SLTWVFQTLY HTLPRSQRKP PSAIATHMTP YHLTGADEAT
TMLITFPTTT PSNLPNQTSH AVAMTHLRIA TDPDKNNSTR PAIRIQGTKG EIQVDGPAFR
PVRFRVIPRK DENATEPVTI REETFPFPDN GHGMYWEADE AARCVRDGKL ESETLPWEES
ILIMEVMDEV RRQGGLTYPE KIESTVYPLQ L
//
