ID D4AIV0_ARTBC Unreviewed; 420 AA.
AC D4AIV0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=ARB_04198 {ECO:0000313|EMBL:EFE36673.1};
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:EFE36673.1, 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 -!- 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:EFE36673.1}.
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DR EMBL; ABSU01000001; EFE36673.1; -; Genomic_DNA.
DR RefSeq; XP_003017318.1; XM_003017272.1.
DR AlphaFoldDB; D4AIV0; -.
DR STRING; 663331.D4AIV0; -.
DR GeneID; 9524427; -.
DR KEGG; abe:ARB_04198; -.
DR eggNOG; KOG2741; Eukaryota.
DR HOGENOM; CLU_023194_5_2_1; -.
DR OMA; EEAFHWQ; -.
DR OrthoDB; 5486222at2759; -.
DR Proteomes; UP000008866; 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 Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT DOMAIN 41..132
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT REGION 397..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 47366 MW; B33F8486B81E47E3 CRC64;
MALFLQGCEF ARQYTSSLFH GRSQPSKRAL KLGVLSNAKI SAAAVASMDP QMAKTATEKY
GFSKSYRSFR DLLDDPLINI VHISLPPNIF FEWATNALTA GKHVICEKPS TANADEARTL
IDDAERRGLI LQDAFHWQFH PAAHRFKEIV DSKRYGRIIR TDAWMTSSPA VPDADPRWQY
DQGGRRTSTN ARPFLTLFLL IMIPFIGGSL MDGSYALSFT QYVLPSKRPK RILSAAARPS
RDDSRVDAAM HALLLFEDEK GNPITSRIYT DMSRSRLGGI LPRVWELPSI EVETDAAILY
FYNAMMPHIY HYISITDKRT GITEYKTQSS GGPLWDERWT TGGKGGKSHW STYRWQLEAF
LEKVRGKEPI CCISNDDAIY NTECIDKIYK EAGMPVRADP EEIRTGERGQ MPGKTEKSSG
//