ID Q2TZV5_ASPOR Unreviewed; 340 AA.
AC Q2TZV5;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=AO090011000704 {ECO:0000313|EMBL:BAE65160.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE65160.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE65160.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007171; BAE65160.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2TZV5; -.
DR STRING; 510516.Q2TZV5; -.
DR EnsemblFungi; BAE65160; BAE65160; AO090011000704.
DR VEuPathDB; FungiDB:AO090011000704; -.
DR HOGENOM; CLU_852535_0_0_1; -.
DR OrthoDB; 2898964at2759; -.
DR Proteomes; UP000006564; Chromosome 7.
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:UP000006564}.
FT DOMAIN 18..115
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT REGION 310..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 37569 MW; 70317644DB97696E CRC64;
MVEYRKTKIN TSQAQDALLR ALASSRSEEV AQEFITVVQA PSYCQAYRNY SDLVNCPTID
VIYIATPHSH HFQNAMLALE AGKHVLCEKN FTVNAGQAKK LSTVAEKKQR FLMEGLWTRF
LPVSVEVRQF LQAGAIGTVT RVFADNGLGM DPYSDFLPGD LMVVKELAGG ALLDLGVYSI
HWVLQAMPKT NRRPIQILST TTEYAVSGVD ETTTILMRFA PSTADGPEIQ ATASASLRAI
TDPDGETAAV RIQGDQGETQ IYGWPWCPSR LRVIRRGPGM NNRGTINRQD RPSTRRSIWT
LLRGGRSCTL HLPRSSRESR DALAREHDSN GDHGYSAAGE
//