XYL2_ASPOR
ID XYL2_ASPOR Reviewed; 358 AA.
AC Q86ZV0;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=D-xylulose reductase A;
DE EC=1.1.1.9 {ECO:0000269|PubMed:16233653};
DE AltName: Full=Xylitol dehydrogenase A;
GN Name=xdhA; ORFNames=AO090038000631;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=16233653; DOI=10.1016/s1389-1723(04)70229-7;
RA Tran L.H., Kitamoto N., Kawai K., Takamizawa K., Suzuki T.;
RT "Cloning and expression of a NAD+-dependent xylitol dehydrogenase gene
RT (xdhA) of Aspergillus oryzae.";
RL J. Biosci. Bioeng. 97:419-422(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CICC 2012, and CICC 2120;
RA Chen H.W., Tan C.H., Liu W., Lin R.;
RT "Cloning and expression of xylitol dehydrogenase (XDH) of Aspergillus
RT oryzae.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
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.R., 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 -!- FUNCTION: Xylitol dehydrogenase which catalyzes the conversion of
CC xylitol to D-xylulose. Xylose is a major component of hemicelluloses
CC such as xylan. Most fungi utilize D-xylose via three enzymatic
CC reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and
CC xylulokinase, to form xylulose 5-phosphate, which enters pentose
CC phosphate pathway. {ECO:0000269|PubMed:16233653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + xylitol = D-xylulose + H(+) + NADH;
CC Xref=Rhea:RHEA:20433, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:17151, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.9;
CC Evidence={ECO:0000269|PubMed:16233653};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20434;
CC Evidence={ECO:0000305|PubMed:16233653};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC step 4/5. {ECO:0000305|PubMed:16233653}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB109101; BAC75870.2; -; Genomic_DNA.
DR EMBL; GQ222265; ACR55076.1; -; Genomic_DNA.
DR EMBL; GQ222266; ACR55077.1; -; Genomic_DNA.
DR EMBL; AP007169; BAE64390.1; -; Genomic_DNA.
DR RefSeq; XP_001825523.1; XM_001825471.2.
DR AlphaFoldDB; Q86ZV0; -.
DR SMR; Q86ZV0; -.
DR STRING; 510516.Q86ZV0; -.
DR EnsemblFungi; BAE64390; BAE64390; AO090038000631.
DR GeneID; 5997618; -.
DR KEGG; aor:AO090038000631; -.
DR VEuPathDB; FungiDB:AO090038000631; -.
DR HOGENOM; CLU_026673_11_5_1; -.
DR OMA; ETWYAMS; -.
DR BioCyc; MetaCyc:MON-13192; -.
DR BRENDA; 1.1.1.9; 522.
DR UniPathway; UPA00146; UER00577.
DR Proteomes; UP000006564; Chromosome 6.
DR GO; GO:0046526; F:D-xylulose reductase activity; IDA:AspGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042843; P:D-xylose catabolic process; IC:AspGD.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
DR GO; GO:0019697; P:L-xylitol catabolic process to xylulose 5-phosphate; IMP:AspGD.
DR CDD; cd05285; sorbitol_DH; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Xylose metabolism; Zinc.
FT CHAIN 1..358
FT /note="D-xylulose reductase A"
FT /id="PRO_0000393511"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 182..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 358 AA; 38222 MW; 29CFC0D386D46741 CRC64;
MGAPPKTAQN LSFVLEGIHK VKFEDRPIPQ LRDAHDVLVD VRFTGICGSD VHYWEHGSIG
QFVVKDPMVL GHESSGVISK VGSAVTTLKV GDHVAMEPGI PCRRCEPCKE GKYNLCEKMA
FAATPPYDGT LAKYYVLPED FCYKLPENIN LQEAAVMEPL SVAVHIVKQA NVAPGQSVVV
FGAGPVGLLC CAVARAFGSP KVIAVDIQKG RLEFAKKYAA TAIFEPSKVS ALENAERIVN
ENDLGRGADI VIDASGAEPS VHTGIHVLRP GGTYVQGGMG RNEITFPIMA ACTKELNVRG
SFRYGSGDYK LAVNLVASGK VSVKELITGV VSFEDAEQAF HEVKAGKGIK TLIAGVDV
