ID G7XDC4_ASPKW Unreviewed; 358 AA.
AC G7XDC4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=D-xylulose reductase {ECO:0000256|RuleBase:RU369026};
DE EC=1.1.1.9 {ECO:0000256|RuleBase:RU369026};
DE AltName: Full=Xylitol dehydrogenase {ECO:0000256|RuleBase:RU369026};
GN ORFNames=AKAW_02909 {ECO:0000313|EMBL:GAA84795.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA84795.1};
RN [1] {ECO:0000313|EMBL:GAA84795.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA84795.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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:0000256|RuleBase:RU369026}.
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:0000256|RuleBase:RU369026};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU369026};
CC Note=Binds 1 or 2 Zn(2+) ions per subunit.
CC {ECO:0000256|RuleBase:RU369026};
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:0000256|RuleBase:RU369026}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; DF126452; GAA84795.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XDC4; -.
DR STRING; 1033177.G7XDC4; -.
DR VEuPathDB; FungiDB:AKAW_02909; -.
DR eggNOG; KOG0024; Eukaryota.
DR InParanoid; G7XDC4; -.
DR UniPathway; UPA00146; UER00577.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR CDD; cd05285; sorbitol_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_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 PANTHER; PTHR43161:SF13; D-XYLULOSE REDUCTASE; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU369026};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277}; NAD {ECO:0000256|RuleBase:RU369026};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU369026};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW ECO:0000256|RuleBase:RU369026};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..351
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 358 AA; 38825 MW; 8C2C8B8F44E38DA7 CRC64;
MEILQQKPTN YAIHTSPAND LRLVECEIPK IAPTECLVHV RATGICGSDV HFWKHGHIGP
MIVTGDNGLG HESAGVVLQV GEAVTRFKPG DRVALECGVP CSKPTCDFCR TGLYHACPDV
VFFSTPPHHG TLRRYHAHPE AWLHKIPDHV SFEEGSLLEP LTVALAGIDR SGLRLADPLV
ICGAGPIGLV TLLAANAAGA EPIVITDLDE NRLAKAKELV PRVRPVKVEK GESSADLGQR
IISELGQEAK LVMECTGVES SVHAGIYATR FGGTVFVIGV GKDFQNIPFM HMSAKEINLK
FQYRYHDIYP KSIALVAAGM IDLKPLVSHR YKLEEGLQAF DTASNPRSGA IKVQILDD
//
