ID G1XRC7_ARTOA Unreviewed; 355 AA.
AC G1XRC7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=D-xylulose reductase {ECO:0000256|ARBA:ARBA00026119};
DE EC=1.1.1.9 {ECO:0000256|ARBA:ARBA00026119};
DE AltName: Full=Xylitol dehydrogenase A {ECO:0000256|ARBA:ARBA00030139};
GN ORFNames=AOL_s00193g126 {ECO:0000313|EMBL:EGX44398.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX44398.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX44398.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(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|ARBA:ARBA00024843}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
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|ARBA:ARBA00025713}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:EGX44398.1}.
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DR EMBL; ADOT01000287; EGX44398.1; -; Genomic_DNA.
DR RefSeq; XP_011127039.1; XM_011128737.1.
DR AlphaFoldDB; G1XRC7; -.
DR STRING; 756982.G1XRC7; -.
DR GeneID; 22897929; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; G1XRC7; -.
DR OMA; VCEMSGH; -.
DR OrthoDB; 3017546at2759; -.
DR Proteomes; UP000008784; 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:InterPro.
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; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..350
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 355 AA; 38136 MW; 7BDF7F54E0EFF681 CRC64;
MSGPQNLSFV LAKPLDVKFE DRPIPELKDP REVLVRVRVT GICGSDVHYW QHGRIGDFIL
KAPMVLGHES AGEIVKVGSA VTDLQPGDRV CMEPGVPCRH CPECKFGKYN LCHDMRFAAT
PPYDGTLAKY YVLPQDFCYK LPENVSLEEG ALMEPLSVGV HVVKQAQVKP GDSVVVFGAG
PVGLLCCSVA KAFGATKVVA VDIVPSRLEF AKKYAATGTF QPTKEGTPAS NAAQIIKENG
LGVGADVVID ASGAEPSIQT SIHVARNGGT FVQAGMGRPD ITFPITALCV KELTVKGSFR
YGAGDYKLAV ELLAHGRLSV KELITKEVKF EDAEKAFEEV KNGKGIKILI RGPED
//
