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Database: UniProt
Entry: E4UZQ8_ARTGP
LinkDB: E4UZQ8_ARTGP
Original site: E4UZQ8_ARTGP 
ID   E4UZQ8_ARTGP            Unreviewed;       349 AA.
AC   E4UZQ8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=D-xylulose reductase {ECO:0000256|ARBA:ARBA00026119, ECO:0000256|RuleBase:RU369026};
DE            EC=1.1.1.9 {ECO:0000256|ARBA:ARBA00026119, ECO:0000256|RuleBase:RU369026};
DE   AltName: Full=Xylitol dehydrogenase {ECO:0000256|RuleBase:RU369026};
DE   Flags: Fragment;
GN   ORFNames=MGYG_05846 {ECO:0000313|EMBL:EFR02845.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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       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|ARBA:ARBA00025713,
CC       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; DS989826; EFR02845.1; -; Genomic_DNA.
DR   RefSeq; XP_003171299.1; XM_003171251.1.
DR   AlphaFoldDB; E4UZQ8; -.
DR   STRING; 535722.E4UZQ8; -.
DR   GeneID; 10027309; -.
DR   VEuPathDB; FungiDB:MGYG_05846; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_5_1; -.
DR   InParanoid; E4UZQ8; -.
DR   OMA; LKGVFHN; -.
DR   OrthoDB; 3017546at2759; -.
DR   UniPathway; UPA00146; UER00577.
DR   Proteomes; UP000002669; 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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW   Xylose metabolism {ECO:0000256|RuleBase:RU369026};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..344
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFR02845.1"
SQ   SEQUENCE   349 AA;  37178 MW;  C568B6C5D3639CA3 CRC64;
     NLSFVLDGIR KVKFEDRPVP ALNNAYDVLI TVKYTGICGS DVHYWDHGSI GPFVLKEPMV
     LGHESSGIVA EIGSAVQSLK VGDKVALEPG ICCRRCEPCK SGKYNLCVDM AFAATPPYDG
     TLARYYVLPE DFCYKLPDTM DLKDGALMEP LGVAIHITRQ AEVKPGDTVV VFGAGPVGLL
     CCAASRAFGA AKIVAVDIQP GRLEFASKYA ATGVFLPGNV SAIENAEKLR SEHELGRGAD
     VVIDASGAEQ SVHTGIHIAR PGGTYVQGGM GRDEISFPIM AACTKELNIK GSFRYNSGDY
     KLALELVGSG KLSVKELVTK VVDFTDAEQA FLEVKSGKGI KTLIAGVEN
//
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