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Database: UniProt
Entry: B6H9K2_PENRW
LinkDB: B6H9K2_PENRW
Original site: B6H9K2_PENRW 
ID   B6H9K2_PENRW            Unreviewed;       362 AA.
AC   B6H9K2;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 78.
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};
GN   ORFNames=Pc16g10990 {ECO:0000313|EMBL:CAP93769.1}, PCH_Pc16g10990
GN   {ECO:0000313|EMBL:CAP93769.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93769.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP93769.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920431; CAP93769.1; -; Genomic_DNA.
DR   RefSeq; XP_002561405.1; XM_002561359.1.
DR   AlphaFoldDB; B6H9K2; -.
DR   STRING; 500485.B6H9K2; -.
DR   GeneID; 8303789; -.
DR   KEGG; pcs:Pc16g10990; -.
DR   VEuPathDB; FungiDB:PCH_Pc16g10990; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_5_1; -.
DR   OMA; IRYTTGC; -.
DR   OrthoDB; 3017546at2759; -.
DR   BioCyc; PCHR:PC16G10990-MONOMER; -.
DR   UniPathway; UPA00146; UER00577.
DR   Proteomes; UP000000724; Contig Pc00c16.
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:UP000000724};
KW   Xylose metabolism {ECO:0000256|RuleBase:RU369026};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          11..358
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   362 AA;  39241 MW;  19DDECA26101AAA6 CRC64;
     MSETNRSFVL RAVKDVVLED RTVPTLKDPW DVRVHVAQTG ICGSDVHYWQ RGRIGDFILN
     SPIVLGHESS GTVVEVGSAV KSLNVGDRVA IEPGVPCRHC DYCRSGSYNL CPDTVFAATP
     PHDGTLSKYY ITQADYCYPV PAHMNLEEAA LVEPVAVAVQ ITKVGKVKPN QTVVVFGCGP
     IGLLCQAVCK AYSAKKVIGV DISQPRADFA KTFGADDVFV PPSRPEGTDD SAWNEAVARM
     MKEKFKLGEG PDVVLEATGA QACIQTGIHL TKKGGTYVQA GMGRENVIFP ITTACIRDLH
     IRGSIRYTAG CYPTAVDLIA SGKIDVKRLI TNRFKFEQAE EAFDLVRQGN ESVIKVIIEG
     VP
//
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