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Database: UniProt
Entry: Q4WT02_ASPFU
LinkDB: Q4WT02_ASPFU
Original site: Q4WT02_ASPFU 
ID   Q4WT02_ASPFU            Unreviewed;       383 AA.
AC   Q4WT02;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 114.
DE   SubName: Full=Xylitol dehydrogenase {ECO:0000313|EMBL:EAL90430.1};
DE            EC=1.1.1.14 {ECO:0000313|EMBL:EAL90430.1};
GN   ORFNames=AFUA_1G11030 {ECO:0000313|EMBL:EAL90430.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90430.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90430.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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. {ECO:0000256|ARBA:ARBA00004921}.
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:EAL90430.1}.
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DR   EMBL; AAHF01000004; EAL90430.1; -; Genomic_DNA.
DR   RefSeq; XP_752468.1; XM_747375.1.
DR   AlphaFoldDB; Q4WT02; -.
DR   STRING; 330879.Q4WT02; -.
DR   EnsemblFungi; EAL90430; EAL90430; AFUA_1G11030.
DR   GeneID; 3510395; -.
DR   KEGG; afm:AFUA_1G11030; -.
DR   VEuPathDB; FungiDB:Afu1g11030; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_5_1; -.
DR   InParanoid; Q4WT02; -.
DR   OMA; RYGATHT; -.
DR   OrthoDB; 3017546at2759; -.
DR   UniPathway; UPA00146; UER00577.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006062; P:sorbitol catabolic process; IBA:GO_Central.
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:SF3; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02000)-RELATED; 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|ARBA:ARBA00022629};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EAL90430.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          36..369
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   383 AA;  41258 MW;  E4866653035C639B CRC64;
     MAFTETLVRP KSVPVNELPD QTSFQNVNHA FILSPGGTFC YKERPTPKIE SERDVIVRVV
     ATGLCGSDVH YWQHGRIGRY AVNRPIVLGH ESSGVIVACG SNVDGLKVGD RVALEPGISC
     NTCKYCRSGH YNLCKSMVFA ATPPYDGTLS TFYKVPAECC YKLPVHISLR DGALVEPLSV
     AVHACRLAGD MQNKSVVVFG AGPVGLLCCS VASAFGAAKV VAVDVVKTRL ATATKYGATH
     RYEMDAEKKN AEELSATAAL EDGADIILDA TGAEPCLNCG LDILRSGGTF VQVGLGNPTL
     MFPVGQVCDK EVVFKGSFRY GPGDYALAIG LLESRRVQLD GMVTHEFSFW KAQEAFQNVV
     HRQGIKCIIY GPGIDEEWAR IAD
//
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