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Database: UniProt
Entry: W7LM86_GIBM7
LinkDB: W7LM86_GIBM7
Original site: W7LM86_GIBM7 
ID   W7LM86_GIBM7            Unreviewed;       375 AA.
AC   W7LM86;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=L-arabinitol 4-dehydrogenase {ECO:0000256|ARBA:ARBA00039783};
DE            EC=1.1.1.12 {ECO:0000256|ARBA:ARBA00038954};
GN   ORFNames=FVEG_00541 {ECO:0000313|EMBL:EWG36570.1};
OS   Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS   fungus) (Fusarium verticillioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG36570.1, ECO:0000313|Proteomes:UP000009096};
RN   [1] {ECO:0000313|EMBL:EWG36570.1, ECO:0000313|Proteomes:UP000009096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arabinitol + NAD(+) = H(+) + L-xylulose + NADH;
CC         Xref=Rhea:RHEA:16381, ChEBI:CHEBI:15378, ChEBI:CHEBI:17399,
CC         ChEBI:CHEBI:18403, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00035840};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC       step 2/5. {ECO:0000256|ARBA:ARBA00037881}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; DS022242; EWG36570.1; -; Genomic_DNA.
DR   RefSeq; XP_018742761.1; XM_018887062.1.
DR   AlphaFoldDB; W7LM86; -.
DR   STRING; 334819.W7LM86; -.
DR   EnsemblFungi; FVEG_00541T0; FVEG_00541T0; FVEG_00541.
DR   GeneID; 30058905; -.
DR   KEGG; fvr:FVEG_00541; -.
DR   VEuPathDB; FungiDB:FVEG_00541; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_5_1; -.
DR   OMA; MRVAMYY; -.
DR   OrthoDB; 3017546at2759; -.
DR   Proteomes; UP000009096; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0019568; P:arabinose catabolic process; IEA:UniProtKB-KW.
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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR045306; SDH-like.
DR   PANTHER; PTHR43161:SF12; L-ARABINITOL 4-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022935};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          53..163
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          202..333
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   375 AA;  39824 MW;  CF961DF73B78C574 CRC64;
     MSPSAVEGNG VADVKTTLKP NIGVYTNPNH DLWVTAAEPS AEAVKSGSDL KHGEVSVAIR
     STGICGSDVH FWHAGCIGPM IVEGDHILGH ESAGEVIAVH PSVSHLKVGD RVAVEPNIPC
     GTCEPCLTGR YNGCESVLFL STPPVPGMLR RYINHPAVWC HKIGNMSFEN GALLEPLSVA
     LAGMQRAQVA LGDPVLICGA GPIGLITLQC CAAAGASPIV ITDISESRLA FAKELCPRVI
     THKVERQSAE DSAKAIVKTF GGIEPSVALE CTGVESSIAA AVWSVKFGGK VFIIGVGKNE
     INIPFMRASV REVDIQLQYR YCNTWPRAIR LVENNVVDLS KLVTHKFKLE DAIKAFETSA
     DAKSGAIKVM IQSLD
//
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