ID R9AEG8_WALI9 Unreviewed; 372 AA.
AC R9AEG8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Sorbitol dehydrogenase {ECO:0000313|EMBL:EOR00568.1};
GN ORFNames=J056_000766 {ECO:0000313|EMBL:EOR00568.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR00568.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
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; KE007234; EOR00568.1; -; Genomic_DNA.
DR RefSeq; XP_009268669.1; XM_009270394.1.
DR AlphaFoldDB; R9AEG8; -.
DR STRING; 1299270.R9AEG8; -.
DR GeneID; 20373718; -.
DR KEGG; wic:J056_000766; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_5_1; -.
DR OMA; KLIMVGM; -.
DR OrthoDB; 3017546at2759; -.
DR Proteomes; UP000014064; 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:SF25; ALCOHOL DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14390)-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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..369
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 372 AA; 39475 MW; 42ABCDCC095D6A5A CRC64;
MSTQTNLIAT LHGAKDLRLE VRPAVQVGEL DAQVDVKATG LCGSDLHYYR HGRNGDFVIR
EPLAMGHEAA GIVTSVGKGV SHIQPGDRVA IEAGIYCSSC SLCKSGRYNL CPGLRFASSA
KTYPHLDGTL QTCFTHPARL LHKMPDNVSF EQASLVEPLS VVLHGSRRSG VRAGHHVAIF
GAGAVGLLAA SVVKAQGATK VTVIDIDENR LKFALEKSFA DNTVLLPLGP RPSSPAESLE
ISKNTADSIL GQSSSDGYDV VFECTGVETC MQAAIYAAKA GGKVVYIGMG TPNATLPVSA
AAFREVDLVG VFRYSNTYDD ALEMFAANKL ASADSLVTHK FKLSDSKNAF ETLSNGKDEN
GRPAIKIMIG DY
//
