ID F6GIB6_LACS5 Unreviewed; 348 AA.
AC F6GIB6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Mannitol dehydrogenase {ECO:0000313|EMBL:AEH02302.1};
DE EC=1.1.1.255 {ECO:0000313|EMBL:AEH02302.1};
GN OrderedLocusNames=Lacal_2460 {ECO:0000313|EMBL:AEH02302.1};
OS Lacinutrix sp. (strain 5H-3-7-4).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lacinutrix.
OX NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH02302.1, ECO:0000313|Proteomes:UP000008297};
RN [1] {ECO:0000313|EMBL:AEH02302.1, ECO:0000313|Proteomes:UP000008297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH02302.1,
RC ECO:0000313|Proteomes:UP000008297};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
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|RuleBase:RU361277}.
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DR EMBL; CP002825; AEH02302.1; -; Genomic_DNA.
DR RefSeq; WP_013871081.1; NC_015638.1.
DR AlphaFoldDB; F6GIB6; -.
DR STRING; 983544.Lacal_2460; -.
DR KEGG; lan:Lacal_2460; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_10; -.
DR OMA; YRFSIDM; -.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000008297; Chromosome.
DR GO; GO:0046029; F:mannitol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; DEATH RESISTOR ADH DOMAIN CONTAINING TARGET, ISOFORM C; 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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEH02302.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008297};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 348 AA; 38327 MW; 8197399FDE4585B9 CRC64;
MTEVKAYGTE SKEADLKQIK IERRDLKEND VEIEILYCGV CHSDIHAAKN DWGNTTYTLV
PGHEIVGKVK QVGDKVSKYK KGDLVGVGCM VDSCQECSAC KDDLEQFCEK GMVGTYNGEN
KHTGKQTFGG YSTSITVREE FVVSVPENLD LKAVAPLLCA GITTYSPLNH WNVKKGDKVG
IIGLGGLGHM GIKFAHAMGA ETYMITTSPD KADDAKKLGA DAVLISKNED EMKEHHGTFD
FLLNTVPVKH DINPYLQLLK RDSTMVMVGA IEPLEPMHGG NIIMGRKRVA GSLIGGIKET
QEMLDFCGDN NVTSEIELIE IKDINKAFER VQDSDVKYRF VIDMSSLK
//