ID   B0RGE9_CLAMS            Unreviewed;       359 AA.
AC   B0RGE9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Integral membrane zinc-binding dehydrogenase {ECO:0000313|EMBL:CAQ01205.1};
GN   OrderedLocusNames=CMS1091 {ECO:0000313|EMBL:CAQ01205.1};
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ01205.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ01205.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ01205.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RGE9; -.
DR   STRING; 31964.CMS1091; -.
DR   KEGG; cms:CMS1091; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_11_2_11; -.
DR   Proteomes; UP000001318; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd08260; Zn_ADH6; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic 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   PANTHER; PTHR43401:SF5; ALCOHOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43401; L-THREONINE 3-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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          23..355
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   359 AA;  37671 MW;  E92CA4095CD78723 CRC64;
     MDEPDPPRPR GAPMRAVVYE RFGETPVVRE LPDPVPSAGG VVVRVEATGV CRSDAHGWLG
     HDDGIELPQV PGHELVGRIH QVGPEVTRFH VGDRVTVPFV CACGRCAECR AGNGQVCRDQ
     TQPGFTHWGS FAELVALHDA DVNLIPVPDE LDAGAAALLG CRFATAFRGL VHRARIRRGE
     HLLVIGCGGV GLSAVMIGVA VGAEVIAVDV DPAALARASE LGAEYTIDSS DLSELDVLDA
     IHAVSPDGVQ VSVEALGRES TLRISVLALA PTGRQVQIGL FATEPTVPVP FVISQELSMH
     GSHGMPAHDY AELMAMVASG ALKPELLIEH RITLDEAPAA LEALASGDRS AGITLVEVG
//