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Database: UniProt
Entry: B9DSD4_STRU0
LinkDB: B9DSD4_STRU0
Original site: B9DSD4_STRU0 
ID   B9DSD4_STRU0            Unreviewed;       346 AA.
AC   B9DSD4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=Zinc-binding alcohol dehydrogenase {ECO:0000313|EMBL:CAR42378.1};
GN   OrderedLocusNames=SUB1076 {ECO:0000313|EMBL:CAR42378.1};
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR42378.1, ECO:0000313|Proteomes:UP000000449};
RN   [1] {ECO:0000313|Proteomes:UP000000449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
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; AM946015; CAR42378.1; -; Genomic_DNA.
DR   RefSeq; WP_012658566.1; NC_012004.1.
DR   AlphaFoldDB; B9DSD4; -.
DR   STRING; 218495.SUB1076; -.
DR   KEGG; sub:SUB1076; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_3_9; -.
DR   OMA; YTAQCDT; -.
DR   OrthoDB; 9769198at2; -.
DR   Proteomes; UP000000449; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08287; FDH_like_ADH3; 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   PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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   Reference proteome {ECO:0000313|Proteomes:UP000000449};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   346 AA;  37125 MW;  9C39C506F68B5E01 CRC64;
     MKAATFIEPG KMVITEREKP IIEAPTDAII KIVRACVCGS DLWWYRGISQ RETGSYAGHE
     AIGIVESVGE AVTNVQAGDF VIVPFTHGCG QCAACKAGFD GNCTNHLPGK KIGYQAEYLR
     YTNADWALVK VPGQPSDYSD DKLNSLLTLS DVMATGYHAA KTAEVKEGDT VVVMGDGAVG
     LCGVIAAKLL GAKRIIAMSR HKDRQELALE FGATDIIAER GDDAVEKVMA LTNQEGVDAI
     LECVGTEQSV DTAVKIARPG AIVGRVGIPQ NPEMNTNNLF WKNIGLRGGI ASVTTFDKEV
     LLEAVLSDKI NPGKVFTKSF TLDDIQLAYE AMDKREAIKS LVLISD
//
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