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
//