ID Q2YP66_BRUA2 Unreviewed; 344 AA.
AC Q2YP66;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN OrderedLocusNames=BAB1_0204 {ECO:0000313|EMBL:CAJ10160.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ10160.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ10160.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ10160.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ10160.1; -; Genomic_DNA.
DR RefSeq; WP_002965452.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YP66; -.
DR SMR; Q2YP66; -.
DR STRING; 359391.BAB1_0204; -.
DR GeneID; 58776623; -.
DR KEGG; bmf:BAB1_0204; -.
DR PATRIC; fig|359391.11.peg.1627; -.
DR HOGENOM; CLU_026673_20_1_5; -.
DR PhylomeDB; Q2YP66; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08297; CAD3; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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:CAJ10160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..340
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 344 AA; 36247 MW; 09640483C3A6008B CRC64;
MAKTMKAAVV RAFGKPLTID EVPIPQPGPG QIQVAIQASG VCHTDLHAAE GDWPVKPNPP
FIPGHEGVGF VSAVGSGVKH VKEGDRVGIP WLYTACGHCR HCLGGWETLC EEQLNTGYSV
NGGFAEYVVA DPNFVGHLPK NIDFNEIAPV LCAGVTVYKG LKVTDTKPGD WVVISGIGGL
GHMAVQYARA MGLNVAAVDI DDRKLDLARR LGATVTVNAK TVADPAAYIR KETDGGAQGV
LVTAVSPKAF EQALGMVARG GTVSLNGLPP GDFPLSIFNM VLNGVTVRGS IVGTRLDLQE
SLDFAADGKV KATIQTGKLE DINAIFDDMR QGNIEGRIVM DLTQ
//
