ID D9QMU8_BRESC Unreviewed; 334 AA.
AC D9QMU8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN OrderedLocusNames=Bresu_2797 {ECO:0000313|EMBL:ADL02104.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL02104.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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DR EMBL; CP002102; ADL02104.1; -; Genomic_DNA.
DR RefSeq; WP_013270205.1; NC_014375.1.
DR AlphaFoldDB; D9QMU8; -.
DR STRING; 633149.Bresu_2797; -.
DR KEGG; bsb:Bresu_2797; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_3_0_5; -.
DR InParanoid; D9QMU8; -.
DR OrthoDB; 9792321at2; -.
DR BioCyc; BSUB633149:G1GM8-2810-MONOMER; -.
DR Proteomes; UP000002696; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR InterPro; IPR014182; ADH_Zn_typ-1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR NCBIfam; TIGR02817; adh_fam_1; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW Reference proteome {ECO:0000313|Proteomes:UP000002696};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 13..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 334 AA; 35410 MW; 9782A9BFBFD8F311 CRC64;
MKAIGTPGPL PADDPAALVA FDAPEPVLKP HDLLVSVRAV SVNPVDVKVR GSRQPEAGQP
SILGYDAAGI VTATGSDVSL FKVGDEVFYA GQIDRPGSNA ERQAVDERIV GRKPERLGFD
EAAALPLVSI TAWELLFDRM HAGRDEDETL LVVGGAGGVG SVLIQLARAI TGLRVVATAA
RPETQAWCLE MGAHAVIDHS GPIDEALTAA GERAPKYIAA LTHTTDHFEA LARAVAVQGV
IGAIDDFKGL PVELLKPKTA GFVWEFMFAR SLHQTPDMIQ QHHILTEIAR LVEAGQMRSP
LTETLGAMTV ETLLEGHRRL QSGATIGKVA LDAI
//
