ID A0A2K0X5R0_9BIFI Unreviewed; 336 AA.
AC A0A2K0X5R0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=BFS08_02495 {ECO:0000313|EMBL:PNP89828.1};
OS Gardnerella sp. KA00735.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=1973156 {ECO:0000313|EMBL:PNP89828.1, ECO:0000313|Proteomes:UP000236541};
RN [1] {ECO:0000313|Proteomes:UP000236541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00735 {ECO:0000313|Proteomes:UP000236541};
RA Bumgarner R.E., Fredricks D.N., Srinivasan S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNP89828.1}.
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DR EMBL; NBMV01000001; PNP89828.1; -; Genomic_DNA.
DR RefSeq; WP_075523146.1; NZ_NBMV01000001.1.
DR AlphaFoldDB; A0A2K0X5R0; -.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000236541; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..332
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 336 AA; 35673 MW; 981D81564DCD4B76 CRC64;
MKAIVATKDK KAQVIEKELR PLEFGEALLD MECCGVCHTD LHVKNQDFGD KTGVVLGHEG
IGIVREVGPG VTTLKPGDRA SVAWFFKGCG HCEFCTTGRE TLCRSVLNAG YTADGGMSEQ
CIVAADYAVK VPEGLDPAPA SSITCAGVTT YKAIKESGVH PGEWLILFGL GGLGNLALQY
AKNVFGAHVI AVDVNEGQLE FAEKYGADLC VNPLKEDVAE FAMKKVGGAH GAVVTAVNKA
AFNAAVDSVR AGGTIAAVGL PPEDMELSIP RLVLDGIRLV GSLVGTRKDL EEAFQFGAEG
KVLPQCHMRK MEDINDIFDE MLAGKIRGRM VIDLSH
//
