ID A0A080N6B1_9BIFI Unreviewed; 371 AA.
AC A0A080N6B1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KFF31449.1};
DE EC=1.1.1.306 {ECO:0000313|EMBL:KFF31449.1};
GN ORFNames=BBOMB_0811 {ECO:0000313|EMBL:KFF31449.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31449.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF31449.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31449.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {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:KFF31449.1}.
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DR EMBL; ATLK01000001; KFF31449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080N6B1; -.
DR STRING; 1341695.BBOMB_0811; -.
DR eggNOG; COG1062; Bacteria.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000028730; Unassembled WGS sequence.
DR GO; GO:0050607; F:mycothiol-dependent formaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08279; Zn_ADH_class_III; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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:KFF31449.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028730};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 18..368
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 371 AA; 39732 MW; 1D420C93D0BFAD5A CRC64;
MPQKIKASIA YGIGKGFAQP EDIIIDDPKG AEVLVDVKAS GLCHSDLHLV EDDDKFFPFP
AVIGHEVAGV VEAVGPEVQG IKVGDHVIAS LEQVCGHCAN CLNGHPQSCT QQQECVREPG
DTPRLSFLDG RPITQAFGTG GFAEKALIHE NQLAVVNNDV KWEEAACIGC ATITGAGAAI
NSAHVRPGQT VAVVGTGGIG LNIISGARIC GAKKIIAIDI LDNKLEFAKK FGATDVVNSK
DRDPVEAVRE LTDGGVDAAF EAIGVRSAMK QCWDMLAVDG MAYCIGLAKP DATIELEINP
ADFLVHQRGF KGVWMGSTNI KYDIPMYADM AVDGRLNMHD IVSQRINLRQ IDEAYEQLKR
GEVIRSVITE F
//
