ID K7RKR1_ACIA4 Unreviewed; 336 AA.
AC K7RKR1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN OrderedLocusNames=PACID_06750 {ECO:0000313|EMBL:AFV88514.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV88514.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV88514.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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DR EMBL; CP003493; AFV88514.1; -; Genomic_DNA.
DR AlphaFoldDB; K7RKR1; -.
DR STRING; 1171373.PACID_06750; -.
DR KEGG; pbo:PACID_06750; -.
DR PATRIC; fig|1171373.8.peg.682; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_7_11; -.
DR Proteomes; UP000000214; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR CDD; cd08298; CAD2; 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; IPR014187; ADH_Zn_typ-2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02822; adh_fam_2; 1.
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 SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:AFV88514.1}.
FT DOMAIN 14..332
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 336 AA; 35709 MW; AB7438586074DF80 CRC64;
MRSWQVTDPA PIDSDPAPLQ LVERPVPEPA AGEVLVQVLA CGVCRTDLHV AEGDLPVHRA
HVTPGHEIVG RVVGFGKGTG RFAPGDRIGI PWLRRTCGVC SYCRSGRENL CSRSSYTGWD
HDGGYAEYAT VPEGFAYRIP DRYDPATAAP LLCAGIIGYR ALRRAEVPAG GRLGLYGFGG
SAHITAQIAL AQGVEVHVFT RGARARTFAL ELGAASAGGS GDPALVPLDS AIIFAPAGQI
VPRALENLAP GGTLALAGIH MSDVPPLDYQ NHLFHEKRLT SVESNTRRDG EEFLTLADRL
DIDPKVTSYP LERADEALRH LGHGDMTGAG VLSISE
//
