ID S6D4X8_ACEPA Unreviewed; 342 AA.
AC S6D4X8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=adh {ECO:0000313|EMBL:CCT59588.1};
GN ORFNames=APA386B_1507 {ECO:0000313|EMBL:CCT59588.1};
OS Acetobacter pasteurianus 386B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1266844 {ECO:0000313|EMBL:CCT59588.1, ECO:0000313|Proteomes:UP000015386};
RN [1] {ECO:0000313|EMBL:CCT59588.1, ECO:0000313|Proteomes:UP000015386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=386B {ECO:0000313|EMBL:CCT59588.1};
RX PubMed=23902333;
RA Illeghems K., De Vuyst L., Weckx S.;
RT "Complete genome sequence and comparative analysis of Acetobacter
RT pasteurianus 386B, a strain well-adapted to the cocoa bean fermentation
RT ecosystem.";
RL BMC Genomics 14:526-526(2013).
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; HF677570; CCT59588.1; -; Genomic_DNA.
DR RefSeq; WP_003624943.1; NC_021991.1.
DR AlphaFoldDB; S6D4X8; -.
DR GeneID; 60376319; -.
DR KEGG; apk:APA386B_1507; -.
DR PATRIC; fig|1266844.4.peg.1472; -.
DR HOGENOM; CLU_026673_20_1_5; -.
DR Proteomes; UP000015386; Chromosome.
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:CCT59588.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 342 AA; 36303 MW; 16DEC0661AB15AF6 CRC64;
MSGKMKAAVV HEFGKPLTIE ELDIPTIKPT QILVKMIACG VCHTDLHAAS GDWPKKPHLP
FIPGHEGVGT VVQVGSEVDW VKEGDVVGVP WLYSACGHCE HCLAGWETLC AKQEETGYSV
NGCFAEYVVA DPNYIAHLPK GVDPVKVAPV LCAGLTVYKG LKMTDTRAGN WVAISGVGGL
GQMAVQYAVA MGLNVVAVDI DDEKLATAKK LGATYTVNAR NTDPAAFMQE KVGGVHGGLI
TAVSTKAFSQ AMGYVRAGGT LVLNGLPPGD FPISIFDMVM NAITIRGSIV GTRLDMIEAL
SFFAEGKVTS VTTTDRIDNI NAIFDALKNG RVEGRVVLDF RN
//