ADH1_ZYMMO
ID ADH1_ZYMMO Reviewed; 337 AA.
AC P20368; Q5NN50; Q6Y8J4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase I;
DE Short=ADH I;
GN Name=adhA; OrderedLocusNames=ZMO1236;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=2185223; DOI=10.1128/jb.172.5.2491-2497.1990;
RA Keshav K.F., Yomano L.P., An H., Ingram L.O.;
RT "Cloning of the Zymomonas mobilis structural gene encoding alcohol
RT dehydrogenase I (adhA): sequence comparison and expression in Escherichia
RT coli.";
RL J. Bacteriol. 172:2491-2497(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA O'Mullan P.J., Stein D., Chase T. Jr., Eveleigh D.E.;
RT "Mannitol dehydrogenase from Zymomonas mobilis.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=8320209; DOI=10.1128/jb.175.13.3926-3933.1993;
RA Yomano L.P., Scopes R.K., Ingram L.O.;
RT "Cloning, sequencing, and expression of the Zymomonas mobilis
RT phosphoglycerate mutase gene (pgm) in Escherichia coli.";
RL J. Bacteriol. 175:3926-3933(1993).
RN [5]
RP PROTEIN SEQUENCE OF 1-31.
RX PubMed=2935393; DOI=10.1111/j.1432-1033.1986.tb09366.x;
RA Neale A.D., Scopes R.K., Kelly J.M., Wettenhall R.E.H.;
RT "The two alcohol dehydrogenases of Zymomonas mobilis. Purification by
RT differential dye ligand chromatography, molecular characterisation and
RT physiological roles.";
RL Eur. J. Biochem. 154:119-124(1986).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by ethanol.
CC -!- PATHWAY: Alcohol metabolism; ethanol biosynthesis via fermentation
CC pathway.
CC -!- SUBUNIT: Multimeric (with different ratios of monomers).
CC -!- MISCELLANEOUS: In Z.mobilis there are two isozymes of alcohol
CC dehydrogenase.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M32100; AAA27682.1; -; Genomic_DNA.
DR EMBL; AY170008; AAO38758.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89860.1; -; Genomic_DNA.
DR EMBL; L09650; AAA71935.2; -; Genomic_DNA.
DR PIR; A35260; A35260.
DR RefSeq; WP_011241052.1; NZ_CP035711.1.
DR AlphaFoldDB; P20368; -.
DR SMR; P20368; -.
DR STRING; 264203.ZMO1236; -.
DR EnsemblBacteria; AAV89860; AAV89860; ZMO1236.
DR GeneID; 58027005; -.
DR KEGG; zmo:ZMO1236; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_1_5; -.
DR OMA; GLKMTDT; -.
DR OrthoDB; 969875at2; -.
DR UniPathway; UPA00778; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043458; P:ethanol biosynthetic process involved in glucose fermentation to ethanol; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..337
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160750"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="T -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="E -> F (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="L -> H (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="E -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="V -> A (in Ref. 1; AAA27682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 36122 MW; 98D75C912CE1EBE5 CRC64;
MKAAVITKDH TIEVKDTKLR PLKYGEALLE MEYCGVCHTD LHVKNGDFGD ETGRITGHEG
IGIVKQVGEG VTSLKVGDRA SVAWFFKGCG HCEYCVSGNE TLCRNVENAG YTVDGAMAEE
CIVVADYSVK VPDGLDPAVA SSITCAGVTT YKAVKVSQIQ PGQWLAIYGL GGLGNLALQY
AKNVFNAKVI AIDVNDEQLA FAKELGADMV INPKNEDAAK IIQEKVGGAH ATVVTAVAKS
AFNSAVEAIR AGGRVVAVGL PPEKMDLSIP RLVLDGIEVL GSLVGTREDL KEAFQFAAEG
KVKPKVTKRK VEEINQIFDE MEHGKFTGRM VVDFTHH
