ID   ADHA_GLUPO              Reviewed;         738 AA.
AC   P28036;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   02-SEP-2026, entry version 138.
DE   RecName: Full=Alcohol dehydrogenase (quinone), dehydrogenase subunit {ECO:0000303|PubMed:2001402};
DE            Short=ADH {ECO:0000303|PubMed:2001402};
DE            EC=1.1.5.5 {ECO:0000250|UniProtKB:O05542};
DE   AltName: Full=Alcohol dehydrogenase (quinone), acceptor subunit {ECO:0000250|UniProtKB:O05542};
DE   AltName: Full=Alcohol dehydrogenase (quinone), subunit I {ECO:0000250|UniProtKB:O05542};
DE   AltName: Full=Ethanol:Q2 reductase {ECO:0000250|UniProtKB:O05542};
DE   AltName: Full=G3-ADH subunit I {ECO:0000250|UniProtKB:O05542};
DE   AltName: Full=Quinohemoprotein alcohol dehydrogenase {ECO:0000250|UniProtKB:O05542};
DE   AltName: Full=Quinohemoprotein-cytochrome c complex {ECO:0000250|UniProtKB:O05542};
DE   AltName: Full=Ubiquinol oxidase {ECO:0000250|UniProtKB:O05542};
DE   Flags: Precursor;
GN   Name=adhA;
OS   Gluconacetobacter polyoxogenes (Acetobacter polyoxogenes).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Acetobacterales; Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 267-279 AND 389-401,
RP   FUNCTION, AND SUBUNIT.
RC   STRAIN=NBI1028;
RX   PubMed=2001402; DOI=10.1016/0167-4781(91)90066-u;
RA   Tamaki T., Fukaya M., Takemura H., Tayama K., Okumura H., Kawamura Y.,
RA   Nishiyama M., Horinouchi S., Beppu T.;
RT   "Cloning and sequencing of the gene cluster encoding two subunits of
RT   membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes.";
RL   Biochim. Biophys. Acta 1088:292-300(1991).
CC   -!- FUNCTION: Dehydrogenase component of the alcohol dehydrogenase
CC       multicomponent enzyme system which is involved in the production of
CC       acetic acid and in the ethanol oxidase respiratory chain (By
CC       similarity). Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the
CC       oxidation of ethanol to acetaldehyde by transferring electrons to the
CC       ubiquinone embedded in the membrane phospholipids (PubMed:2001402). The
CC       electrons transfer from ethanol to membranous ubiquinone occurs from
CC       pyrroloquinoline quinone (PQQ) to one heme c in subunit I (AdhA), and
CC       finally to two heme c in subunit II (AdhB) (By similarity). Besides
CC       ubiquinone reduction, ADH also has a ubiquinol (QH2) oxidation reaction
CC       which mediates electron transfer from ubiquinol to the non-energy
CC       generating bypass oxidase system (By similarity). The electrons
CC       transfer occurs from ubiquinol (QH2) to the additional heme c within
CC       subunit II (AdhB) (By similarity). {ECO:0000250|UniProtKB:O05542,
CC       ECO:0000269|PubMed:2001402}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ethanol + a ubiquinone = a ubiquinol + acetaldehyde;
CC         Xref=Rhea:RHEA:26442, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:16236, ChEBI:CHEBI:16389,
CC         ChEBI:CHEBI:17976; EC=1.1.5.5;
CC         Evidence={ECO:0000250|UniProtKB:O05542};
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000250|UniProtKB:O05542};
CC       Note=Binds 1 PQQ group per subunit. {ECO:0000250|UniProtKB:O05542};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:O05542};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GR64};
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000250|UniProtKB:O05542};
CC       Note=Binds 1 heme c group covalently per subunit.
CC       {ECO:0000250|UniProtKB:O05542};
CC   -!- SUBUNIT: The alcohol dehydrogenase multicomponent enzyme system is
CC       composed of a dehydrogenase subunit I (AdhA) and a cytochrome c subunit
CC       II (AdhB). {ECO:0000305|PubMed:2001402}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; D00635; BAA00528.1; -; Genomic_DNA.
DR   PIR; S14270; S14270.
DR   AlphaFoldDB; P28036; -.
DR   SMR; P28036; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   CDD; cd10279; PQQ_ADH_II; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR018391; PQQ_b-propeller_rpt.
DR   InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR   InterPro; IPR002372; PQQ_rpt_dom.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_sf.
DR   InterPro; IPR001479; Quinoprotein_DH_CS.
DR   NCBIfam; TIGR03075; PQQ_enz_alc_DH; 1.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   Pfam; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 6.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Oxidoreductase;
KW   PQQ; Respiratory chain; Signal; Transport.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..738
FT                   /note="Alcohol dehydrogenase (quinone), dehydrogenase
FT                   subunit"
FT                   /id="PRO_0000025561"
FT   DOMAIN          634..738
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         97
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         149
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         278
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         298
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         343
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         370
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         584
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         650
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         653
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         654
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   BINDING         693
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT   DISULFID        143..144
FT                   /evidence="ECO:0000250|UniProtKB:Q8GR64"
SQ   SEQUENCE   738 AA;  80841 MW;  1E2B6ED7BCD92AF6 CRC64;
     MISAVFGKRR SLSRTLTAGT ICAALISGYA TMASADDGQG ATGEAIIHAD DHPGNWMTYG
     RTYSDQRYSP LDQINRSNVG NLKLAWYLDL DTNRGQEGTP LVIDGVMYAT TNWSMMKAVD
     AATGKLLWSY DPRVPGNIAD KGCCDTVNRG AAYWNGKVYF GTFDGRLIAL DAKTGKLVWS
     VNTIPPEAEL GKQRSYTVDG APRIAKGRVI IGNGGSEFGA RGFVSAFDAE TGKVDWRFFT
     VPNPKNEPDA ASDSVLMNKA YQTWSPTGAW TRQGGGGTVW DSIVYDPVAD LVYLGVGNGS
     PWNYKYRSEG KGDNLFLGSI VALKPETGEY VWHFQETPMD QWDFTSDQQI MTLDLPINGE
     TRHVIVHARK NGFFYIIDAK TGEFISGKNY VYVNWASGLD PKTGRPIYNP DALYTLTGKE
     WYGIPGDLGG HNFAAMAFSP KTGLVYIPAQ QVPFLYTNQV GGFTPHPDSW NLGLDMNKVG
     IPDSPEAKQA FVKDLKGWIV AWDPQKQAEA WRVDHKGPWN GGILATGGDL LFQGLANGEF
     HAYDATNGSD LFHFAADSGI IAPPVTYLAN GKQYVAVEVG WGGIYPFFLG GLARTSGWTV
     NHSRIIAFSL DGKSGPLPKQ NDQGFLPVKP PAQFDSKRTD NGYFQFQTYC AACHGDNAEG
     AGVLPDLRWS GSIRHEDAFY NVVGRGALTA YGMDRLHGNM NPTEIEDIRQ FLIKRANETY
     QREVDARKNA DGIPEQLP
//