ADHA_GLUPO
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 03-AUG-2022, entry version 127.
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; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC 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=a ubiquinone + ethanol = 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:0070469; C:respirasome; IEA:UniProtKB-KW.
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 Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR001479; Quinoprotein_DH_CS.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 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
