ADHA_ACEAC
ID ADHA_ACEAC Reviewed; 742 AA.
AC P18278;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Alcohol dehydrogenase (quinone), dehydrogenase subunit {ECO:0000303|PubMed:2722742};
DE Short=ADH {ECO:0000250|UniProtKB:O05542};
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 {ECO:0000250|UniProtKB:O05542}; Synonyms=adh1;
OS Acetobacter aceti.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX NCBI_TaxID=435;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 36-50.
RC STRAIN=K6033;
RX PubMed=2722742; DOI=10.1128/jb.171.6.3115-3122.1989;
RA Inoue T., Sunagawa M., Mori A., Imai C., Fukuda M., Takagi M., Yano K.;
RT "Cloning and sequencing of the gene encoding the 72-kilodalton
RT dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti.";
RL J. Bacteriol. 171:3115-3122(1989).
RN [2]
RP 3D-STRUCTURE MODELING.
RX PubMed=7772016; DOI=10.1042/bj3080375;
RA Cozier G.E., Giles I.G., Anthony C.;
RT "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter
RT aceti modelled on that of methanol dehydrogenase from Methylobacterium
RT extorquens.";
RL Biochem. J. 308:375-379(1995).
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.
CC Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of
CC ethanol to acetaldehyde by transferring electrons to the ubiquinone
CC embedded in the membrane phospholipids. The electrons transfer from
CC ethanol to membranous ubiquinone occurs from pyrroloquinoline quinone
CC (PQQ) to one heme c in subunit I (AdhA), and finally to two heme c in
CC subunit II (AdhB). Besides ubiquinone reduction, ADH also has a
CC ubiquinol (QH2) oxidation reaction which mediates electron transfer
CC from ubiquinol to the non-energy generating bypass oxidase system. The
CC electrons transfer occurs from ubiquinol (QH2) to the additional heme c
CC within subunit II (AdhB). {ECO:0000250|UniProtKB:O05542}.
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:0000250|UniProtKB:P28036}.
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; D90004; BAA14058.1; -; Genomic_DNA.
DR PIR; JS0326; JS0326.
DR AlphaFoldDB; P18278; -.
DR SMR; P18278; -.
DR BRENDA; 1.1.5.5; 33.
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 InterPro; IPR006311; TAT_signal.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 5.
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:0000269|PubMed:2722742"
FT CHAIN 36..742
FT /note="Alcohol dehydrogenase (quinone), dehydrogenase
FT subunit"
FT /id="PRO_0000025559"
FT DOMAIN 636..715
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 722..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 96
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 148
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 216
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 649
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 652
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 /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 692
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 142..143
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
SQ SEQUENCE 742 AA; 81521 MW; 9C6C9268DABB825A CRC64;
MTRPASAKRR SLLGILAAGT ICAAALPYAA VPARADGQGN TGEAIIHADD HPENWLSYGR
TYSEQRYSPL DQINRSNVGD LKLLGYYTLD TNRGQEATPL VVDGIMYATT NWSKMEALDA
ATGKLLWQYD PKVPGNIADK GCCDTVNRGA GYWNGKVFWG TFDGRLVAAD AKTGKKVWAV
NTIPADASLG KQRSYTVDGA VRVAKGLVLI GNGGAEFGAR GFVSAFDAET GKLKWRFYTV
PNNKNEPDHA ASDNILMNKA YKTWGPKGAW VRQGGGGTVW DSLVYDPVSD LIYLAVGNGS
PWNYKYRSEG IGSNLFLGSI VALKPETGEY VWHFQATPMD QWDYTSVQQI MTLDMPVKGE
MRHVIVHAPK NGFFYVLDAK TGEFLSGKNY VYQNWANGLD PLTGRPMYNP DGLYTLNGKF
WYGIPGPLGA HNFMAMAYSP KTHLVYIPAH QIPFGYKNQV GGFKPHADSW NVGLDMTKNG
LPDTPEARTA YIKDLHGWLL AWDPVKMETV WKIDHKGPWN GGILATGGDL LFQGLANGEF
HAYDATNGSD LYKFDAQSGI IAPPMTYSVN GKQYVAVEVG WGGIYPISMG GVGRTSGWTV
NHSYIAAFSL DGKAKLPALN NRGFLPVKPP AQYDQKVVDN GYFQYQTYCQ TCHGDNGEGA
GMLPDLRWAG AIRHQDAFYN VVGRGALTAY GMDRFDTSMT PDEIEAIRQY LIKRANDTYQ
REVDARKNDK NIPENPTLGI NP
