ADHA_GLUOX
ID ADHA_GLUOX Reviewed; 757 AA.
AC O05542; Q5FS09;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Alcohol dehydrogenase (quinone), dehydrogenase subunit {ECO:0000303|PubMed:9055427};
DE Short=ADH {ECO:0000303|PubMed:9055427};
DE EC=1.1.5.5 {ECO:0000269|PubMed:7592433, ECO:0000269|PubMed:8617755, ECO:0000269|PubMed:9878716};
DE AltName: Full=Alcohol dehydrogenase (quinone), acceptor subunit {ECO:0000305};
DE AltName: Full=Alcohol dehydrogenase (quinone), subunit I {ECO:0000303|PubMed:9055427};
DE AltName: Full=Ethanol:Q2 reductase {ECO:0000303|PubMed:9878716};
DE AltName: Full=G3-ADH subunit I {ECO:0000303|PubMed:9055427};
DE AltName: Full=Quinohemoprotein alcohol dehydrogenase {ECO:0000303|PubMed:9055427};
DE AltName: Full=Quinohemoprotein-cytochrome c complex {ECO:0000303|PubMed:18838797};
DE AltName: Full=Ubiquinol oxidase {ECO:0000303|PubMed:9878716};
DE Flags: Precursor;
GN Name=adhA {ECO:0000303|PubMed:9055427}; OrderedLocusNames=GOX1068;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-50, FUNCTION,
RP PYROGLUTAMATE FORMATION AT GLN-35, AND COFACTOR.
RC STRAIN=ATCC 621 / DSM 50049 / NBRC 3172 / NCIMB 7069 / NRRL B-72;
RX PubMed=9055427; DOI=10.1128/aem.63.3.1131-1138.1997;
RA Kondo K., Horinouchi S.;
RT "Characterization of the genes encoding the three-component membrane-bound
RT alcohol dehydrogenase from Gluconobacter suboxydans and their expression in
RT Acetobacter pasteurianus.";
RL Appl. Environ. Microbiol. 63:1131-1138(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
RN [3]
RP FUNCTION.
RX PubMed=1646200; DOI=10.1128/jb.173.11.3440-3445.1991;
RA Matsushita K., Nagatani Y., Shinagawa E., Adachi O., Ameyama M.;
RT "Reconstitution of the ethanol oxidase respiratory chain in membranes of
RT quinoprotein alcohol dehydrogenase-deficient Gluconobacter suboxydans
RT subsp. alpha strains.";
RL J. Bacteriol. 173:3440-3445(1991).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=7592433; DOI=10.1128/jb.177.22.6552-6559.1995;
RA Matsushita K., Yakushi T., Takaki Y., Toyama H., Adachi O.;
RT "Generation mechanism and purification of an inactive form convertible in
RT vivo to the active form of quinoprotein alcohol dehydrogenase in
RT Gluconobacter suboxydans.";
RL J. Bacteriol. 177:6552-6559(1995).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RX PubMed=8617755; DOI=10.1074/jbc.271.9.4850;
RA Matsushita K., Yakushi T., Toyama H., Shinagawa E., Adachi O.;
RT "Function of multiple heme c moieties in intramolecular electron transport
RT and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-
RT cytochrome c complex of Gluconobacter suboxydans.";
RL J. Biol. Chem. 271:4850-4857(1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=9878716; DOI=10.1016/s0005-2728(98)00158-3;
RA Matsushita K., Yakushi T., Toyama H., Adachi O., Miyoshi H., Tagami E.,
RA Sakamoto K.;
RT "The quinohemoprotein alcohol dehydrogenase of Gluconobacter suboxydans has
RT ubiquinol oxidation activity at a site different from the ubiquinone
RT reduction site.";
RL Biochim. Biophys. Acta 1409:154-164(1999).
RN [7]
RP FUNCTION.
RX PubMed=18838797; DOI=10.1271/bbb.80363;
RA Matsushita K., Kobayashi Y., Mizuguchi M., Toyama H., Adachi O.,
RA Sakamoto K., Miyoshi H.;
RT "A tightly bound quinone functions in the ubiquinone reaction sites of
RT quinoprotein alcohol dehydrogenase of an acetic acid bacterium,
RT Gluconobacter suboxydans.";
RL Biosci. Biotechnol. Biochem. 72:2723-2731(2008).
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 (PubMed:1646200, PubMed:7592433,
CC PubMed:8617755, PubMed:9878716, PubMed:18838797). The electrons
CC 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) (PubMed:8617755,
CC PubMed:9878716, PubMed:18838797). Besides ubiquinone reduction, ADH
CC also has a ubiquinol (QH2) oxidation reaction which mediates electron
CC transfer from ubiquinol to the non-energy generating bypass oxidase
CC system (PubMed:9878716). The electrons transfer occurs from ubiquinol
CC (QH2) to the additional heme c within subunit II (AdhB)
CC (PubMed:8617755, PubMed:9878716). Also able to use quinone analogs such
CC as 2,3-dimethoxy-5-methyl-6-n-decyl-1,4-benzoquinone (DB) and 2,3-
CC dimethoxy-5-methyl-6-n-pentyl-1,4-benzoquinone (PB) (PubMed:9878716).
CC {ECO:0000269|PubMed:1646200, ECO:0000269|PubMed:18838797,
CC ECO:0000269|PubMed:7592433, ECO:0000269|PubMed:8617755,
CC ECO:0000269|PubMed:9878716, ECO:0000305|PubMed:9055427}.
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; Evidence={ECO:0000269|PubMed:7592433,
CC ECO:0000269|PubMed:8617755, ECO:0000269|PubMed:9878716};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:8617755, ECO:0000305|PubMed:9055427};
CC Note=Binds 1 PQQ group per subunit. {ECO:0000269|PubMed:8617755};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:8617755};
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:0000269|PubMed:8617755, ECO:0000305|PubMed:9055427};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:8617755};
CC -!- ACTIVITY REGULATION: 2,6-dichloro-4-dicyanovinylphenol (PC16) and
CC antimycin A inhibit ubiquinol oxidation activity more selectively than
CC the ubiquinone reductase activity. {ECO:0000269|PubMed:9878716}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.7 uM for ubiquinone-2 (for ubiquinone reduction activity in
CC inactive ADH at pH 5) {ECO:0000269|PubMed:9878716};
CC KM=8.4 uM for ubiquinone-2 (for ubiquinone reduction activity in
CC active ADH at pH 5) {ECO:0000269|PubMed:9878716};
CC KM=13 uM for ubiquinol-2 (for ubiquinol oxidation activity in
CC inactive ADH at pH 5) {ECO:0000269|PubMed:9878716};
CC KM=32 uM for ethanol (for ubiquinone reduction activity in active ADH
CC at pH 4.5) {ECO:0000269|PubMed:8617755};
CC KM=36 uM for ubiquinol-2 (for ubiquinol oxidation activity in active
CC ADH at pH 5) {ECO:0000269|PubMed:9878716};
CC KM=40 uM for ethanol (for ubiquinone reduction activity in inactive
CC ADH at pH 4.5) {ECO:0000269|PubMed:8617755};
CC KM=170 uM for ferricyanide (for ubiquinol oxidation activity in
CC active ADH at pH 5) {ECO:0000269|PubMed:9878716};
CC KM=200 uM for ferricyanide (for ubiquinol oxidation activity in
CC inactive ADH at pH 5) {ECO:0000269|PubMed:9878716};
CC Vmax=175 umol/min/mg enzyme toward ubiquinol-2 (for ubiquinol
CC oxidation activity in inactive ADH at pH 5)
CC {ECO:0000269|PubMed:9878716};
CC Vmax=167 umol/min/mg enzyme toward ferricyanide (for ubiquinol
CC oxidation activity in inactive ADH at pH 5)
CC {ECO:0000269|PubMed:9878716};
CC Vmax=104 umol/min/mg enzyme toward ubiquinol-2 (for ubiquinol
CC oxidation activity in active ADH at pH 5)
CC {ECO:0000269|PubMed:9878716};
CC Vmax=81 umol/min/mg enzyme toward ferricyanide (for ubiquinol
CC oxidation activity in active ADH at pH 5)
CC {ECO:0000269|PubMed:9878716};
CC Vmax=71 umol/min/mg enzyme toward ethanol (for ubiquinone reduction
CC activity in active ADH at pH 4.5) {ECO:0000269|PubMed:8617755};
CC Vmax=54 umol/min/mg enzyme toward ubiquinone-2 (for ubiquinone
CC reduction activity in active ADH at pH 5)
CC {ECO:0000269|PubMed:9878716};
CC Vmax=7.1 umol/min/mg enzyme toward ethanol (for ubiquinone reduction
CC activity in inactive ADH at pH 4.5) {ECO:0000269|PubMed:8617755};
CC Vmax=2 umol/min/mg enzyme toward ubiquinone-2 (for ubiquinone
CC reduction activity in inactive ADH at pH 5)
CC {ECO:0000269|PubMed:9878716};
CC pH dependence:
CC Optimum pH is 5 for ubiquinol oxidation activity.
CC {ECO:0000269|PubMed:9878716};
CC -!- SUBUNIT: The alcohol dehydrogenase multicomponent enzyme system is
CC composed of a dehydrogenase subunit I (AdhA), a cytochrome c subunit II
CC (AdhB) and a subunit III (AdhS). {ECO:0000269|PubMed:8617755,
CC ECO:0000305|PubMed:9878716}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000305|PubMed:7592433}.
CC -!- MISCELLANEOUS: Inactive ADH is produced under conditions of low pH and
CC high aeration, where the bypass oxidase activity is highly elevated. In
CC spite of having 10 times less enzyme activity than active ADH, inactive
CC ADH is not distinguished from active ADH with respect to their subunit
CC compositions, molecular sizes and prosthetic groups. It seems that in
CC inactive ADH, an improper interaction between subunit II and subunit
CC I/III complex impairs efficient intersubunit electron transport in the
CC ADH complex. {ECO:0000269|PubMed:7592433, ECO:0000269|PubMed:8617755,
CC ECO:0000269|PubMed:9878716}.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; D86375; BAA19753.1; -; Genomic_DNA.
DR EMBL; CP000009; AAW60837.1; -; Genomic_DNA.
DR RefSeq; WP_011252629.1; NZ_LT900338.1.
DR AlphaFoldDB; O05542; -.
DR SMR; O05542; -.
DR STRING; 290633.GOX1068; -.
DR EnsemblBacteria; AAW60837; AAW60837; GOX1068.
DR KEGG; gox:GOX1068; -.
DR eggNOG; COG2010; Bacteria.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_0_1_5; -.
DR OMA; DIANDHL; -.
DR BioCyc; MetaCyc:MON-15242; -.
DR Proteomes; UP000006375; Chromosome.
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; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
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; Pyrrolidone carboxylic acid; Reference proteome; Respiratory chain;
KW Signal; Transport.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:9055427"
FT CHAIN 35..757
FT /note="Alcohol dehydrogenase (quinone), dehydrogenase
FT subunit"
FT /id="PRO_0000025562"
FT DOMAIN 640..719
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 726..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 95
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 147
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 277
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 369
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 588
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
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 656
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 657
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 696
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 MOD_RES 35
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9055427"
FT DISULFID 141..142
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT CONFLICT 230
FT /note="G -> S (in Ref. 1; BAA19753)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="A -> R (in Ref. 1; BAA19753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 82853 MW; 56B3940B711BB0CC CRC64;
MTSGLLTPIK VTKKRLLSCA AALAFSAAVP VAFAQEDTGT AITSSDNGGH PGDWLSYGRS
YSEQRYSPLD QINTENVGKL KLAWHYDLDT NRGQEGTPLI VNGVMYATTN WSKMKALDAA
TGKLLWSYDP KVPGNIADRG CCDTVSRGAA YWNGKVYFGT FDGRLIALDA KTGKLVWSVY
TIPKEAQLGH QRSYTVDGAP RIAKGKVLIG NGGAEFGARG FVSAFDAETG KLDWRFFTVP
NPENKPDGAA SDDILMSKAY PTWGKNGAWK QQGGGGTVWD SLVYDPVTDL VYLGVGNGSP
WNYKFRSEGK GDNLFLGSIV AINPDTGKYV WHFQETPMDE WDYTSVQQIM TLDMPVNGEM
RHVIVHAPKN GFFYIIDAKT GKFITGKPYT YENWANGLDP VTGRPNYVPD ALWTLTGKPW
LGIPGELGGH NFAAMAYSPK TKLVYIPAQQ IPLLYDGQKG GFKAYHDAWN LGLDMNKIGL
FDDNDPEHVA AKKDFLKVLK GWTVAWDPEK MAPAFTINHK GPWNGGLLAT AGNVIFQGLA
NGEFHAYDAT NGNDLYSFPA QSAIIAPPVT YTANGKQYVA VEVGWGGIYP FLYGGVARTS
GWTVNHSRVI AFSLDGKDSL PPKNELGFTP VKPVPTYDEA RQKDGYFMYQ TFCSACHGDN
AISGGVLPDL RWSGAPRGRE SFYKLVGRGA LTAYGMDRFD TSMTPEQIED IRNFIVKRAN
ESYDDEVKAR ENSTGVPNDQ FLNVPQSTAD VPTADHP
