ADHB_GLUOX
ID ADHB_GLUOX Reviewed; 478 AA.
AC Q47945; O08083; Q5FS10;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Alcohol dehydrogenase (quinone), cytochrome c 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), subunit II {ECO:0000303|PubMed:9055427};
DE AltName: Full=Cytochrome c-553 {ECO:0000305};
DE AltName: Full=Cytochrome c553 {ECO:0000305};
DE AltName: Full=Ethanol:Q2 reductase {ECO:0000303|PubMed:9878716};
DE AltName: Full=G3-ADH subunit II {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=adhB {ECO:0000303|PubMed:9055427}; OrderedLocusNames=GOX1067;
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].
RA Takeda Y., Shimizu T.;
RT "Cloning and sequencing of the gene encoding cytochrome c-553 (CO) from
RT Gluconabacter suboxydans.";
RL J. Ferment. Bioeng. 72:1-6(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-52, FUNCTION, AND
RP PYROGLUTAMATE FORMATION AT GLN-37.
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBUNIT, AND SUBSTRATE SPECIFICITY.
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 [8]
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: Cytochrome c 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:1646200, PubMed:9878716). The electrons transfer occurs
CC from ubiquinol (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=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:8617755};
CC Note=Binds 3 heme c groups 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=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=70 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=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:9878716}.
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DR EMBL; M58760; AAA24935.1; -; Genomic_DNA.
DR EMBL; D86375; BAA19754.1; -; Genomic_DNA.
DR EMBL; CP000009; AAW60836.1; -; Genomic_DNA.
DR RefSeq; WP_011252628.1; NZ_LT900338.1.
DR AlphaFoldDB; Q47945; -.
DR SMR; Q47945; -.
DR STRING; 290633.GOX1067; -.
DR EnsemblBacteria; AAW60836; AAW60836; GOX1067.
DR KEGG; gox:GOX1067; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_028594_0_0_5; -.
DR OMA; GDYSFED; -.
DR BioCyc; MetaCyc:MON-15243; -.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion 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; -; 3.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; SSF46626; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Respiratory chain; Signal; Transport.
FT SIGNAL 1..36
FT /evidence="ECO:0000269|PubMed:9055427"
FT CHAIN 37..478
FT /note="Alcohol dehydrogenase (quinone), cytochrome c
FT subunit"
FT /id="PRO_0000006597"
FT DOMAIN 42..145
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 189..304
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 327..417
FT /note="Cytochrome c 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 56
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 59
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 60
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 204
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 207
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 208
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 340
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 343
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 344
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT MOD_RES 37
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9055427"
SQ SEQUENCE 478 AA; 51198 MW; 3FBC1F935AD1D866 CRC64;
MLNALTRDRL VSEMKQGWKL AAAIGLMAVS FGAAHAQDAD EALIKRGEYV ARLSDCIACH
TALHGQPYAG GLEIKSPIGT IYSTNITPDP EHGIGNYTLE DFTKALRKGI RKDGATVYPA
MPYPEFARLS DDDIRAMYAF FMHGVKPVAL QNKAPDISWP LSMRWPLGMW RAMFVPSMTP
GVDKSISDPE VARGEYLVNG PGHCGECHTP RGFGMQVKAY GTAGGNAYLA GGAPIDNWIA
PSLRSNSDTG LGRWSEDDIV TFLKSGRIDH SAVFGGMADV VAYSTQHWSD DDLRATAKYL
KSMPAVPEGK NLGQDDGQTT ALLNKGGQGN AGAEVYLHNC AICHMNDGTG VNRMFPPLAG
NPVVITDDPT SLANVVAFGG ILPPTNSAPS AVAMPGFKNH LSDQEMADVV NFMRKGWGNN
APGTVSASDI QKLRTTGAPV STAGWNVSSK GWMAYMPQPY GEDWTFSPQT HTGVDDAQ
