UniProtKB - Q47945 (ADHB_GLUOX)
Alcohol dehydrogenase (quinone), cytochrome c subunit
adhB
Functioni
Cytochrome c component of the alcohol dehydrogenase multicomponent enzyme system which is involved in the production of acetic acid and in the ethanol oxidase respiratory chain. Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of ethanol to acetaldehyde by transferring electrons to the ubiquinone embedded in the membrane phospholipids (PubMed:1646200, PubMed:7592433, PubMed:8617755, PubMed:9878716, PubMed:18838797).
The electrons transfer from ethanol to membranous ubiquinone occurs from pyrroloquinoline quinone (PQQ) to one heme c in subunit I (AdhA), and finally to two heme c in subunit II (AdhB) (PubMed:8617755, PubMed:9878716, PubMed:18838797).
Besides ubiquinone reduction, ADH also has a ubiquinol (QH2) oxidation reaction which mediates electron transfer from ubiquinol to the non-energy generating bypass oxidase system (PubMed:1646200, PubMed:9878716).
The electrons transfer occurs from ubiquinol (QH2) to the additional heme c within subunit II (AdhB) (PubMed:8617755, PubMed:9878716).
Also able to use quinone analogs such as 2,3-dimethoxy-5-methyl-6-n-decyl-1,4-benzoquinone (DB) and 2,3-dimethoxy-5-methyl-6-n-pentyl-1,4-benzoquinone (PB) (PubMed:9878716).
1 Publication5 PublicationsMiscellaneous
Catalytic activityi
- EC:1.1.5.53 Publications
Cofactori
Activity regulationi
Kineticsi
- KM=7.7 µM for ubiquinone-2 (for ubiquinone reduction activity in inactive ADH at pH 5)1 Publication
- KM=8.4 µM for ubiquinone-2 (for ubiquinone reduction activity in active ADH at pH 5)1 Publication
- KM=13 µM for ubiquinol-2 (for ubiquinol oxidation activity in inactive ADH at pH 5)1 Publication
- KM=32 µM for ethanol (for ubiquinone reduction activity in active ADH at pH 4.5)1 Publication
- KM=36 µM for ubiquinol-2 (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
- KM=170 µM for ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
- KM=200 µM for ferricyanide (for ubiquinol oxidation activity in inactive ADH at pH 5)1 Publication
- Vmax=175 µmol/min/mg enzyme toward ubiquinol-2 (for ubiquinol oxidation activity in inactive ADH at pH 5)1 Publication
- Vmax=167 µmol/min/mg enzyme toward ferricyanide (for ubiquinol oxidation activity in inactive ADH at pH 5)1 Publication
- Vmax=104 µmol/min/mg enzyme toward ubiquinol-2 (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
- Vmax=81 µmol/min/mg enzyme toward ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
- Vmax=70 µmol/min/mg enzyme toward ethanol (for ubiquinone reduction activity in active ADH at pH 4.5)1 Publication
- Vmax=54 µmol/min/mg enzyme toward ubiquinone-2 (for ubiquinone reduction activity in active ADH at pH 5)1 Publication
- Vmax=2 µmol/min/mg enzyme toward ubiquinone-2 (for ubiquinone reduction activity in inactive ADH at pH 5)1 Publication
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 56 | Heme 1; covalentPROSITE-ProRule annotation | 1 | |
Binding sitei | 59 | Heme 1; covalentPROSITE-ProRule annotation | 1 | |
Metal bindingi | 60 | Iron (heme 1 axial ligand)PROSITE-ProRule annotation | 1 | |
Binding sitei | 204 | Heme 2; covalentPROSITE-ProRule annotation | 1 | |
Binding sitei | 207 | Heme 2; covalentPROSITE-ProRule annotation | 1 | |
Metal bindingi | 208 | Iron (heme 2 axial ligand)PROSITE-ProRule annotation | 1 | |
Binding sitei | 340 | Heme 3; covalentPROSITE-ProRule annotation | 1 | |
Binding sitei | 343 | Heme 3; covalentPROSITE-ProRule annotation | 1 | |
Metal bindingi | 344 | Iron (heme 3 axial ligand)PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- electron transfer activity Source: InterPro
- heme binding Source: InterPro
- iron ion binding Source: InterPro
- oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Electron transport, Respiratory chain, Transport |
Ligand | Heme, Iron, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Alcohol dehydrogenase (quinone), cytochrome c subunit1 Publication (EC:1.1.5.53 Publications)Short name: ADH1 Publication Alternative name(s): Alcohol dehydrogenase (quinone), subunit II1 Publication Cytochrome c-553Curated Cytochrome c553Curated Ethanol:Q2 reductase1 Publication G3-ADH subunit II1 Publication Quinohemoprotein-cytochrome c complex1 Publication Ubiquinol oxidase1 Publication |
Gene namesi | Name:adhB1 Publication Ordered Locus Names:GOX1067 |
Organismi | Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) |
Taxonomic identifieri | 290633 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell membrane Curated; Peripheral membrane protein Curated; Periplasmic side Curated
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- respirasome Source: UniProtKB-KW
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 36 | 1 PublicationAdd BLAST | 36 | |
ChainiPRO_0000006597 | 37 – 478 | Alcohol dehydrogenase (quinone), cytochrome c subunitAdd BLAST | 442 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 37 | Pyrrolidone carboxylic acid1 Publication | 1 |
Keywords - PTMi
Pyrrolidone carboxylic acidExpressioni
Inductioni
Interactioni
Subunit structurei
The alcohol dehydrogenase multicomponent enzyme system is composed of a dehydrogenase subunit I (AdhA), a cytochrome c subunit II (AdhB) and a subunit III (AdhS).
1 Publication1 PublicationProtein-protein interaction databases
STRINGi | 290633.GOX1067 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 42 – 145 | Cytochrome c 1PROSITE-ProRule annotationAdd BLAST | 104 | |
Domaini | 189 – 304 | Cytochrome c 2PROSITE-ProRule annotationAdd BLAST | 116 | |
Domaini | 327 – 417 | Cytochrome c 3PROSITE-ProRule annotationAdd BLAST | 91 |
Keywords - Domaini
Repeat, SignalPhylogenomic databases
eggNOGi | COG2010, Bacteria |
HOGENOMi | CLU_028594_0_0_5 |
OMAi | GDYSFED |
Family and domain databases
Gene3Di | 1.10.760.10, 3 hits |
InterProi | View protein in InterPro IPR009056, Cyt_c-like_dom IPR036909, Cyt_c-like_dom_sf IPR008168, Cyt_C_IC IPR014353, Membr-bd_ADH_cyt_c |
Pfami | View protein in Pfam PF13442, Cytochrome_CBB3, 1 hit |
PIRSFi | PIRSF000018, Mb_ADH_cyt_c, 1 hit |
PRINTSi | PR00605, CYTCHROMECIC |
SUPFAMi | SSF46626, SSF46626, 3 hits |
PROSITEi | View protein in PROSITE PS51007, CYTC, 3 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MLNALTRDRL VSEMKQGWKL AAAIGLMAVS FGAAHAQDAD EALIKRGEYV
60 70 80 90 100
ARLSDCIACH TALHGQPYAG GLEIKSPIGT IYSTNITPDP EHGIGNYTLE
110 120 130 140 150
DFTKALRKGI RKDGATVYPA MPYPEFARLS DDDIRAMYAF FMHGVKPVAL
160 170 180 190 200
QNKAPDISWP LSMRWPLGMW RAMFVPSMTP GVDKSISDPE VARGEYLVNG
210 220 230 240 250
PGHCGECHTP RGFGMQVKAY GTAGGNAYLA GGAPIDNWIA PSLRSNSDTG
260 270 280 290 300
LGRWSEDDIV TFLKSGRIDH SAVFGGMADV VAYSTQHWSD DDLRATAKYL
310 320 330 340 350
KSMPAVPEGK NLGQDDGQTT ALLNKGGQGN AGAEVYLHNC AICHMNDGTG
360 370 380 390 400
VNRMFPPLAG NPVVITDDPT SLANVVAFGG ILPPTNSAPS AVAMPGFKNH
410 420 430 440 450
LSDQEMADVV NFMRKGWGNN APGTVSASDI QKLRTTGAPV STAGWNVSSK
460 470
GWMAYMPQPY GEDWTFSPQT HTGVDDAQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M58760 Genomic DNA Translation: AAA24935.1 D86375 Genomic DNA Translation: BAA19754.1 CP000009 Genomic DNA Translation: AAW60836.1 |
RefSeqi | WP_011252628.1, NZ_LT900338.1 |
Genome annotation databases
EnsemblBacteriai | AAW60836; AAW60836; GOX1067 |
KEGGi | gox:GOX1067 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M58760 Genomic DNA Translation: AAA24935.1 D86375 Genomic DNA Translation: BAA19754.1 CP000009 Genomic DNA Translation: AAW60836.1 |
RefSeqi | WP_011252628.1, NZ_LT900338.1 |
3D structure databases
SMRi | Q47945 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 290633.GOX1067 |
Genome annotation databases
EnsemblBacteriai | AAW60836; AAW60836; GOX1067 |
KEGGi | gox:GOX1067 |
Phylogenomic databases
eggNOGi | COG2010, Bacteria |
HOGENOMi | CLU_028594_0_0_5 |
OMAi | GDYSFED |
Family and domain databases
Gene3Di | 1.10.760.10, 3 hits |
InterProi | View protein in InterPro IPR009056, Cyt_c-like_dom IPR036909, Cyt_c-like_dom_sf IPR008168, Cyt_C_IC IPR014353, Membr-bd_ADH_cyt_c |
Pfami | View protein in Pfam PF13442, Cytochrome_CBB3, 1 hit |
PIRSFi | PIRSF000018, Mb_ADH_cyt_c, 1 hit |
PRINTSi | PR00605, CYTCHROMECIC |
SUPFAMi | SSF46626, SSF46626, 3 hits |
PROSITEi | View protein in PROSITE PS51007, CYTC, 3 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ADHB_GLUOX | |
Accessioni | Q47945Primary (citable) accession number: Q47945 Secondary accession number(s): O08083, Q5FS10 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | November 1, 1996 | |
Last modified: | February 23, 2022 | |
This is version 140 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |