UniProtKB - P0A388 (ADHB_GLUPO)
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 (By similarity).
Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of ethanol to acetaldehyde by transferring electrons to the ubiquinone embedded in the membrane phospholipids (PubMed:2001402).
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) (By similarity).
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 (By similarity).
The electrons transfer occurs from ubiquinol (QH2) to the additional heme c within subunit II (AdhB) (By similarity).
By similarity1 PublicationCatalytic activityi
- EC:1.1.5.5By similarity
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 45 | Heme 1; covalentPROSITE-ProRule annotation | 1 | |
Binding sitei | 48 | Heme 1; covalentPROSITE-ProRule annotation | 1 | |
Metal bindingi | 49 | Iron (heme 1 axial ligand)PROSITE-ProRule annotation | 1 | |
Binding sitei | 193 | Heme 2; covalentPROSITE-ProRule annotation | 1 | |
Binding sitei | 196 | Heme 2; covalentPROSITE-ProRule annotation | 1 | |
Metal bindingi | 197 | Iron (heme 2 axial ligand)PROSITE-ProRule annotation | 1 | |
Binding sitei | 330 | Heme 3; covalentPROSITE-ProRule annotation | 1 | |
Binding sitei | 333 | Heme 3; covalentPROSITE-ProRule annotation | 1 | |
Metal bindingi | 334 | 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:1.1.5.5By similarity)Short name: ADH1 Publication Alternative name(s): Alcohol dehydrogenase (quinone), subunit IIBy similarity Cytochrome c-553By similarity Cytochrome c553By similarity Ethanol:Q2 reductaseBy similarity G3-ADH subunit IIBy similarity Quinohemoprotein-cytochrome c complexBy similarity Ubiquinol oxidaseBy similarity |
Gene namesi | Name:adhB1 Publication |
Organismi | Gluconacetobacter polyoxogenes (Acetobacter polyoxogenes) |
Taxonomic identifieri | 439 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter |
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 – 23 | Sequence analysisAdd BLAST | 23 | |
ChainiPRO_0000006596 | 24 – 468 | Alcohol dehydrogenase (quinone), cytochrome c subunitAdd BLAST | 445 |
Interactioni
Subunit structurei
The alcohol dehydrogenase multicomponent enzyme system is composed of a dehydrogenase subunit I (AdhA) and a cytochrome c subunit II (AdhB).
1 PublicationStructurei
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 31 – 134 | Cytochrome c 1PROSITE-ProRule annotationAdd BLAST | 104 | |
Domaini | 178 – 293 | Cytochrome c 2PROSITE-ProRule annotationAdd BLAST | 116 | |
Domaini | 317 – 407 | Cytochrome c 3PROSITE-ProRule annotationAdd BLAST | 91 |
Keywords - Domaini
Repeat, SignalFamily 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 IPR014353, Membr-bd_ADH_cyt_c |
Pfami | View protein in Pfam PF00034, Cytochrom_C, 1 hit PF13442, Cytochrome_CBB3, 1 hit |
PIRSFi | PIRSF000018, Mb_ADH_cyt_c, 1 hit |
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
MINRLKVTFS AAAFSLLAGT ALAQTPDADS ALVQKGAYVA RLGDCVACHT
60 70 80 90 100
ALHGQSYAGG LEIKSPIGTI YSTNITPDPT YGIGRYTFAE FDEAVRHGIR
110 120 130 140 150
KDGSTLYPAM PYPSFSRMTK EDMQALYAYF MHGVKPVAQP DKQPDISWPL
160 170 180 190 200
SMRWPLGIWR MMFSPSPKDF TPAPGTDPEI ARGDYLVTGP GHCGACHTPR
210 220 230 240 250
GFAMQEKALD AAGGPDFLSG GAPIDNWVAP SLRNDPVVGL GRWSEDDIYT
260 270 280 290 300
FLKSGRIDHS AVFGGMGDVV AWSTQYFTDD DLHAIAKYLK SLPPVPPSQG
310 320 330 340 350
NYTYDPSTAN MLASGNTASV PGADTYVKEC AICHRNDGGG VARMFPPLAG
360 370 380 390 400
NPVVVTENPT SLVNVIAHGG VLPPSNWAPS AVAMPGYSKS LSAQQIADVV
410 420 430 440 450
NFIRTSWGNK APGTVTAADV TKLRDTGAPV SSSGWNSVSS GWSVFLPQPY
460
GSGWTFAPQT HTGQDAAQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D00635 Genomic DNA Translation: BAA00529.1 |
PIRi | S14271 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D00635 Genomic DNA Translation: BAA00529.1 |
PIRi | S14271 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
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 IPR014353, Membr-bd_ADH_cyt_c |
Pfami | View protein in Pfam PF00034, Cytochrom_C, 1 hit PF13442, Cytochrome_CBB3, 1 hit |
PIRSFi | PIRSF000018, Mb_ADH_cyt_c, 1 hit |
SUPFAMi | SSF46626, SSF46626, 3 hits |
PROSITEi | View protein in PROSITE PS51007, CYTC, 3 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ADHB_GLUPO | |
Accessioni | P0A388Primary (citable) accession number: P0A388 Secondary accession number(s): Q03318 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 15, 2005 |
Last sequence update: | March 15, 2005 | |
Last modified: | April 7, 2021 | |
This is version 64 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |