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Entry version 122 (08 May 2019)
Sequence version 1 (01 Nov 1990)
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Protein

Alcohol dehydrogenase (quinone), dehydrogenase subunit

Gene

adhA

Organism
Acetobacter aceti
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Dehydrogenase 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. 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). 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. The electrons transfer occurs from ubiquinol (QH2) to the additional heme c within subunit II (AdhB).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei96Pyrroloquinoline quinoneBy similarity1
Binding sitei148Pyrroloquinoline quinoneBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi216CalciumBy similarity1
Binding sitei278Pyrroloquinoline quinoneBy similarity1
Metal bindingi298CalciumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei343Proton acceptorBy similarity1
Metal bindingi343CalciumBy similarity1
Binding sitei370Pyrroloquinoline quinoneBy similarity1
Binding sitei584Pyrroloquinoline quinone; via amide nitrogenBy similarity1
Binding sitei649Heme c (covalent)By similarity1
Binding sitei652Heme c (covalent)By similarity1
Metal bindingi653Iron (heme axial ligand); via tele nitrogenBy similarity1
Metal bindingi692Iron (heme axial ligand)By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Respiratory chain, Transport
LigandCalcium, Heme, Iron, Metal-binding, PQQ

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.5.5 33

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alcohol dehydrogenase (quinone), dehydrogenase subunit1 Publication (EC:1.1.5.5By similarity)
Short name:
ADHBy similarity
Alternative name(s):
Alcohol dehydrogenase (quinone), acceptor subunitBy similarity
Alcohol dehydrogenase (quinone), subunit IBy similarity
Ethanol:Q2 reductaseBy similarity
G3-ADH subunit IBy similarity
Quinohemoprotein alcohol dehydrogenaseBy similarity
Quinohemoprotein-cytochrome c complexBy similarity
Ubiquinol oxidaseBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:adhABy similarity
Synonyms:adh1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAcetobacter aceti
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri435 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacterAcetobacter subgen. Acetobacter

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 351 PublicationAdd BLAST35
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002555936 – 742Alcohol dehydrogenase (quinone), dehydrogenase subunitAdd BLAST707

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi142 ↔ 143By similarity

Keywords - PTMi

Disulfide bond

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The alcohol dehydrogenase multicomponent enzyme system is composed of a dehydrogenase subunit I (AdhA) and a cytochrome c subunit II (AdhB).

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P18278

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini636 – 715Cytochrome cPROSITE-ProRule annotationAdd BLAST80

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the bacterial PQQ dehydrogenase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.760.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009056 Cyt_c-like_dom
IPR036909 Cyt_c-like_dom_sf
IPR018391 PQQ_beta_propeller_repeat
IPR017512 PQQ_MeOH/EtOH_DH
IPR002372 PQQ_repeat
IPR011047 Quinoprotein_ADH-like_supfam
IPR001479 Quinoprotein_DH_CS
IPR006311 TAT_signal

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13442 Cytochrome_CBB3, 1 hit
PF13360 PQQ_2, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00564 PQQ, 5 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46626 SSF46626, 1 hit
SSF50998 SSF50998, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03075 PQQ_enz_alc_DH, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00363 BACTERIAL_PQQ_1, 1 hit
PS00364 BACTERIAL_PQQ_2, 1 hit
PS51007 CYTC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P18278-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTRPASAKRR SLLGILAAGT ICAAALPYAA VPARADGQGN TGEAIIHADD
60 70 80 90 100
HPENWLSYGR TYSEQRYSPL DQINRSNVGD LKLLGYYTLD TNRGQEATPL
110 120 130 140 150
VVDGIMYATT NWSKMEALDA ATGKLLWQYD PKVPGNIADK GCCDTVNRGA
160 170 180 190 200
GYWNGKVFWG TFDGRLVAAD AKTGKKVWAV NTIPADASLG KQRSYTVDGA
210 220 230 240 250
VRVAKGLVLI GNGGAEFGAR GFVSAFDAET GKLKWRFYTV PNNKNEPDHA
260 270 280 290 300
ASDNILMNKA YKTWGPKGAW VRQGGGGTVW DSLVYDPVSD LIYLAVGNGS
310 320 330 340 350
PWNYKYRSEG IGSNLFLGSI VALKPETGEY VWHFQATPMD QWDYTSVQQI
360 370 380 390 400
MTLDMPVKGE MRHVIVHAPK NGFFYVLDAK TGEFLSGKNY VYQNWANGLD
410 420 430 440 450
PLTGRPMYNP DGLYTLNGKF WYGIPGPLGA HNFMAMAYSP KTHLVYIPAH
460 470 480 490 500
QIPFGYKNQV GGFKPHADSW NVGLDMTKNG LPDTPEARTA YIKDLHGWLL
510 520 530 540 550
AWDPVKMETV WKIDHKGPWN GGILATGGDL LFQGLANGEF HAYDATNGSD
560 570 580 590 600
LYKFDAQSGI IAPPMTYSVN GKQYVAVEVG WGGIYPISMG GVGRTSGWTV
610 620 630 640 650
NHSYIAAFSL DGKAKLPALN NRGFLPVKPP AQYDQKVVDN GYFQYQTYCQ
660 670 680 690 700
TCHGDNGEGA GMLPDLRWAG AIRHQDAFYN VVGRGALTAY GMDRFDTSMT
710 720 730 740
PDEIEAIRQY LIKRANDTYQ REVDARKNDK NIPENPTLGI NP
Length:742
Mass (Da):81,521
Last modified:November 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9C6C9268DABB825A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D90004 Genomic DNA Translation: BAA14058.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JS0326

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90004 Genomic DNA Translation: BAA14058.1
PIRiJS0326

3D structure databases

SMRiP18278
ModBaseiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.5.5 33

Family and domain databases

Gene3Di1.10.760.10, 1 hit
InterProiView protein in InterPro
IPR009056 Cyt_c-like_dom
IPR036909 Cyt_c-like_dom_sf
IPR018391 PQQ_beta_propeller_repeat
IPR017512 PQQ_MeOH/EtOH_DH
IPR002372 PQQ_repeat
IPR011047 Quinoprotein_ADH-like_supfam
IPR001479 Quinoprotein_DH_CS
IPR006311 TAT_signal
PfamiView protein in Pfam
PF13442 Cytochrome_CBB3, 1 hit
PF13360 PQQ_2, 2 hits
SMARTiView protein in SMART
SM00564 PQQ, 5 hits
SUPFAMiSSF46626 SSF46626, 1 hit
SSF50998 SSF50998, 1 hit
TIGRFAMsiTIGR03075 PQQ_enz_alc_DH, 1 hit
PROSITEiView protein in PROSITE
PS00363 BACTERIAL_PQQ_1, 1 hit
PS00364 BACTERIAL_PQQ_2, 1 hit
PS51007 CYTC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiADHA_ACEAC
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P18278
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 8, 2019
This is version 122 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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