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Entry version 51 (13 Feb 2019)
Sequence version 1 (15 Jan 2008)
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Protein

Quinoprotein alcohol dehydrogenase (cytochrome c)

Gene

qedA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
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

Catalyzes the oxidation of primary alcohols to the corresponding aldehydes, except for methanol, which is a very poor substrate (PubMed:18218017, PubMed:7730276). Prefers monoalcohols but also active with 1,2-propanediol and 1,3-propanediol. Not active with sugar alcohols such as D-sorbitol (PubMed:7730276).2 Publications

<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:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Enhanced by the presence of ethylamine or NH4+ ions. Active with phenazine methosulfate (PMS) but not with NADP+, potassium ferricyanide or molecular oxygen.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.163 mM for ethanol1 Publication
  2. KM=1.62 mM for butane-1-ol1 Publication
  3. KM=24.9 mM for propane-1,2-diol1 Publication
  1. Vmax=26.3 µmol/min/mg enzyme with ethanol as substrate1 Publication
  2. Vmax=21.5 µmol/min/mg enzyme with butane-1-ol as substrate1 Publication
  3. Vmax=12.3 µmol/min/mg enzyme with propane-1,2-diol as substrate1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi45Calcium 1By similarity1
Metal bindingi51Calcium 1By similarity1
<p>This subsection of the ‘Function’ 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 sitei95Pyrroloquinoline quinoneBy similarity1
Binding sitei145Pyrroloquinoline quinoneBy similarity1
Binding sitei189Pyrroloquinoline quinoneBy similarity1
Metal bindingi213Calcium 2By similarity1
Metal bindingi300Calcium 2By similarity1
<p>This subsection of the ‘Function’ 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 sitei350Proton acceptorBy similarity1
Metal bindingi350Calcium 2By similarity1
Binding sitei378Pyrroloquinoline quinoneBy similarity1
Binding sitei523Pyrroloquinoline quinoneBy similarity1
Binding sitei587Pyrroloquinoline quinone; via amide nitrogenBy 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
LigandCalcium, Metal-binding, PQQ

<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:
Quinoprotein alcohol dehydrogenase (cytochrome c)Curated (EC:1.1.2.81 Publication)
Alternative name(s):
Quinoprotein alcohol dehydrogenase (cytochrome c550)Curated
Quinoprotein alcohol dehydrogenase ADH I1 Publication
Short name:
ADH I1 Publication
Quinoprotein ethanol dehydrogenase1 Publication
Short name:
QEDH1 Publication
<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:qedA1 Publication
<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>OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
<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 identifieri303 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

<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

Periplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene show a strong reduction in the growth rate on ethanol, however growth on 1-butanol and 1,2-propanediol are not influenced.1 Publication

<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 – 34Sequence analysisAdd BLAST34
<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_000041953335 – 623Quinoprotein alcohol dehydrogenase (cytochrome c)1 PublicationAdd BLAST589

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 bondi139 ↔ 140By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
A8R3S4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by ethanol (PubMed:7730276, PubMed:19202108). Repressed by lactate, acetate and tricarboxylic acid cycle intermediates such as citrate and succinate (PubMed:19202108). Up-regulated by exaE and agmR (PubMed:18218017, PubMed:19202108).3 Publications

<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

Homodimer.1 Publication

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
A8R3S4

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

More...
SMRi
A8R3S4

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati515 – 556WD 1Sequence analysisAdd BLAST42
Repeati559 – 601WD 2Sequence analysisAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni207 – 209Pyrroloquinoline quinone bindingBy similarity3

<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

Repeat, Signal, WD repeat

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K00114

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10277 PQQ_ADH_I, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034119 ADHI
IPR018391 PQQ_beta_propeller_repeat
IPR017512 PQQ_MeOH/EtOH_DH
IPR002372 PQQ_repeat
IPR011047 Quinoprotein_ADH-like_supfam
IPR001479 Quinoprotein_DH_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01011 PQQ, 1 hit
PF13360 PQQ_2, 1 hit

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
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

<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>.<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.

A8R3S4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTIRSLPAAL SPLSMAVQAV LLVSSLALAP AANAKPVTWE DIANDHLNTQ
60 70 80 90 100
NVLQYGMGTN AQRWSPLAMV NDKNVFKLTP AWSYSFGDER QRGQESQAII
110 120 130 140 150
NDGVIYVTGS YSRVFALDAK TGRRLWTYNH RLPDNIRPCC DVVNRGAAIF
160 170 180 190 200
GDKIYFGTLD ARVIALNKDT GKVVWNKKFG DHSAGYTMTG APTLIKDQKS
210 220 230 240 250
GKVLLIHGSS GDEFGVVGQL YARDPETGEE VWMRPFVEGH MGRLNGKDST
260 270 280 290 300
PTGDVKAPSW PDDPTTETGK VESWSHGGGA PWQSASFDPE TNTIIVGAGN
310 320 330 340 350
PGPWNTWART SKDGNPHDFD SLYTSGQVGV DPTTGEVKWF YQHTPNDAWD
360 370 380 390 400
FSGNNELVLF DYKDKDGKQY KATAHADRNG FFYVVDRTNG KLKNAFPFVD
410 420 430 440 450
NITWASHIDL KTGRPVENEG QRPAKPLPGE TKGKPVEVSP PFLGGKNWNP
460 470 480 490 500
MAYSQDTGLF YVPANHWKEE YWTEEVNYKK GSAYLGIGFR IKRMYEDHVG
510 520 530 540 550
SLRAMDPTTG KVVWEHNERL PLWAGVLATK GNLVFTGTGD GYFKAFNAKT
560 570 580 590 600
GEELWKFQTG SGIVSPPITW EQDGEQYIGV TVGYGGAVPL WGGDMAELTK
610 620
PVAQGGSFWV FKIPAWDTKT AKR
Length:623
Mass (Da):68,727
Last modified:January 15, 2008 - 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:i08435869960257CE
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
AB333783 Genomic DNA Translation: BAF91141.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:BAF91141

<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
AB333783 Genomic DNA Translation: BAF91141.1

3D structure databases

ProteinModelPortaliA8R3S4
SMRiA8R3S4
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA8R3S4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAF91141

Phylogenomic databases

KOiK00114

Family and domain databases

CDDicd10277 PQQ_ADH_I, 1 hit
InterProiView protein in InterPro
IPR034119 ADHI
IPR018391 PQQ_beta_propeller_repeat
IPR017512 PQQ_MeOH/EtOH_DH
IPR002372 PQQ_repeat
IPR011047 Quinoprotein_ADH-like_supfam
IPR001479 Quinoprotein_DH_CS
PfamiView protein in Pfam
PF01011 PQQ, 1 hit
PF13360 PQQ_2, 1 hit
SMARTiView protein in SMART
SM00564 PQQ, 5 hits
SUPFAMiSSF50998 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiQEDH_PSEPU
<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: A8R3S4
<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: October 3, 2012
Last sequence update: January 15, 2008
Last modified: February 13, 2019
This is version 51 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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