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Entry version 148 (23 Feb 2022)
Sequence version 1 (01 May 1999)
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Protein

Quinoprotein ethanol dehydrogenase

Gene

exaA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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 ethanol and other primary alcohols to the corresponding aldehydes, except methanol, which is a very poor substrate. Uses a specific inducible cytochrome c550, encoded by the adjacent gene in the locus, as electron acceptor. Is a key enzyme of the carbon and energy metabolism during growth of P.aeruginosa on ethanol as the sole carbon and energy source. Is also able to use secondary alcohols as well as aminoalcohols like ethanolamine and 1-amino-2-propanol, and aldehydes as substrates.

3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Inhibited by cyclopropanone ethylhemiketal. Activated by ammonia (500mM), methylamine (5mM), ethylamine (5mM), octylamine (5mM), ethanolamine (5mM) and 1-amino-2-propanol (5mM), in assays using artificial electron acceptors (PubMed:3144289). Ammonia is not needed for, nor does it stimulate, the ethanol-oxidizing activity when using the natural electron acceptor cytochrome c550 (PubMed:8380982).2 Publications

<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

kcat is 11 sec(-1) for the oxidation of ethanol using artificial electron acceptor (at pH 9). kcat is 15 sec(-1) for the oxidation of 1-propanol using artificial electron acceptor (at pH 9). kcat is 11 sec(-1) for the oxidation of 2-propanol using artificial electron acceptor (at pH 9). kcat is 40 sec(-1) for the oxidation of 1,3-propanediol using artificial electron acceptor (at pH 9). kcat is 42 sec(-1) for the oxidation of 1-butanol using artificial electron acceptor (at pH 9). kcat is 2.4 sec(-1) for the oxidation of 2-propanol using natural electron acceptor cytochrome c550 (at pH 7).1 Publication
  1. KM=14 µM for ethanol1 Publication
  2. KM=21 µM for 1-propanol1 Publication
  3. KM=680 µM for 2-propanol1 Publication
  4. KM=980 µM for (2S)-2-butanol1 Publication
  5. KM=4.5 mM for ethanal1 Publication
  6. KM=94 mM for methanol1 Publication
  7. KM=12 µM for ethanol (at pH 9)1 Publication
  8. KM=62 µM for 1-propanol (at pH 9)1 Publication
  9. KM=1.4 mM for 2-propanol (at pH 9)1 Publication
  10. KM=21 mM for 1,3-propanediol (at pH 9)1 Publication
  11. KM=0.43 mM for 1-butanol (at pH 9)1 Publication

pH dependencei

Optimum pH is 9 in assays using artificial electron acceptors (PubMed:3144289). However, in a system with homogenous QEDH, cytochrome c550 and a membrane fraction of P.aeruginosa, electron transport from ethanol to O2 is observed at the more physiological conditions of pH 7, and the system is inactive at pH 9 (PubMed:8380982).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ethanol degradation

This protein is involved in step 1 of the subpathway that synthesizes acetate from ethanol.1 Publication This subpathway is part of the pathway ethanol degradation, which is itself part of Alcohol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetate from ethanol, the pathway ethanol degradation and in Alcohol metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi45Calcium 1Combined sources1 Publication1
Metal bindingi48Calcium 1Combined sources1 Publication1
Metal bindingi51Calcium 1Combined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei95Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei145Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei189Pyrroloquinoline quinoneCombined sources1 Publication1
Metal bindingi213Calcium 2; catalyticCombined sources1 Publication1
Metal bindingi300Calcium 2; catalyticCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei350Proton acceptor1 Publication1
Metal bindingi350Calcium 2; catalyticCombined sources1 Publication1
Binding sitei378Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei523Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei587Pyrroloquinoline quinone; via amide nitrogenCombined sources1 Publication1

<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

GO - Biological processi

  • ethanol catabolic process Source: UniProtKB-UniPathway
  • ethanol oxidation Source: PseudoCAP

<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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.2.8, 5087
1.1.2.B3, 5087

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00780;UER00767

<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%5Fand%5Ftaxonomy%5Fsection">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 ethanol dehydrogenase3 Publications (EC:1.1.2.81 Publication2 Publications)
Short name:
QEDH2 Publications
Alternative name(s):
Quinoprotein alcohol dehydrogenase (cytochrome c)Curated
Quinoprotein alcohol dehydrogenase (cytochrome c550)Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:exaA1 Publication
Ordered Locus Names:PA1982
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri208964 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002438 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

Organism-specific databases

Pseudomonas genome database

More...
PseudoCAPi
PA1982

<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

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi139 – 140CC → AA: 15-fold decrease in catalytic activity with the natural electron acceptor cytochrome c550. Does not affect, or even increases, catalytic activity with artificial electron acceptors. Shows high decreased affinity for primary alcohols, while the affinity for the secondary alcohol 2-propanol is unaltered. 2 Publications2

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03205, Pyrroloquinoline Quinone

<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 – 341 Publication1 PublicationAdd BLAST34
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002556535 – 623Quinoprotein ethanol dehydrogenaseAdd 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 ↔ 140Combined sources1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The disulfide ring formed between the two adjacent cysteine residues Cys-139 and Cys-140 is essential for efficient electron transfer at pH 7 from QEDH to its natural electron acceptor cytochrome c550.1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9Z4J7

<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 growth on ethanol.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts with cytochrome c550 (PubMed:19224199).

4 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
287.DR97_5865

<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

Secondary structure

1623
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q9Z4J7

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9Z4J7

<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

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 bindingCombined sources1 Publication3
Regioni244 – 281DisorderedSequence analysisAdd BLAST38
Regioni413 – 434DisorderedSequence analysisAdd BLAST22

<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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_018478_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Z4J7

Identification of Orthologs from Complete Genome Data

More...
OMAi
PWNSHLR

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9Z4J7

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, 6 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q9Z4J7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTRTSPAPA GLLRPSLHCL AFAVALGSAG AALAKDVTWE DIANDDKTTG
60 70 80 90 100
DVLQYGMGTH AQRWSPLKQV NADNVFKLTP AWSYSFGDEK QRGQESQAIV
110 120 130 140 150
SDGVIYVTAS YSRLFALDAK TGKRLWTYNH RLPDDIRPCC DVVNRGAAIY
160 170 180 190 200
GDKVFFGTLD ASVVALNKNT GKVVWKKKFA DHGAGYTMTG APTIVKDGKT
210 220 230 240 250
GKVLLIHGSS GDEFGVVGRL FARDPDTGEE IWMRPFVEGH MGRLNGKDST
260 270 280 290 300
VTGDVKAPSW PDDRNSPTGK VESWSHGGGA PWQSASFDAE TNTIIVGAGN
310 320 330 340 350
PGPWNTWART AKGGNPHDYD SLYTSGQVGV DPSSGEVKWF YQHTPNDAWD
360 370 380 390 400
FSGNNELVLF DYKAKDGKIV KATAHADRNG FFYVVDRSNG KLQNAFPFVD
410 420 430 440 450
NITWASHIDL KTGRPVEREG QRPPLPEPGQ KHGKAVEVSP PFLGGKNWNP
460 470 480 490 500
MAYSQDTGLF YVPANHWKED YWTEEVSYTK GSAYLGMGFR IKRMYDDHVG
510 520 530 540 550
SLRAMDPVSG KVVWEHKEHL PLWAGVLATA GNLVFTGTGD GYFKAFDAKS
560 570 580 590 600
GKELWKFQTG SGIVSPPITW EQDGEQYLGV TVGYGGAVPL WGGDMADLTR
610 620
PVAQGGSFWV FKLPSWDNRT ASR
Length:623
Mass (Da):68,123
Last modified:May 1, 1999 - 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:i32DDE5DF20B291D6
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ009858 Genomic DNA Translation: CAA08896.1
AE004091 Genomic DNA Translation: AAG05370.1
AF068264 Genomic DNA Translation: AAC79657.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B83399

NCBI Reference Sequences

More...
RefSeqi
NP_250672.1, NC_002516.2
WP_003088524.1, NZ_QZGE01000030.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAG05370; AAG05370; PA1982

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
880475

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pae:PA1982

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|208964.12.peg.2066

<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
AJ009858 Genomic DNA Translation: CAA08896.1
AE004091 Genomic DNA Translation: AAG05370.1
AF068264 Genomic DNA Translation: AAC79657.1
PIRiB83399
RefSeqiNP_250672.1, NC_002516.2
WP_003088524.1, NZ_QZGE01000030.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FLGX-ray2.60A/B35-616[»]
SMRiQ9Z4J7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi287.DR97_5865

Chemistry databases

DrugBankiDB03205, Pyrroloquinoline Quinone

Proteomic databases

PaxDbiQ9Z4J7

Genome annotation databases

EnsemblBacteriaiAAG05370; AAG05370; PA1982
GeneIDi880475
KEGGipae:PA1982
PATRICifig|208964.12.peg.2066

Organism-specific databases

PseudoCAPiPA1982

Phylogenomic databases

HOGENOMiCLU_018478_0_0_6
InParanoidiQ9Z4J7
OMAiPWNSHLR
PhylomeDBiQ9Z4J7

Enzyme and pathway databases

UniPathwayiUPA00780;UER00767
BRENDAi1.1.2.8, 5087
1.1.2.B3, 5087

Miscellaneous databases

EvolutionaryTraceiQ9Z4J7

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, 6 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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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<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_PSEAE
<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: Q9Z4J7
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: February 23, 2022
This is version 148 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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