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Entry version 150 (18 Sep 2019)
Sequence version 2 (15 Mar 2005)
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Protein

Alcohol dehydrogenase (quinone), dehydrogenase subunit

Gene

adhA

Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
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 (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: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 Publications

Miscellaneous

Inactive ADH is produced under conditions of low pH and high aeration, where the bypass oxidase activity is highly elevated. In spite of having 10 times less enzyme activity than active ADH, inactive ADH is not distinguished from active ADH with respect to their subunit compositions, molecular sizes and prosthetic groups. It seems that in inactive ADH, an improper interaction between subunit II and subunit I/III complex impairs efficient intersubunit electron transport in the ADH complex.3 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 <a href="http://www.uniprot.org/help/function_section">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

2,6-dichloro-4-dicyanovinylphenol (PC16) and antimycin A inhibit ubiquinol oxidation activity more selectively than the ubiquinone reductase activity.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=7.7 µM for ubiquinone-2 (for ubiquinone reduction activity in inactive ADH at pH 5)1 Publication
  2. KM=8.4 µM for ubiquinone-2 (for ubiquinone reduction activity in active ADH at pH 5)1 Publication
  3. KM=13 µM for ubiquinol-2 (for ubiquinol oxidation activity in inactive ADH at pH 5)1 Publication
  4. KM=32 µM for ethanol (for ubiquinone reduction activity in active ADH at pH 4.5)1 Publication
  5. KM=36 µM for ubiquinol-2 (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
  6. KM=40 µM for ethanol (for ubiquinone reduction activity in inactive ADH at pH 4.5)1 Publication
  7. KM=170 µM for ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
  8. KM=200 µM for ferricyanide (for ubiquinol oxidation activity in inactive ADH at pH 5)1 Publication
  1. Vmax=175 µmol/min/mg enzyme toward ubiquinol-2 (for ubiquinol oxidation activity in inactive ADH at pH 5)1 Publication
  2. Vmax=167 µmol/min/mg enzyme toward ferricyanide (for ubiquinol oxidation activity in inactive ADH at pH 5)1 Publication
  3. Vmax=104 µmol/min/mg enzyme toward ubiquinol-2 (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
  4. Vmax=81 µmol/min/mg enzyme toward ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
  5. Vmax=71 µmol/min/mg enzyme toward ethanol (for ubiquinone reduction activity in active ADH at pH 4.5)1 Publication
  6. Vmax=54 µmol/min/mg enzyme toward ubiquinone-2 (for ubiquinone reduction activity in active ADH at pH 5)1 Publication
  7. Vmax=7.1 µmol/min/mg enzyme toward ethanol (for ubiquinone reduction activity in inactive ADH at pH 4.5)1 Publication
  8. Vmax=2 µmol/min/mg enzyme toward ubiquinone-2 (for ubiquinone reduction activity in inactive ADH at pH 5)1 Publication

pH dependencei

Optimum pH is 5 for ubiquinol oxidation activity.1 Publication

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 sitei95Pyrroloquinoline quinoneBy similarity1
Binding sitei147Pyrroloquinoline 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 bindingi215CalciumBy similarity1
Binding sitei277Pyrroloquinoline quinoneBy similarity1
Metal bindingi297CalciumBy 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 sitei342Proton acceptorBy similarity1
Metal bindingi342CalciumBy similarity1
Binding sitei369Pyrroloquinoline quinoneBy similarity1
Binding sitei588Pyrroloquinoline quinone; via amide nitrogenBy similarity1
Binding sitei653Heme c (covalent)By similarity1
Binding sitei656Heme c (covalent)By similarity1
Metal bindingi657Iron (heme axial ligand); via tele nitrogenBy similarity1
Metal bindingi696Iron (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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15242

<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:1.1.5.53 Publications)
Short name:
ADH1 Publication
Alternative name(s):
Alcohol dehydrogenase (quinone), acceptor subunitCurated
Alcohol dehydrogenase (quinone), subunit I1 Publication
Ethanol:Q2 reductase1 Publication
G3-ADH subunit I1 Publication
Quinohemoprotein alcohol dehydrogenase1 Publication
Quinohemoprotein-cytochrome c complex1 Publication
Ubiquinol oxidase1 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:adhA1 Publication
Ordered Locus Names:GOX1068
<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>OrganismiGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
<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 identifieri290633 [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 lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000006375 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<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 – 341 PublicationAdd 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_000002556235 – 757Alcohol dehydrogenase (quinone), dehydrogenase subunitAdd BLAST723

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei35Pyrrolidone carboxylic acid1 Publication1
<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 bondi141 ↔ 142By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

<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

Constitutively expressed.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_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), a cytochrome c subunit II (AdhB) and a subunit III (AdhS).

1 Publication1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
290633.GOX1068

<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

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SMRi
O05542

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>Domaini640 – 719Cytochrome 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DZG Bacteria
COG4993 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000217981

KEGG Orthology (KO)

More...
KOi
K22473

Identification of Orthologs from Complete Genome Data

More...
OMAi
WNTWART

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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13442 Cytochrome_CBB3, 1 hit
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
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.

O05542-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTSGLLTPIK VTKKRLLSCA AALAFSAAVP VAFAQEDTGT AITSSDNGGH
60 70 80 90 100
PGDWLSYGRS YSEQRYSPLD QINTENVGKL KLAWHYDLDT NRGQEGTPLI
110 120 130 140 150
VNGVMYATTN WSKMKALDAA TGKLLWSYDP KVPGNIADRG CCDTVSRGAA
160 170 180 190 200
YWNGKVYFGT FDGRLIALDA KTGKLVWSVY TIPKEAQLGH QRSYTVDGAP
210 220 230 240 250
RIAKGKVLIG NGGAEFGARG FVSAFDAETG KLDWRFFTVP NPENKPDGAA
260 270 280 290 300
SDDILMSKAY PTWGKNGAWK QQGGGGTVWD SLVYDPVTDL VYLGVGNGSP
310 320 330 340 350
WNYKFRSEGK GDNLFLGSIV AINPDTGKYV WHFQETPMDE WDYTSVQQIM
360 370 380 390 400
TLDMPVNGEM RHVIVHAPKN GFFYIIDAKT GKFITGKPYT YENWANGLDP
410 420 430 440 450
VTGRPNYVPD ALWTLTGKPW LGIPGELGGH NFAAMAYSPK TKLVYIPAQQ
460 470 480 490 500
IPLLYDGQKG GFKAYHDAWN LGLDMNKIGL FDDNDPEHVA AKKDFLKVLK
510 520 530 540 550
GWTVAWDPEK MAPAFTINHK GPWNGGLLAT AGNVIFQGLA NGEFHAYDAT
560 570 580 590 600
NGNDLYSFPA QSAIIAPPVT YTANGKQYVA VEVGWGGIYP FLYGGVARTS
610 620 630 640 650
GWTVNHSRVI AFSLDGKDSL PPKNELGFTP VKPVPTYDEA RQKDGYFMYQ
660 670 680 690 700
TFCSACHGDN AISGGVLPDL RWSGAPRGRE SFYKLVGRGA LTAYGMDRFD
710 720 730 740 750
TSMTPEQIED IRNFIVKRAN ESYDDEVKAR ENSTGVPNDQ FLNVPQSTAD

VPTADHP
Length:757
Mass (Da):82,853
Last modified:March 15, 2005 - v2
<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:i56B3940B711BB0CC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti230G → S in BAA19753 (PubMed:9055427).Curated1
Sequence conflicti675A → R in BAA19753 (PubMed:9055427).Curated1

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
D86375 Genomic DNA Translation: BAA19753.1
CP000009 Genomic DNA Translation: AAW60837.1

NCBI Reference Sequences

More...
RefSeqi
WP_011252629.1, NZ_LT900338.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAW60837; AAW60837; GOX1068

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29628550

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gox:GOX1068

<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
D86375 Genomic DNA Translation: BAA19753.1
CP000009 Genomic DNA Translation: AAW60837.1
RefSeqiWP_011252629.1, NZ_LT900338.1

3D structure databases

SMRiO05542
ModBaseiSearch...

Protein-protein interaction databases

STRINGi290633.GOX1068

Genome annotation databases

EnsemblBacteriaiAAW60837; AAW60837; GOX1068
GeneIDi29628550
KEGGigox:GOX1068

Phylogenomic databases

eggNOGiENOG4105DZG Bacteria
COG4993 LUCA
HOGENOMiHOG000217981
KOiK22473
OMAiWNTWART

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15242

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
PfamiView protein in Pfam
PF13442 Cytochrome_CBB3, 1 hit
PF01011 PQQ, 1 hit
PF13360 PQQ_2, 1 hit
SMARTiView protein in SMART
SM00564 PQQ, 6 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_GLUOX
<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: O05542
Secondary accession number(s): Q5FS09
<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, 1997
Last sequence update: March 15, 2005
Last modified: September 18, 2019
This is version 150 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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