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UniProtKB - Q47945 (ADHB_GLUOX)

Entry version 134 (18 Sep 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Alcohol dehydrogenase (quinone), cytochrome c subunit

Gene

adhB

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

Cytochrome c component of the alcohol dehydrogenase multicomponent enzyme system which is involved in the production of acetic acid and in the ethanol oxidase respiratory chain. 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:1646200, 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.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

heme c1 PublicationNote: Binds 3 heme c groups covalently per subunit.1 Publication

<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=170 µM for ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5)1 Publication
  7. 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=70 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=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 sitei56Heme 1 (covalent)PROSITE-ProRule annotation1
Binding sitei59Heme 1 (covalent)PROSITE-ProRule annotation1
<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 bindingi60Iron (heme 1 axial ligand)PROSITE-ProRule annotation1
Binding sitei204Heme 2 (covalent)PROSITE-ProRule annotation1
Binding sitei207Heme 2 (covalent)PROSITE-ProRule annotation1
Metal bindingi208Iron (heme 2 axial ligand)PROSITE-ProRule annotation1
Binding sitei340Heme 3 (covalent)PROSITE-ProRule annotation1
Binding sitei343Heme 3 (covalent)PROSITE-ProRule annotation1
Metal bindingi344Iron (heme 3 axial ligand)PROSITE-ProRule annotation1

<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

Complete GO annotation on QuickGO ...

<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
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:MONOMER-15243

<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), cytochrome c subunit1 Publication (EC:1.1.5.53 Publications)
Short name:
ADH1 Publication
Alternative name(s):
Alcohol dehydrogenase (quinone), subunit II1 Publication
Cytochrome c-553Curated
Cytochrome c553Curated
Ethanol:Q2 reductase1 Publication
G3-ADH subunit II1 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:adhB1 Publication
Ordered Locus Names:GOX1067
<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 lineageiBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter ›
<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

Complete GO annotation on QuickGO ...

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 – 361 PublicationAdd BLAST36
<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_000000659737 – 478Alcohol dehydrogenase (quinone), cytochrome c subunitAdd BLAST442

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 residuei37Pyrrolidone carboxylic acid1 Publication1

Keywords - PTMi

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.GOX1067

<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>Domaini42 – 145Cytochrome c 1PROSITE-ProRule annotationAdd BLAST104
Domaini189 – 304Cytochrome c 2PROSITE-ProRule annotationAdd BLAST116
Domaini327 – 417Cytochrome c 3PROSITE-ProRule annotationAdd BLAST91

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4107TJ9 Bacteria
ENOG410XPC5 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000178965

KEGG Orthology (KO)

More...KOi		K22474

Identification of Orthologs from Complete Genome Data

More...OMAi		GDYSFED

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.760.10, 3 hits

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
IPR008168 Cyt_C_IC
IPR014353 Membr-bd_ADH_cyt_c

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00034 Cytochrom_C, 1 hit
PF13442 Cytochrome_CBB3, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000018 Mb_ADH_cyt_c, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00605 CYTCHROMECIC

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46626 SSF46626, 3 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51007 CYTC, 3 hits

<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.

Q47945-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLNALTRDRL VSEMKQGWKL AAAIGLMAVS FGAAHAQDAD EALIKRGEYV 
        60         70         80         90        100
ARLSDCIACH TALHGQPYAG GLEIKSPIGT IYSTNITPDP EHGIGNYTLE 
       110        120        130        140        150
DFTKALRKGI RKDGATVYPA MPYPEFARLS DDDIRAMYAF FMHGVKPVAL 
       160        170        180        190        200
QNKAPDISWP LSMRWPLGMW RAMFVPSMTP GVDKSISDPE VARGEYLVNG 
       210        220        230        240        250
PGHCGECHTP RGFGMQVKAY GTAGGNAYLA GGAPIDNWIA PSLRSNSDTG 
       260        270        280        290        300
LGRWSEDDIV TFLKSGRIDH SAVFGGMADV VAYSTQHWSD DDLRATAKYL 
       310        320        330        340        350
KSMPAVPEGK NLGQDDGQTT ALLNKGGQGN AGAEVYLHNC AICHMNDGTG 
       360        370        380        390        400
VNRMFPPLAG NPVVITDDPT SLANVVAFGG ILPPTNSAPS AVAMPGFKNH 
       410        420        430        440        450
LSDQEMADVV NFMRKGWGNN APGTVSASDI QKLRTTGAPV STAGWNVSSK 
       460        470 
GWMAYMPQPY GEDWTFSPQT HTGVDDAQ
Length:478
Mass (Da):51,198
Last modified:November 1, 1996 - 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:i3FBC1F935AD1D866
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
M58760 Genomic DNA Translation: AAA24935.1
D86375 Genomic DNA Translation: BAA19754.1
CP000009 Genomic DNA Translation: AAW60836.1

NCBI Reference Sequences

More...RefSeqi		WP_011252628.1, NZ_LT900338.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAW60836; AAW60836; GOX1067

Database of genes from NCBI RefSeq genomes

More...GeneIDi		29628685

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		gox:GOX1067

<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
M58760 Genomic DNA Translation: AAA24935.1
D86375 Genomic DNA Translation: BAA19754.1
CP000009 Genomic DNA Translation: AAW60836.1
RefSeqiWP_011252628.1, NZ_LT900338.1

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Protein-protein interaction databases

STRINGi290633.GOX1067

Genome annotation databases

EnsemblBacteriaiAAW60836; AAW60836; GOX1067
GeneIDi29628685
KEGGigox:GOX1067

Phylogenomic databases

eggNOGiENOG4107TJ9 Bacteria
ENOG410XPC5 LUCA
HOGENOMiHOG000178965
KOiK22474
OMAiGDYSFED

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15243

Family and domain databases

Gene3Di1.10.760.10, 3 hits
InterProiView protein in InterPro
IPR009056 Cyt_c-like_dom
IPR036909 Cyt_c-like_dom_sf
IPR008168 Cyt_C_IC
IPR014353 Membr-bd_ADH_cyt_c
PfamiView protein in Pfam
PF00034 Cytochrom_C, 1 hit
PF13442 Cytochrome_CBB3, 1 hit
PIRSFiPIRSF000018 Mb_ADH_cyt_c, 1 hit
PRINTSiPR00605 CYTCHROMECIC
SUPFAMiSSF46626 SSF46626, 3 hits
PROSITEiView protein in PROSITE
PS51007 CYTC, 3 hits

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 nameiADHB_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: Q47945
Secondary accession number(s): O08083, Q5FS10
<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: November 1, 1996
Last modified: September 18, 2019
This is version 134 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

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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