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Entry version 106 (02 Jun 2021)
Sequence version 1 (01 Mar 2001)
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Protein

FMN-dependent NAD(P)H:quinone oxidoreductase 1

Gene

azoR1

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

Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (PubMed:24915188).

Shows a preference for benzoquinones (PubMed:24915188).

1 Publication

Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines (PubMed:17904577, PubMed:20057057).

NADPH is the preferred electron donor for azoreductase activity, but it can also use NADH (PubMed:17904577).

Can reduce different classes of azo dyes, including the common azo dyes methyl red and p-aminoazobenzene sulfonamide (PAABSA) (PubMed:17904577, PubMed:20057057).

Can activate several azo pro-drugs used in the treatment of inflammatory bowel disease (IBD), including balsalazide, sulfasalazine and olsalazine (PubMed:17904577, PubMed:20057057).

Also acts as a nitrodeductase, and can reduce and hence activate the nitroaromatic drug nitrofurazone, a broad spectrum antibiotic (PubMed:22355582).

3 Publications

Miscellaneous

Rate of quinone reduction is higher than reduction of azo substrates, suggesting the enzyme is better suited for carrying out quinone rather than azo reduction.1 Publication

<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

FMNUniRule annotation2 PublicationsNote: Binds 1 FMN per subunit.UniRule annotation2 Publications

<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

Azoreductase activity increases with salt strength.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

kcat is 13 sec(-1) with methyl red as substrate. kcat is 13 sec(-1) with sulfasalazine as substrate. kcat is 37 sec(-1) with balsalazide as substrate. kcat is 2.5 sec(-1) with olsalazine as substrate. kcat is 10 sec(-1) with NADH as substrate. kcat is 34 sec(-1) with NADPH as substrate.1 Publication
  1. KM=76 µM for methyl red (in the presence of NADPH)1 Publication
  2. KM=92.7 µM for methyl red (in the presence of NADPH)1 Publication
  3. KM=69 µM for sulfasalazine (in the presence of NADPH)1 Publication
  4. KM=124 µM for balsalazide (in the presence of NADPH)1 Publication
  5. KM=98.6 µM for balsalazide (in the presence of NADPH)1 Publication
  6. KM=104 µM for olsalazine (in the presence of NADPH)1 Publication
  7. KM=15.7 µM for nitrofurazone1 Publication
  8. KM=464 µM for NADH (in the presence of methyl red)1 Publication
  9. KM=538 µM for NADH (in the presence of methyl red)1 Publication
  10. KM=1100 µM for NADPH (in the presence of methyl red)1 Publication
  11. KM=1197 µM for NADPH (in the presence of methyl red)1 Publication
  1. Vmax=28 µmol/sec/mg enzyme with methyl red as substrate (in the presence of NADPH)1 Publication
  2. Vmax=28 µmol/sec/mg enzyme with sulfasalazine as substrate (in the presence of NADPH)1 Publication
  3. Vmax=81 µmol/sec/mg enzyme with balsalazide as substrate (in the presence of NADPH)1 Publication
  4. Vmax=5.4 µmol/sec/mg enzyme with olsalazine as substrate (in the presence of NADPH)1 Publication
  5. Vmax=22 µmol/sec/mg enzyme with NADH as substrate (in the presence of methyl red)1 Publication
  6. Vmax=74 µmol/sec/mg enzyme with NADPH as substrate (in the presence of methyl red)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei10FMNUniRule annotationCombined sources5 Publications1
Binding sitei99SubstrateCombined sources2 Publications1
Binding sitei131SubstrateCombined sources2 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei131Important in the architecture of the active site1 Publication1
Binding sitei187FMNCombined sources3 Publications1
Binding sitei188SubstrateCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi16 – 18FMNUniRule annotationCombined sources5 Publications3
Nucleotide bindingi97 – 100FMNUniRule annotationCombined sources5 Publications4
Nucleotide bindingi145 – 148FMNUniRule annotationCombined sources5 Publications4

<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
LigandFlavoprotein, FMN, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
PAER208964:G1FZ6-798-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.7.1.6, 5087

<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:
FMN-dependent NAD(P)H:quinone oxidoreductase 1Curated (EC:1.6.5.-UniRule annotation1 Publication)
Alternative name(s):
Azo-dye reductase 1UniRule annotation
FMN-dependent NADH-azo compound oxidoreductase 1UniRule annotation
FMN-dependent NADH-azoreductase 1UniRule annotation (EC:1.7.1.17UniRule annotation)
<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:azoR11 PublicationUniRule annotation
Ordered Locus Names:PA0785
<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
PA0785

<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>Mutagenesisi131Y → F: 2-fold increase in specific activity towards methyl red and 20% decrease in specific activity towards balsalazide. 2.5-fold increase in the kcat with NADH as substrate. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB08209, Methyl red

<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 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_00001663471 – 212FMN-dependent NAD(P)H:quinone oxidoreductase 1Add BLAST212

Proteomic databases

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

More...
PaxDbi
Q9I5F3

<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 (PubMed:17904577). Homotetramer formed by a dimer of dimers when the ionic strength is high (PubMed:17904577).

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

Secondary structure

1212
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

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SMRi
Q9I5F3

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9I5F3

<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

<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 azoreductase type 1 family.UniRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_088964_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9I5F3

Identification of Orthologs from Complete Genome Data

More...
OMAi
SSPMYNY

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9I5F3

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.360, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01216, Azoreductase_type1, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003680, Flavodoxin_fold
IPR029039, Flavoprotein-like_sf
IPR023048, NADH:quinone_OxRdtase_FMN_depd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02525, Flavodoxin_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52218, SSF52218, 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.

Q9I5F3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRILAVHAS PRGERSQSRR LAEVFLAAYR EAHPQARVAR REVGRVPLPA
60 70 80 90 100
VTEAFVAAAF HPQPEQRSLA MQADLALSDQ LVGELFDSDL LVISTPMYNF
110 120 130 140 150
SVPSGLKAWI DQIVRLGVTF DFVLDNGVAQ YRPLLRGKRA LIVTSRGGHG
160 170 180 190 200
FGPGGENQAM NHADPWLRTA LGFIGIDEVT VVAAEGEESG GRSFEDSCDE
210
AEQRLLALAR SA
Length:212
Mass (Da):23,050
Last modified:March 1, 2001 - 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:i356AF121972823B2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AE004091 Genomic DNA Translation: AAG04174.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H83547

NCBI Reference Sequences

More...
RefSeqi
NP_249476.1, NC_002516.2
WP_003114189.1, NZ_QZGE01000007.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAG04174; AAG04174; PA0785

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
882036

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pae:PA0785

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|208964.12.peg.816

<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
AE004091 Genomic DNA Translation: AAG04174.1
PIRiH83547
RefSeqiNP_249476.1, NC_002516.2
WP_003114189.1, NZ_QZGE01000007.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V9CX-ray2.18A/B1-212[»]
3KEGX-ray2.10A/B1-212[»]
3LT5X-ray2.30A/B1-212[»]
3R6WX-ray2.08A/B1-212[»]
4N65X-ray1.82A/B1-212[»]
4N9QX-ray2.00A/B1-212[»]
SMRiQ9I5F3
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB08209, Methyl red

Proteomic databases

PaxDbiQ9I5F3

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
882036

Genome annotation databases

EnsemblBacteriaiAAG04174; AAG04174; PA0785
GeneIDi882036
KEGGipae:PA0785
PATRICifig|208964.12.peg.816

Organism-specific databases

PseudoCAPiPA0785

Phylogenomic databases

HOGENOMiCLU_088964_0_0_6
InParanoidiQ9I5F3
OMAiSSPMYNY
PhylomeDBiQ9I5F3

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-798-MONOMER
BRENDAi1.7.1.6, 5087

Miscellaneous databases

EvolutionaryTraceiQ9I5F3

Family and domain databases

Gene3Di3.40.50.360, 1 hit
HAMAPiMF_01216, Azoreductase_type1, 1 hit
InterProiView protein in InterPro
IPR003680, Flavodoxin_fold
IPR029039, Flavoprotein-like_sf
IPR023048, NADH:quinone_OxRdtase_FMN_depd
PfamiView protein in Pfam
PF02525, Flavodoxin_2, 1 hit
SUPFAMiSSF52218, SSF52218, 1 hit

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 nameiAZOR1_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: Q9I5F3
<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: July 26, 2002
Last sequence update: March 1, 2001
Last modified: June 2, 2021
This is version 106 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, Reference proteome

Documents

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