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UniProtKB - P38489 (NFSB_ECOLI)

Entry version 164 (26 Feb 2020)
Sequence version 1 (01 Oct 1994)
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Protein

Oxygen-insensitive NAD(P)H nitroreductase

Gene

nfsB

Organism
Escherichia coli (strain K12)
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

Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.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

FMN

<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

Subject to competitive inhibition by dicoumarol, nicotinic acid and acetate with respect to NADH. Subject to uncompetitive inhibition by dicoumarol, nicotinic acid and acetate with respect to nitrofurazone and nitrofurantoin.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=350 µM for NADH1 Publication
  2. KM=1850 µM for nitrofurazone1 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 sitei41NAD or NADP; via amide nitrogen1
    Binding sitei71FMN3 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 bindingi10 – 14FMN3 Publications5
    Nucleotide bindingi153 – 158NAD or NADPBy similarity6
    Nucleotide bindingi165 – 166FMN3 Publications2
    Nucleotide bindingi205 – 207FMN3 Publications3

    <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 ...

    GO - Biological processi

    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
    LigandFlavoprotein, FMN, NAD, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:DIHYDROPTERIREDUCT-MONOMER
    ECOL316407:JW0567-MONOMER
    MetaCyc:DIHYDROPTERIREDUCT-MONOMER

    <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:
    Oxygen-insensitive NAD(P)H nitroreductase (EC:1.-.-.-)
    Alternative name(s):
    Dihydropteridine reductase (EC:1.5.1.34)
    FMN-dependent nitroreductase
    <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:nfsB1 Publication
    Synonyms:dprA, nfnB1 Publication, nfsI, ntr
    Ordered Locus Names:b0578, JW0567
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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
    • UP000000318 <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
    • UP000000625 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 ...

    <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

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL1075080

    Drug and drug target database

    More...    DrugBanki    		DB04138 2,4-Dinitro,5-[Bis(2-Bromoethyl)Amino]-N-(2',3'-Dioxopropyl)Benzamide
    DB03228 5-[Bis-2(Chloro-Ethyl)-Amino]-2,4-Dintro-Benzamide
    DB04392 Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone]
    DB04272 Citric acid
    DB03247 Flavin mononucleotide
    DB04253 Tretazicar

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000727111 – 217Oxygen-insensitive NAD(P)H nitroreductaseAdd BLAST217

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P38489

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P38489

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

    More...    PaxDbi    		P38489

    PRoteomics IDEntifications database

    More...    PRIDEi    		P38489

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...    SWISS-2DPAGEi    		P38489

    <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.

    4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-909296,EBI-909296

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4262913, 20 interactors
    850145, 1 interactor

    Database of interacting proteins

    More...    DIPi    		DIP-10330N

    Protein interaction database and analysis system

    More...    IntActi    		P38489, 12 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0578

    <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

    1217
    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    		P38489

    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    		P38489

    <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 nitroreductase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4108RCM Bacteria
    COG0778 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_070764_4_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P38489

    KEGG Orthology (KO)

    More...    KOi    		K10679

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P38489

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd02149 NfsB_like_nitroreductase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.109.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR033878 NfsB-like
    IPR029479 Nitroreductase
    IPR000415 Nitroreductase-like

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00881 Nitroreductase, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF55469 SSF55469, 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.

    P38489-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV 
            60         70         80         90        100
    ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD 
           110        120        130        140        150
    QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF 
           160        170        180        190        200
    LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN 
           210 
    ATLPKSRLPQ NITLTEV
    Length:217
    Mass (Da):23,905
    Last modified:October 1, 1994 - 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:iA516CEFC3D46AEAC
    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 conflicti5S → C AA sequence (PubMed:3060113).Curated1
    Sequence conflicti10 – 12RHS → CIV AA sequence (PubMed:3060113).Curated3
    Sequence conflicti19S → M AA sequence (PubMed:3060113).Curated1
    Sequence conflicti21Missing AA sequence (PubMed:1472094).Curated1
    Sequence conflicti28E → D AA sequence (PubMed:1472094).Curated1
    Sequence conflicti180E → I AA sequence (PubMed:1472094).Curated1

    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
    		D25414 Genomic DNA Translation: BAA05004.1
    U07860 Genomic DNA Translation: AAC43263.1
    U82598 Genomic DNA Translation: AAB40776.1
    U00096 Genomic DNA Translation: AAC73679.1
    AP009048 Genomic DNA Translation: BAA35218.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		I67685
    S01818

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415110.1, NC_000913.3
    WP_000351487.1, NZ_SSZK01000024.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73679; AAC73679; b0578
    BAA35218; BAA35218; BAA35218

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		945778

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0567
    eco:b0578

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1696

    <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
    		D25414 Genomic DNA Translation: BAA05004.1
    U07860 Genomic DNA Translation: AAC43263.1
    U82598 Genomic DNA Translation: AAB40776.1
    U00096 Genomic DNA Translation: AAC73679.1
    AP009048 Genomic DNA Translation: BAA35218.1
    PIRiI67685
    S01818
    RefSeqiNP_415110.1, NC_000913.3
    WP_000351487.1, NZ_SSZK01000024.1

    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
    1DS7X-ray2.06A/B1-217[»]
    1ICRX-ray1.70A/B1-217[»]
    1ICUX-ray1.80A/B/C/D1-217[»]
    1ICVX-ray2.40A/B/C/D1-217[»]
    1IDTX-ray2.00A/B1-217[»]
    1OO5X-ray2.50A/B1-217[»]
    1OO6X-ray2.00A/B1-217[»]
    1OONX-ray2.49A/B1-217[»]
    1OOQX-ray2.00A/B1-217[»]
    1YKIX-ray1.70A/B/C/D1-217[»]
    1YLRX-ray1.70A/B1-217[»]
    1YLUX-ray2.00A/B1-217[»]
    3X21X-ray3.00A/B/C/D/E/F/G/H/I/J1-217[»]
    3X22X-ray2.00A/B1-217[»]
    SMRiP38489
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4262913, 20 interactors
    850145, 1 interactor
    DIPiDIP-10330N
    IntActiP38489, 12 interactors
    STRINGi511145.b0578

    Chemistry databases

    ChEMBLiCHEMBL1075080
    DrugBankiDB04138 2,4-Dinitro,5-[Bis(2-Bromoethyl)Amino]-N-(2',3'-Dioxopropyl)Benzamide
    DB03228 5-[Bis-2(Chloro-Ethyl)-Amino]-2,4-Dintro-Benzamide
    DB04392 Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone]
    DB04272 Citric acid
    DB03247 Flavin mononucleotide
    DB04253 Tretazicar

    2D gel databases

    SWISS-2DPAGEiP38489

    Proteomic databases

    EPDiP38489
    jPOSTiP38489
    PaxDbiP38489
    PRIDEiP38489

    Genome annotation databases

    EnsemblBacteriaiAAC73679; AAC73679; b0578
    BAA35218; BAA35218; BAA35218
    GeneIDi945778
    KEGGiecj:JW0567
    eco:b0578
    PATRICifig|1411691.4.peg.1696

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...    EchoBASEi    		EB4146

    Phylogenomic databases

    eggNOGiENOG4108RCM Bacteria
    COG0778 LUCA
    HOGENOMiCLU_070764_4_1_6
    InParanoidiP38489
    KOiK10679
    PhylomeDBiP38489

    Enzyme and pathway databases

    BioCyciEcoCyc:DIHYDROPTERIREDUCT-MONOMER
    ECOL316407:JW0567-MONOMER
    MetaCyc:DIHYDROPTERIREDUCT-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP38489

    Protein Ontology

    More...    PROi    		PR:P38489

    Family and domain databases

    CDDicd02149 NfsB_like_nitroreductase, 1 hit
    Gene3Di3.40.109.10, 1 hit
    InterProiView protein in InterPro
    IPR033878 NfsB-like
    IPR029479 Nitroreductase
    IPR000415 Nitroreductase-like
    PfamiView protein in Pfam
    PF00881 Nitroreductase, 1 hit
    SUPFAMiSSF55469 SSF55469, 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 nameiNFSB_ECOLI
    <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: P38489
    Secondary accession number(s): P19575
    <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: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: February 26, 2020
    This is version 164 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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