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UniProtKB - P38489 (NFSB_ECOLI)

Entry version 172 (23 Feb 2022)
Sequence version 1 (01 Oct 1994)
Previous versions | rss
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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 sitei14NADBy similarity1
Binding sitei41NAD; via amide nitrogenBy similarity1
Binding sitei71FMN3 Publications1
Binding sitei71NADBy similarity1
Binding sitei74NADBy similarity1
Binding sitei107NAD; via carbonyl oxygenBy similarity1

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 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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.7.1.B2, 2026

<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

<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, 5-[Bis(2-bromoethyl)amino]-N-(2,3-dioxopropyl)-2,4-dinitrobenzamide
DB03228, 5-[Bis-2(Chloro-Ethyl)-Amino]-2,4-Dintro-Benzamide
DB04392, Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone]
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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000727111 – 217Oxygen-insensitive NAD(P)H nitroreductaseAdd BLAST217

Proteomic databases

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">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P38489
With#Exp.IntAct
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

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P38489

<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		COG0778, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_070764_4_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P38489

Database for complete collections of gene phylogenies

More...PhylomeDBi		P38489

Family and domain databases

Conserved Domains Database

More...CDDi		cd02149, NfsB-like, 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

BindingDBiP38489
ChEMBLiCHEMBL1075080
DrugBankiDB04138, 5-[Bis(2-bromoethyl)amino]-N-(2,3-dioxopropyl)-2,4-dinitrobenzamide
DB03228, 5-[Bis-2(Chloro-Ethyl)-Amino]-2,4-Dintro-Benzamide
DB04392, Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone]
DB03247, Flavin mononucleotide
DB04253, Tretazicar

2D gel databases

SWISS-2DPAGEiP38489

Proteomic databases

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

eggNOGiCOG0778, Bacteria
HOGENOMiCLU_070764_4_1_6
InParanoidiP38489
PhylomeDBiP38489

Enzyme and pathway databases

BioCyciEcoCyc:DIHYDROPTERIREDUCT-MONOMER
BRENDAi1.7.1.B2, 2026

Miscellaneous databases

EvolutionaryTraceiP38489

Protein Ontology

More...PROi		PR:P38489

Family and domain databases

CDDicd02149, NfsB-like, 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

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 23, 2022
This is version 172 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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