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Protein

Respiratory nitrate reductase 1 alpha chain

Gene

narG

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

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi50Iron-sulfur (4Fe-4S); via pros nitrogen1
Metal bindingi54Iron-sulfur (4Fe-4S)1
Metal bindingi58Iron-sulfur (4Fe-4S)1
Metal bindingi93Iron-sulfur (4Fe-4S)1
Metal bindingi223Molybdenum1

<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

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • nitrate assimilation Source: UniProtKB-KW
  • nitrate metabolic process Source: EcoCyc

<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, Nitrate assimilation, Transport
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:NARG-MONOMER
MetaCyc:NARG-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.7.5.1 2026
1.7.99.4 2026

Protein family/group databases

Transport Classification Database

More...
TCDBi
5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

<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:
Respiratory nitrate reductase 1 alpha chain (EC:1.7.5.1)
Alternative name(s):
Nitrate reductase A subunit alpha
Quinol-nitrate oxidoreductase subunit alpha
<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:narG
Synonyms:bisD, narC
Ordered Locus Names:b1224, JW1215
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10638 narG

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section 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_and_biotech_section">'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>Mutagenesisi50H → S: Loss of activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04464 N-Formylmethionine

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00000632332 – 1247Respiratory nitrate reductase 1 alpha chainAdd BLAST1246

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P09152

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

More...
PaxDbi
P09152

PRoteomics IDEntifications database

More...
PRIDEi
P09152

<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

By nitrate.

<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

Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane. Interacts with the NarJ chaperone.4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4263271, 68 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1974 Nitrate reductase A complex

Database of interacting proteins

More...
DIPi
DIP-10311N

Protein interaction database and analysis system

More...
IntActi
P09152, 23 interactors

Molecular INTeraction database

More...
MINTi
P09152

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_1283

<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

11247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1Q16X-ray1.90A1-1247[»]
1R27X-ray2.00A/C2-1247[»]
1SIWX-ray2.20A2-1247[»]
1Y4ZX-ray2.00A2-1247[»]
1Y5IX-ray1.90A2-1247[»]
1Y5LX-ray2.50A2-1247[»]
1Y5NX-ray2.50A2-1247[»]
3EGWX-ray1.90A2-1245[»]
3IR5X-ray2.30A1-1247[»]
3IR6X-ray2.80A1-1247[»]
3IR7X-ray2.50A1-1247[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P09152

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P09152

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P09152

<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>Domaini43 – 1074Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST65

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Apoenzyme contains at least 2 NarJ-binding sites, one interfering with membrane anchoring and another being involved in molybdenum insertion. The first binding-site is a short peptide sequence near the N-terminus that contains a twin-arginine homologous motif.2 Publications

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CRU Bacteria
COG5013 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000237341

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P09152

KEGG Orthology (KO)

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KOi
K00370

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P09152

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02776 MopB_CT_Nitrate-R-NarG-like, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009010 Asp_de-COase-like_dom_sf
IPR037943 MopB_CT_Nitrate-R-NarG-like
IPR006657 MoPterin_dinucl-bd_dom
IPR006656 Mopterin_OxRdtase
IPR006963 Mopterin_OxRdtase_4Fe-4S_dom
IPR006655 Mopterin_OxRdtase_prok_CS
IPR027467 MopterinOxRdtase_cofactor_BS
IPR006468 NarG
IPR028189 Nitr_red_alph_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00384 Molybdopterin, 1 hit
PF01568 Molydop_binding, 1 hit
PF14710 Nitr_red_alph_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00926 Molybdop_Fe4S4, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50692 SSF50692, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01580 narG, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51669 4FE4S_MOW_BIS_MGD, 1 hit
PS00551 MOLYBDOPTERIN_PROK_1, 1 hit
PS00490 MOLYBDOPTERIN_PROK_2, 1 hit
PS00932 MOLYBDOPTERIN_PROK_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

P09152-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKFLDRFRY FKQKGETFAD GHGQLLNTNR DWEDGYRQRW QHDKIVRSTH
60 70 80 90 100
GVNCTGSCSW KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS
110 120 130 140 150
WYLYSANRLK YPMMRKRLMK MWREAKALHS DPVEAWASII EDADKAKSFK
160 170 180 190 200
QARGRGGFVR SSWQEVNELI AASNVYTIKN YGPDRVAGFS PIPAMSMVSY
210 220 230 240 250
ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE SADWYNSSYI
260 270 280 290 300
IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ
310 320 330 340 350
GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY
360 370 380 390 400
AAGRMLRAAD LVDALGQENN PEWKTVAFNT NGEMVAPNGS IGFRWGEKGK
410 420 430 440 450
WNLEQRDGKT GEETELQLSL LGSQDEIAEV GFPYFGGDGT EHFNKVELEN
460 470 480 490 500
VLLHKLPVKR LQLADGSTAL VTTVYDLTLA NYGLERGLND VNCATSYDDV
510 520 530 540 550
KAYTPAWAEQ ITGVSRSQII RIAREFADNA DKTHGRSMII VGAGLNHWYH
560 570 580 590 600
LDMNYRGLIN MLIFCGCVGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ
610 620 630 640 650
RPARHMNSTS YFYNHSSQWR YETVTAEELL SPMADKSRYT GHLIDFNVRA
660 670 680 690 700
ERMGWLPSAP QLGTNPLTIA GEAEKAGMNP VDYTVKSLKE GSIRFAAEQP
710 720 730 740 750
ENGKNHPRNL FIWRSNLLGS SGKGHEFMLK YLLGTEHGIQ GKDLGQQGGV
760 770 780 790 800
KPEEVDWQDN GLEGKLDLVV TLDFRLSSTC LYSDIILPTA TWYEKDDMNT
810 820 830 840 850
SDMHPFIHPL SAAVDPAWEA KSDWEIYKAI AKKFSEVCVG HLGKETDIVT
860 870 880 890 900
LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIMVVE RDYPATYERF
910 920 930 940 950
TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI
960 970 980 990 1000
DAAEMILTLA PETNGQVAVK AWAALSEFTG RDHTHLALNK EDEKIRFRDI
1010 1020 1030 1040 1050
QAQPRKIISS PTWSGLEDEH VSYNAGYTNV HELIPWRTLS GRQQLYQDHQ
1060 1070 1080 1090 1100
WMRDFGESLL VYRPPIDTRS VKEVIGQKSN GNQEKALNFL TPHQKWGIHS
1110 1120 1130 1140 1150
TYSDNLLMLT LGRGGPVVWL SEADAKDLGI ADNDWIEVFN SNGALTARAV
1160 1170 1180 1190 1200
VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG
1210 1220 1230 1240
GYAHLAYGFN YYGTVGSNRD EFVVVRKMKN IDWLDGEGND QVQESVK
Length:1,247
Mass (Da):140,489
Last modified:January 23, 2007 - v4
<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:i640ABAD5FF01DF25
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 conflicti10Y → K AA sequence (PubMed:3053688).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
X16181 Genomic DNA Translation: CAA34303.1
X01164 Genomic DNA Translation: CAA25611.1
M11586 Genomic DNA Translation: AAA24201.1
U00096 Genomic DNA Translation: AAC74308.1
AP009048 Genomic DNA Translation: BAA36094.1
X15996 Genomic DNA Translation: CAA34127.1
L36649 Genomic DNA Translation: AAA64296.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E64869 RDECNA

NCBI Reference Sequences

More...
RefSeqi
NP_415742.1, NC_000913.3
WP_000032939.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74308; AAC74308; b1224
BAA36094; BAA36094; BAA36094

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945782

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1215
eco:b1224

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1057

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16181 Genomic DNA Translation: CAA34303.1
X01164 Genomic DNA Translation: CAA25611.1
M11586 Genomic DNA Translation: AAA24201.1
U00096 Genomic DNA Translation: AAC74308.1
AP009048 Genomic DNA Translation: BAA36094.1
X15996 Genomic DNA Translation: CAA34127.1
L36649 Genomic DNA Translation: AAA64296.1
PIRiE64869 RDECNA
RefSeqiNP_415742.1, NC_000913.3
WP_000032939.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90A1-1247[»]
1R27X-ray2.00A/C2-1247[»]
1SIWX-ray2.20A2-1247[»]
1Y4ZX-ray2.00A2-1247[»]
1Y5IX-ray1.90A2-1247[»]
1Y5LX-ray2.50A2-1247[»]
1Y5NX-ray2.50A2-1247[»]
3EGWX-ray1.90A2-1245[»]
3IR5X-ray2.30A1-1247[»]
3IR6X-ray2.80A1-1247[»]
3IR7X-ray2.50A1-1247[»]
ProteinModelPortaliP09152
SMRiP09152
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263271, 68 interactors
ComplexPortaliCPX-1974 Nitrate reductase A complex
DIPiDIP-10311N
IntActiP09152, 23 interactors
MINTiP09152
STRINGi316385.ECDH10B_1283

Chemistry databases

DrugBankiDB04464 N-Formylmethionine

Protein family/group databases

TCDBi5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

Proteomic databases

jPOSTiP09152
PaxDbiP09152
PRIDEiP09152

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74308; AAC74308; b1224
BAA36094; BAA36094; BAA36094
GeneIDi945782
KEGGiecj:JW1215
eco:b1224
PATRICifig|1411691.4.peg.1057

Organism-specific databases

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

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EchoBASEi
EB0632
EcoGeneiEG10638 narG

Phylogenomic databases

eggNOGiENOG4105CRU Bacteria
COG5013 LUCA
HOGENOMiHOG000237341
InParanoidiP09152
KOiK00370
PhylomeDBiP09152

Enzyme and pathway databases

BioCyciEcoCyc:NARG-MONOMER
MetaCyc:NARG-MONOMER
BRENDAi1.7.5.1 2026
1.7.99.4 2026

Miscellaneous databases

EvolutionaryTraceiP09152

Protein Ontology

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PROi
PR:P09152

Family and domain databases

CDDicd02776 MopB_CT_Nitrate-R-NarG-like, 1 hit
InterProiView protein in InterPro
IPR009010 Asp_de-COase-like_dom_sf
IPR037943 MopB_CT_Nitrate-R-NarG-like
IPR006657 MoPterin_dinucl-bd_dom
IPR006656 Mopterin_OxRdtase
IPR006963 Mopterin_OxRdtase_4Fe-4S_dom
IPR006655 Mopterin_OxRdtase_prok_CS
IPR027467 MopterinOxRdtase_cofactor_BS
IPR006468 NarG
IPR028189 Nitr_red_alph_N
PfamiView protein in Pfam
PF00384 Molybdopterin, 1 hit
PF01568 Molydop_binding, 1 hit
PF14710 Nitr_red_alph_N, 1 hit
SMARTiView protein in SMART
SM00926 Molybdop_Fe4S4, 1 hit
SUPFAMiSSF50692 SSF50692, 1 hit
TIGRFAMsiTIGR01580 narG, 1 hit
PROSITEiView protein in PROSITE
PS51669 4FE4S_MOW_BIS_MGD, 1 hit
PS00551 MOLYBDOPTERIN_PROK_1, 1 hit
PS00490 MOLYBDOPTERIN_PROK_2, 1 hit
PS00932 MOLYBDOPTERIN_PROK_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiNARG_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: P09152
Secondary accession number(s): P78294
<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: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 193 of the entry and version 4 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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