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UniProtKB - P24183 (FDNG_ECOLI)

Entry version 185 (11 Dec 2019)
Sequence version 3 (26 Feb 2008)
Previous versions | rss
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Protein

Formate dehydrogenase, nitrate-inducible, major subunit

Gene

fdnG

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

Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).1 Publication

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi50Iron-sulfur (4Fe-4S)1
Metal bindingi53Iron-sulfur (4Fe-4S)1
Metal bindingi57Iron-sulfur (4Fe-4S)1
Metal bindingi92Iron-sulfur (4Fe-4S)1
Metal bindingi196Molybdenum1

<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

  • anaerobic respiration Source: EcoCyc
  • formate oxidation Source: EcoCyc
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
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:FDNG-MONOMER
ECOL316407:JW1470-MONOMER
MetaCyc:FDNG-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.5.6 2026

Protein family/group databases

Transport Classification Database

More...TCDBi		5.A.3.2.1 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:
Formate dehydrogenase, nitrate-inducible, major subunit (EC:1.17.5.31 Publication)
Alternative name(s):
Anaerobic formate dehydrogenase major subunit
Formate dehydrogenase-N subunit alpha
Short name:
FDH-N 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:fdnG
Ordered Locus Names:b1474, JW1470
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

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

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Periplasm

<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

Drug and drug target database

More...DrugBanki		DB07918 2-HEPTYL-4-HYDROXY QUINOLINE N-OXIDE

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 33Tat-type signalPROSITE-ProRule annotationAdd BLAST33
<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_000006322234 – 1015Formate dehydrogenase, nitrate-inducible, major subunitAdd BLAST982

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P24183

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

More...PaxDbi		P24183

PRoteomics IDEntifications database

More...PRIDEi		P24183

<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 under anaerobic conditions.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Trimer of heterotrimers, consisting of subunits alpha, beta and gamma.

1 Publication

<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

WithEntry#Exp.IntActNotes
P130246EBI-550115,EBI-550129

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4262900, 30 interactors
850396, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1975 Formate dehydrogenase N complex

Database of interacting proteins

More...DIPi		DIP-9573N

Protein interaction database and analysis system

More...IntActi		P24183, 15 interactors

STRING: functional protein association networks

More...STRINGi		511145.b1474

<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

11015
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		P24183

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		P24183

<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 – 1064Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST64

<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 prokaryotic molybdopterin-containing oxidoreductase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4107QIW Bacteria
COG0243 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000163271

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P24183

KEGG Orthology (KO)

More...KOi		K08348

Database for complete collections of gene phylogenies

More...PhylomeDBi		P24183

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009010 Asp_de-COase-like_dom_sf
IPR006443 Formate-DH-alph_fdnG
IPR006657 MoPterin_dinucl-bd_dom
IPR006656 Mopterin_OxRdtase
IPR006963 Mopterin_OxRdtase_4Fe-4S_dom
IPR006655 Mopterin_OxRdtase_prok_CS
IPR027467 MopterinOxRdtase_cofactor_BS
IPR006311 TAT_signal

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04879 Molybdop_Fe4S4, 1 hit
PF00384 Molybdopterin, 1 hit
PF01568 Molydop_binding, 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		TIGR01553 formate-DH-alph, 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
PS00932 MOLYBDOPTERIN_PROK_3, 1 hit
PS51318 TAT, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P24183-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDVSRRQFFK ICAGGMAGTT VAALGFAPKQ ALAQARNYKL LRAKEIRNTC 
        60         70         80         90        100
TYCSVGCGLL MYSLGDGAKN AREAIYHIEG DPDHPVSRGA LCPKGAGLLD 
       110        120        130        140        150
YVNSENRLRY PEYRAPGSDK WQRISWEEAF SRIAKLMKAD RDANFIEKNE 
       160        170        180        190        200
QGVTVNRWLS TGMLCASGAS NETGMLTQKF ARSLGMLAVD NQARVUHGPT 
       210        220        230        240        250
VASLAPTFGR GAMTNHWVDI KNANVVMVMG GNAAEAHPVG FRWAMEAKNN 
       260        270        280        290        300
NDATLIVVDP RFTRTASVAD IYAPIRSGTD ITFLSGVLRY LIENNKINAE 
       310        320        330        340        350
YVKHYTNASL LVRDDFAFED GLFSGYDAEK RQYDKSSWNY QLDENGYAKR 
       360        370        380        390        400
DETLTHPRCV WNLLKEHVSR YTPDVVENIC GTPKADFLKV CEVLASTSAP 
       410        420        430        440        450
DRTTTFLYAL GWTQHTVGAQ NIRTMAMIQL LLGNMGMAGG GVNALRGHSN 
       460        470        480        490        500
IQGLTDLGLL STSLPGYLTL PSEKQVDLQS YLEANTPKAT LADQVNYWSN 
       510        520        530        540        550
YPKFFVSLMK SFYGDAAQKE NNWGYDWLPK WDQTYDVIKY FNMMDEGKVT 
       560        570        580        590        600
GYFCQGFNPV ASFPDKNKVV SCLSKLKYMV VIDPLVTETS TFWQNHGESN 
       610        620        630        640        650
DVDPASIQTE VFRLPSTCFA EEDGSIANSG RWLQWHWKGQ DAPGEARNDG 
       660        670        680        690        700
EILAGIYHHL RELYQSEGGK GVEPLMKMSW NYKQPHEPQS DEVAKENNGY 
       710        720        730        740        750
ALEDLYDANG VLIAKKGQLL SSFAHLRDDG TTASSCWIYT GSWTEQGNQM 
       760        770        780        790        800
ANRDNSDPSG LGNTLGWAWA WPLNRRVLYN RASADINGKP WDPKRMLIQW 
       810        820        830        840        850
NGSKWTGNDI PDFGNAAPGT PTGPFIMQPE GMGRLFAINK MAEGPFPEHY 
       860        870        880        890        900
EPIETPLGTN PLHPNVVSNP VVRLYEQDAL RMGKKEQFPY VGTTYRLTEH 
       910        920        930        940        950
FHTWTKHALL NAIAQPEQFV EISETLAAAK GINNGDRVTV SSKRGFIRAV 
       960        970        980        990       1000
AVVTRRLKPL NVNGQQVETV GIPIHWGFEG VARKGYIANT LTPNVGDANS 
      1010 
QTPEYKAFLV NIEKA
Length:1,015
Mass (Da):112,963
Last modified:February 26, 2008 - v3
<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:iE4B9449D6B2407DA
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 conflicti96A → P (PubMed:1834669).Curated1
Sequence conflicti484 – 491ANTPKATL → GEHAERRRW (PubMed:1834669).Curated8
Sequence conflicti941S → A (PubMed:1834669).Curated1

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the occurrence of non-standard amino acids selenocysteine (Sec) or pyrrolysine (Pyl) in the protein sequence.<p><a href='/help/non_std' target='_top'>More...</a></p>Non-standard residuei196Selenocysteine1

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
M75029 Genomic DNA No translation available.
U00096 Genomic DNA Translation: AAD13438.1
AP009048 Genomic DNA Translation: BAA15123.1

Protein sequence database of the Protein Information Resource

More...PIRi		E64900 JS0628

NCBI Reference Sequences

More...RefSeqi		NP_415991.1, NC_000913.3
WP_010723100.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAD13438; AAD13438; b1474
BAA15123; BAA15123; BAA15123

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946035

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1470
eco:b1474

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|511145.12.peg.1540

Keywords - Coding sequence diversityi

Selenocysteine

<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
M75029 Genomic DNA No translation available.
U00096 Genomic DNA Translation: AAD13438.1
AP009048 Genomic DNA Translation: BAA15123.1
PIRiE64900 JS0628
RefSeqiNP_415991.1, NC_000913.3
WP_010723100.1, NZ_LN832404.1

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
1KQFX-ray1.60A1-1015[»]
1KQGX-ray2.80A1-1015[»]
SMRiP24183
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4262900, 30 interactors
850396, 1 interactor
ComplexPortaliCPX-1975 Formate dehydrogenase N complex
DIPiDIP-9573N
IntActiP24183, 15 interactors
STRINGi511145.b1474

Chemistry databases

DrugBankiDB07918 2-HEPTYL-4-HYDROXY QUINOLINE N-OXIDE

Protein family/group databases

TCDBi5.A.3.2.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

Proteomic databases

jPOSTiP24183
PaxDbiP24183
PRIDEiP24183

Genome annotation databases

EnsemblBacteriaiAAD13438; AAD13438; b1474
BAA15123; BAA15123; BAA15123
GeneIDi946035
KEGGiecj:JW1470
eco:b1474
PATRICifig|511145.12.peg.1540

Organism-specific databases

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

More...EchoBASEi		EB1209

Phylogenomic databases

eggNOGiENOG4107QIW Bacteria
COG0243 LUCA
HOGENOMiHOG000163271
InParanoidiP24183
KOiK08348
PhylomeDBiP24183

Enzyme and pathway databases

BioCyciEcoCyc:FDNG-MONOMER
ECOL316407:JW1470-MONOMER
MetaCyc:FDNG-MONOMER
BRENDAi1.1.5.6 2026

Miscellaneous databases

EvolutionaryTraceiP24183

Protein Ontology

More...PROi		PR:P24183

Family and domain databases

InterProiView protein in InterPro
IPR009010 Asp_de-COase-like_dom_sf
IPR006443 Formate-DH-alph_fdnG
IPR006657 MoPterin_dinucl-bd_dom
IPR006656 Mopterin_OxRdtase
IPR006963 Mopterin_OxRdtase_4Fe-4S_dom
IPR006655 Mopterin_OxRdtase_prok_CS
IPR027467 MopterinOxRdtase_cofactor_BS
IPR006311 TAT_signal
PfamiView protein in Pfam
PF04879 Molybdop_Fe4S4, 1 hit
PF00384 Molybdopterin, 1 hit
PF01568 Molydop_binding, 1 hit
SMARTiView protein in SMART
SM00926 Molybdop_Fe4S4, 1 hit
SUPFAMiSSF50692 SSF50692, 1 hit
TIGRFAMsiTIGR01553 formate-DH-alph, 1 hit
PROSITEiView protein in PROSITE
PS51669 4FE4S_MOW_BIS_MGD, 1 hit
PS00551 MOLYBDOPTERIN_PROK_1, 1 hit
PS00932 MOLYBDOPTERIN_PROK_3, 1 hit
PS51318 TAT, 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 nameiFDNG_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: P24183
Secondary accession number(s): P78261
<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: March 1, 1992
Last sequence update: February 26, 2008
Last modified: December 11, 2019
This is version 185 of the entry and version 3 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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