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Entry version 193 (08 May 2019)
Sequence version 2 (26 Feb 2008)
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Protein

Formate dehydrogenase H

Gene

fdhF

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

Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors.

<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:

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

Inhibited by aerobic conditions.2 Publications

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 bindingi8Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation2 Publications1
Metal bindingi10Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation2 Publications1
Metal bindingi11Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation2 Publications1
Metal bindingi15Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation2 Publications1
Metal bindingi42Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei44Electron donor/acceptor1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei44Molybdopterin guanine dinucleotide 22 Publications1
Active sitei140Proton donor/acceptor1
Metal bindingi140Molybdenum1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei141Important for catalytic activity1
Binding sitei297Molybdopterin guanine dinucleotide 2; via amide nitrogen2 Publications1
Binding sitei301Molybdopterin guanine dinucleotide 12 Publications1
Sitei333Important for catalytic activity1
Binding sitei335Molybdopterin guanine dinucleotide 12 Publications1
Binding sitei445Molybdopterin guanine dinucleotide 12 Publications1
Binding sitei478Molybdopterin guanine dinucleotide 12 Publications1
Binding sitei588Molybdopterin guanine dinucleotide 1; via amide nitrogen2 Publications1
Binding sitei654Molybdopterin guanine dinucleotide 12 Publications1
Binding sitei655Molybdopterin guanine dinucleotide 22 Publications1
Binding sitei678Molybdopterin guanine dinucleotide 12 Publications1
Binding sitei679Molybdopterin guanine dinucleotide 22 Publications1

<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

<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:FORMATEDEHYDROGH-MONOMER
ECOL316407:JW4040-MONOMER
MetaCyc:FORMATEDEHYDROGH-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.99.33 2026
1.2.1.2 2026

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.D.1.9.2 the h(+) or na(+)-translocating nadh dehydrogenase (ndh) 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 H (EC:1.17.1.93 Publications, EC:1.17.99.73 Publications)
Alternative name(s):
Formate dehydrogenase-H subunit alpha
Short name:
FDH-H
Formate-hydrogen-lyase-linked, selenocysteine-containing polypeptide
<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:fdhF
Ordered Locus Names:b4079, JW4040
<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
EG10285 fdhF

<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

<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
DB02345 Selenocysteine

<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_00000632211 – 715Formate dehydrogenase HAdd BLAST715

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P07658

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

More...
PaxDbi
P07658

PRoteomics IDEntifications database

More...
PRIDEi
P07658

<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 formate. Repressed by oxygen, nitrate, nitrite, and other electron acceptors.

<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

Consists of two separable enzymatic activities: a formate dehydrogenase component (FDH-H) and hydrogenase-3.

2 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

WithEntry#Exp.IntActNotes
hycGP164333EBI-1121603,EBI-541977

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262950, 28 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-317 Formate hydrogenlyase-H/Hydrogenase-3 complex

Database of interacting proteins

More...
DIPi
DIP-9572N

Protein interaction database and analysis system

More...
IntActi
P07658, 13 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b4079

<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

1715
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
P07658

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07658

<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>Domaini1 – 564Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST56

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni110 – 112MGD 1 binding3
Regioni173 – 180MGD 2 binding8
Regioni201 – 204MGD 2 binding4
Regioni221 – 223MGD 2 binding3
Regioni402 – 410MGD 1 binding9
Regioni428 – 429MGD 1 binding2
Regioni579 – 581MGD 1 binding3
Regioni581 – 587MGD 2 binding7
Regioni661 – 662MGD 1 binding2

<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
ENOG4107QIW Bacteria
COG0243 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000031440

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07658

KEGG Orthology (KO)

More...
KOi
K22015

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07658

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02790 MopB_CT_Formate-Dh_H, 1 hit
cd02753 MopB_Formate-Dh-H, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009010 Asp_de-COase-like_dom_sf
IPR041925 CT_Formate-Dh_H
IPR041924 Formate_Dh-H_N
IPR006478 Formate_DH_asu
IPR006657 MoPterin_dinucl-bd_dom
IPR006656 Mopterin_OxRdtase
IPR006963 Mopterin_OxRdtase_4Fe-4S_dom
IPR006655 Mopterin_OxRdtase_prok_CS
IPR027467 MopterinOxRdtase_cofactor_BS

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
TIGR01591 Fdh-alpha, 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>. 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.

P07658-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKVVTVCPY CASGCKINLV VDNGKIVRAE AAQGKTNQGT LCLKGYYGWD
60 70 80 90 100
FINDTQILTP RLKTPMIRRQ RGGKLEPVSW DEALNYVAER LSAIKEKYGP
110 120 130 140 150
DAIQTTGSSR GTGNETNYVM QKFARAVIGT NNVDCCARVU HGPSVAGLHQ
160 170 180 190 200
SVGNGAMSNA INEIDNTDLV FVFGYNPADS HPIVANHVIN AKRNGAKIIV
210 220 230 240 250
CDPRKIETAR IADMHIALKN GSNIALLNAM GHVIIEENLY DKAFVASRTE
260 270 280 290 300
GFEEYRKIVE GYTPESVEDI TGVSASEIRQ AARMYAQAKS AAILWGMGVT
310 320 330 340 350
QFYQGVETVR SLTSLAMLTG NLGKPHAGVN PVRGQNNVQG ACDMGALPDT
360 370 380 390 400
YPGYQYVKDP ANREKFAKAW GVESLPAHTG YRISELPHRA AHGEVRAAYI
410 420 430 440 450
MGEDPLQTDA ELSAVRKAFE DLELVIVQDI FMTKTASAAD VILPSTSWGE
460 470 480 490 500
HEGVFTAADR GFQRFFKAVE PKWDLKTDWQ IISEIATRMG YPMHYNNTQE
510 520 530 540 550
IWDELRHLCP DFYGATYEKM GELGFIQWPC RDTSDADQGT SYLFKEKFDT
560 570 580 590 600
PNGLAQFFTC DWVAPIDKLT DEYPMVLSTV REVGHYSCRS MTGNCAALAA
610 620 630 640 650
LADEPGYAQI NTEDAKRLGI EDEALVWVHS RKGKIITRAQ VSDRPNKGAI
660 670 680 690 700
YMTYQWWIGA CNELVTENLS PITKTPEYKY CAVRVEPIAD QRAAEQYVID
710
EYNKLKTRLR EAALA
Length:715
Mass (Da):79,374
Last modified:February 26, 2008 - v2
<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:iC7C86F6F704A142D
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 conflicti19L → V in AAA23754 (PubMed:2941757).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 residuei140Selenocysteine1 Publication1

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
M13563 Genomic DNA Translation: AAA23754.2
U00006 Genomic DNA Translation: AAC43173.2
U00096 Genomic DNA Translation: AAD13462.1
AP009048 Genomic DNA Translation: BAE78081.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A24145 DEECFS

NCBI Reference Sequences

More...
RefSeqi
NP_418503.1, NC_000913.3
WP_001300547.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAD13462; AAD13462; b4079
BAE78081; BAE78081; BAE78081

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948584

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4040
eco:b4079

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.4203

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
M13563 Genomic DNA Translation: AAA23754.2
U00006 Genomic DNA Translation: AAC43173.2
U00096 Genomic DNA Translation: AAD13462.1
AP009048 Genomic DNA Translation: BAE78081.1
PIRiA24145 DEECFS
RefSeqiNP_418503.1, NC_000913.3
WP_001300547.1, 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
1AA6X-ray2.30A1-715[»]
1FDIX-ray2.90A1-715[»]
1FDOX-ray2.80A1-715[»]
2IV2X-ray2.27X1-715[»]
SMRiP07658
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4262950, 28 interactors
ComplexPortaliCPX-317 Formate hydrogenlyase-H/Hydrogenase-3 complex
DIPiDIP-9572N
IntActiP07658, 13 interactors
STRINGi511145.b4079

Chemistry databases

DrugBankiDB02345 Selenocysteine

Protein family/group databases

TCDBi3.D.1.9.2 the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family

Proteomic databases

jPOSTiP07658
PaxDbiP07658
PRIDEiP07658

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD13462; AAD13462; b4079
BAE78081; BAE78081; BAE78081
GeneIDi948584
KEGGiecj:JW4040
eco:b4079
PATRICifig|511145.12.peg.4203

Organism-specific databases

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

More...
EchoBASEi
EB0281
EcoGeneiEG10285 fdhF

Phylogenomic databases

eggNOGiENOG4107QIW Bacteria
COG0243 LUCA
HOGENOMiHOG000031440
InParanoidiP07658
KOiK22015
PhylomeDBiP07658

Enzyme and pathway databases

BioCyciEcoCyc:FORMATEDEHYDROGH-MONOMER
ECOL316407:JW4040-MONOMER
MetaCyc:FORMATEDEHYDROGH-MONOMER
BRENDAi1.1.99.33 2026
1.2.1.2 2026

Miscellaneous databases

EvolutionaryTraceiP07658

Protein Ontology

More...
PROi
PR:P07658

Family and domain databases

CDDicd02790 MopB_CT_Formate-Dh_H, 1 hit
cd02753 MopB_Formate-Dh-H, 1 hit
InterProiView protein in InterPro
IPR009010 Asp_de-COase-like_dom_sf
IPR041925 CT_Formate-Dh_H
IPR041924 Formate_Dh-H_N
IPR006478 Formate_DH_asu
IPR006657 MoPterin_dinucl-bd_dom
IPR006656 Mopterin_OxRdtase
IPR006963 Mopterin_OxRdtase_4Fe-4S_dom
IPR006655 Mopterin_OxRdtase_prok_CS
IPR027467 MopterinOxRdtase_cofactor_BS
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
TIGRFAMsiTIGR01591 Fdh-alpha, 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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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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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 nameiFDHF_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: P07658
Secondary accession number(s): P78137, Q2M6M5
<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: April 1, 1988
Last sequence update: February 26, 2008
Last modified: May 8, 2019
This is version 193 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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