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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-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Formate + NAD+ = CO2 + NADH.
Formate + acceptor = CO2 + reduced acceptor.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by aerobic conditions.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Active sitei44Electron donor/acceptor1
Binding sitei44Molybdopterin guanine dinucleotide 22 Publications1
Active sitei140Proton donor/acceptor1
Metal bindingi140Molybdenum1
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

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron carrier activity Source: InterPro
  • formate dehydrogenase (NAD+) activity Source: UniProtKB-EC
  • molybdenum ion binding Source: EcoCyc

GO - Biological processi

  • formate oxidation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

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

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenase H (EC:1.1.99.33, EC:1.2.1.2)
Alternative name(s):
Formate dehydrogenase-H subunit alpha
Short name:
FDH-H
Formate-hydrogen-lyase-linked, selenocysteine-containing polypeptide
Gene namesi
Name:fdhF
Ordered Locus Names:b4079, JW4040
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10285. fdhF.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000632211 – 715Formate dehydrogenase HAdd BLAST715

Proteomic databases

PaxDbiP07658.
PRIDEiP07658.

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Consists of two separable enzymatic activities: a formate dehydrogenase component (FDH-H) and hydrogenase-3.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi4262950. 9 interactors.
DIPiDIP-9572N.
IntActiP07658. 13 interactors.
STRINGi511145.b4079.

Structurei

Secondary structure

1715
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Beta strandi9 – 11Combined sources3
Beta strandi16 – 22Combined sources7
Beta strandi25 – 31Combined sources7
Turni35 – 39Combined sources5
Helixi43 – 47Combined sources5
Helixi50 – 53Combined sources4
Beta strandi57 – 59Combined sources3
Beta strandi69 – 72Combined sources4
Helixi80 – 98Combined sources19
Helixi100 – 102Combined sources3
Beta strandi103 – 106Combined sources4
Helixi114 – 126Combined sources13
Helixi137 – 140Combined sources4
Beta strandi143 – 145Combined sources3
Helixi148 – 152Combined sources5
Helixi161 – 166Combined sources6
Beta strandi168 – 174Combined sources7
Helixi177 – 180Combined sources4
Helixi182 – 193Combined sources12
Beta strandi197 – 201Combined sources5
Helixi207 – 210Combined sources4
Beta strandi213 – 216Combined sources4
Helixi223 – 236Combined sources14
Helixi242 – 248Combined sources7
Helixi252 – 260Combined sources9
Helixi265 – 267Combined sources3
Helixi268 – 271Combined sources4
Helixi275 – 287Combined sources13
Beta strandi288 – 296Combined sources9
Helixi299 – 301Combined sources3
Beta strandi302 – 304Combined sources3
Helixi305 – 318Combined sources14
Beta strandi322 – 324Combined sources3
Beta strandi328 – 332Combined sources5
Helixi338 – 343Combined sources6
Helixi352 – 354Combined sources3
Helixi360 – 369Combined sources10
Helixi383 – 385Combined sources3
Helixi386 – 391Combined sources6
Beta strandi397 – 402Combined sources6
Helixi405 – 408Combined sources4
Beta strandi409 – 411Combined sources3
Helixi412 – 421Combined sources10
Beta strandi422 – 431Combined sources10
Helixi434 – 437Combined sources4
Beta strandi440 – 445Combined sources6
Helixi448 – 450Combined sources3
Beta strandi453 – 456Combined sources4
Beta strandi460 – 465Combined sources6
Beta strandi472 – 474Combined sources3
Helixi478 – 488Combined sources11
Helixi498 – 508Combined sources11
Turni510 – 514Combined sources5
Helixi517 – 520Combined sources4
Turni521 – 523Combined sources3
Beta strandi526 – 528Combined sources3
Beta strandi541 – 543Combined sources3
Beta strandi553 – 556Combined sources4
Beta strandi571 – 573Combined sources3
Beta strandi575 – 579Combined sources5
Beta strandi583 – 585Combined sources3
Helixi592 – 594Combined sources3
Helixi596 – 599Combined sources4
Beta strandi607 – 611Combined sources5
Helixi612 – 618Combined sources7
Beta strandi625 – 629Combined sources5
Beta strandi634 – 645Combined sources12
Beta strandi649 – 652Combined sources4
Beta strandi657 – 659Combined sources3
Helixi661 – 663Combined sources3
Turni671 – 673Combined sources3
Beta strandi681 – 687Combined sources7
Helixi691 – 713Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AA6X-ray2.30A1-715[»]
1FDIX-ray2.90A1-715[»]
1FDOX-ray2.80A1-715[»]
2IV2X-ray2.27X1-715[»]
ProteinModelPortaliP07658.
SMRiP07658.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07658.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 564Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST56

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Sequence similaritiesi

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107QIW. Bacteria.
COG0243. LUCA.
HOGENOMiHOG000031440.
InParanoidiP07658.
KOiK00123.
OMAiWGVTLQP.
PhylomeDBiP07658.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
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.
[Graphical view]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01591. Fdh-alpha. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
[Graphical view]

Sequencei

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
Checksum:iC7C86F6F704A142D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19L → V in AAA23754 (PubMed:2941757).Curated1

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei140Selenocysteine1 Publication1

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.

Genome annotation databases

EnsemblBacteriaiAAD13462; AAD13462; b4079.
BAE78081; BAE78081; BAE78081.
GeneIDi948584.
KEGGiecj:JW4040.
eco:b4079.
PATRICi32123709. VBIEscCol129921_4203.

Keywords - Coding sequence diversityi

Selenocysteine

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AA6X-ray2.30A1-715[»]
1FDIX-ray2.90A1-715[»]
1FDOX-ray2.80A1-715[»]
2IV2X-ray2.27X1-715[»]
ProteinModelPortaliP07658.
SMRiP07658.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262950. 9 interactors.
DIPiDIP-9572N.
IntActiP07658. 13 interactors.
STRINGi511145.b4079.

Protein family/group databases

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

Proteomic databases

PaxDbiP07658.
PRIDEiP07658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD13462; AAD13462; b4079.
BAE78081; BAE78081; BAE78081.
GeneIDi948584.
KEGGiecj:JW4040.
eco:b4079.
PATRICi32123709. VBIEscCol129921_4203.

Organism-specific databases

EchoBASEiEB0281.
EcoGeneiEG10285. fdhF.

Phylogenomic databases

eggNOGiENOG4107QIW. Bacteria.
COG0243. LUCA.
HOGENOMiHOG000031440.
InParanoidiP07658.
KOiK00123.
OMAiWGVTLQP.
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.
PROiP07658.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
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.
[Graphical view]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01591. Fdh-alpha. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFDHF_ECOLI
AccessioniPrimary (citable) accession number: P07658
Secondary accession number(s): P78137, Q2M6M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 26, 2008
Last modified: November 2, 2016
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.