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Protein

Formate dehydrogenase-O iron-sulfur subunit

Gene

fdoH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit (By similarity).By similarity

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 4 [4Fe-4S] clusters per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi42 – 421Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi45 – 451Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi49 – 491Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi100 – 1001Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi103 – 1031Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi108 – 1081Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi112 – 1121Iron-sulfur 4 (4Fe-4S)By similarity
Metal bindingi133 – 1331Iron-sulfur 4 (4Fe-4S)By similarity
Metal bindingi136 – 1361Iron-sulfur 4 (4Fe-4S)By similarity
Metal bindingi139 – 1391Iron-sulfur 4 (4Fe-4S)By similarity
Metal bindingi143 – 1431Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi160 – 1601Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi175 – 1751Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi179 – 1791Iron-sulfur 1 (4Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

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

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciEcoCyc:FDOH-MONOMER.
ECOL316407:JW3864-MONOMER.
MetaCyc:FDOH-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenase-O iron-sulfur subunit
Alternative name(s):
Aerobic formate dehydrogenase iron-sulfur subunit
FDH-Z subunit beta
Formate dehydrogenase-O subunit beta
Gene namesi
Name:fdoH
Ordered Locus Names:b3893, JW3864
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11857. fdoH.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 260260Cytoplasmic1 PublicationAdd
BLAST
Transmembranei261 – 27919HelicalCuratedAdd
BLAST
Topological domaini280 – 30021Periplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • formate dehydrogenase complex Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW
  • intrinsic component of the cytoplasmic side of the plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 300300Formate dehydrogenase-O iron-sulfur subunitPRO_0000159249Add
BLAST

Proteomic databases

EPDiP0AAJ5.
PaxDbiP0AAJ5.
PRIDEiP0AAJ5.

Interactioni

Subunit structurei

Formate dehydrogenase is a membrane-bound complex, formed by subunits alpha, beta and gamma.

Protein-protein interaction databases

BioGridi4263325. 18 interactions.
IntActiP0AAJ5. 4 interactions.
STRINGi511145.b3893.

Structurei

3D structure databases

ProteinModelPortaliP0AAJ5.
SMRiP0AAJ5. Positions 2-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 60314Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini91 – 123334Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini124 – 153304Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 189324Fe-4S ferredoxin-type 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105QA4. Bacteria.
COG0437. LUCA.
HOGENOMiHOG000163382.
InParanoidiP0AAJ5.
KOiK00124.
OMAiISATVKF.
OrthoDBiEOG6XSZQF.
PhylomeDBiP0AAJ5.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR006470. Formate_DH_bsu_Proteobacteria.
IPR014603. Formate_DH_Fe-S_su.
IPR015246. Formate_DH_TM.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
PF09163. Form-deh_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF036298. FDH_4Fe4S. 1 hit.
TIGRFAMsiTIGR01582. FDH-beta. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AAJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYQSQDIIR RSATNGLTPA PQARDFQEEV AKLIDVTTCI GCKACQVACS
60 70 80 90 100
EWNDIRDTVG NNIGVYDNPN DLSAKSWTVM RFSEVEQNDK LEWLIRKDGC
110 120 130 140 150
MHCSDPGCLK ACPAEGAIIQ YANGIVDFQS EQCIGCGYCI AGCPFDIPRL
160 170 180 190 200
NPEDNRVYKC TLCVDRVVVG QEPACVKTCP TGAIHFGTKE SMKTLASERV
210 220 230 240 250
AELKTRGYDN AGLYDPAGVG GTHVMYVLHH ADKPNLYHGL PENPEISETV
260 270 280 290 300
KFWKGIWKPL AAVGFAATFA ASIFHYVGVG PNRADEEENN LHEEKDEERK
Length:300
Mass (Da):33,100
Last modified:October 11, 2005 - v1
Checksum:i950B40FE1A6016E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03026.1.
U00096 Genomic DNA. Translation: AAD13455.1.
AP009048 Genomic DNA. Translation: BAE77416.1.
PIRiS40837.
RefSeqiNP_418329.1. NC_000913.3.
WP_000331377.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAD13455; AAD13455; b3893.
BAE77416; BAE77416; BAE77416.
GeneIDi948395.
KEGGiecj:JW3864.
eco:b3893.
PATRICi32123293. VBIEscCol129921_4007.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03026.1.
U00096 Genomic DNA. Translation: AAD13455.1.
AP009048 Genomic DNA. Translation: BAE77416.1.
PIRiS40837.
RefSeqiNP_418329.1. NC_000913.3.
WP_000331377.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AAJ5.
SMRiP0AAJ5. Positions 2-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263325. 18 interactions.
IntActiP0AAJ5. 4 interactions.
STRINGi511145.b3893.

Proteomic databases

EPDiP0AAJ5.
PaxDbiP0AAJ5.
PRIDEiP0AAJ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD13455; AAD13455; b3893.
BAE77416; BAE77416; BAE77416.
GeneIDi948395.
KEGGiecj:JW3864.
eco:b3893.
PATRICi32123293. VBIEscCol129921_4007.

Organism-specific databases

EchoBASEiEB1803.
EcoGeneiEG11857. fdoH.

Phylogenomic databases

eggNOGiENOG4105QA4. Bacteria.
COG0437. LUCA.
HOGENOMiHOG000163382.
InParanoidiP0AAJ5.
KOiK00124.
OMAiISATVKF.
OrthoDBiEOG6XSZQF.
PhylomeDBiP0AAJ5.

Enzyme and pathway databases

BioCyciEcoCyc:FDOH-MONOMER.
ECOL316407:JW3864-MONOMER.
MetaCyc:FDOH-MONOMER.

Miscellaneous databases

PROiP0AAJ5.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR006470. Formate_DH_bsu_Proteobacteria.
IPR014603. Formate_DH_Fe-S_su.
IPR015246. Formate_DH_TM.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
PF09163. Form-deh_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF036298. FDH_4Fe4S. 1 hit.
TIGRFAMsiTIGR01582. FDH-beta. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase."
    Abaibou H., Pommier J., Giordano G., Mandrand-Berthelot M.-A.
    J. Bacteriol. 177:7141-7149(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: K12.
  5. "Topological analysis of the aerobic membrane-bound formate dehydrogenase of Escherichia coli."
    Benoit S., Abaibou H., Mandrand-Berthelot M.-A.
    J. Bacteriol. 180:6625-6634(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.

Entry informationi

Entry nameiFDOH_ECOLI
AccessioniPrimary (citable) accession number: P0AAJ5
Secondary accession number(s): P32175, Q2M8J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.