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Protein

Sulfurtransferase FdhD

Gene

fdhD

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

Functioni

Required for formate dehydrogenase (FDH) activity (PubMed:3077634, PubMed:8522521, PubMed:22194618, PubMed:25649206). Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. Specifically interacts with IscS and stimulates its cysteine desulfurase activity. Also binds the molybdenum cofactor (PubMed:22194618, PubMed:25649206). Required for activity of formate dehydrogenase N (FDH-N), formate dehydrogenase O (FDH-O) and formate dehydrogenase H (FDH-H) (PubMed:3077634, PubMed:8522521, PubMed:22194618).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei121 – 1211Cysteine persulfide intermediateUniRule annotation1 Publication
Binding sitei240 – 2401MolybdenumUniRule annotation1 Publication

GO - Molecular functioni

  • molybdopterin cofactor binding Source: EcoCyc
  • sulfur carrier activity Source: EcoCyc
  • sulfurtransferase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11859-MONOMER.
ECOL316407:JW3866-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfurtransferase FdhDUniRule annotationCurated
Gene namesi
Name:fdhD1 PublicationUniRule annotation
Ordered Locus Names:b3895, JW3866
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11859. fdhD.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mutants lack FDH-N activity and exhibit defects in FDH-H activity.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1211C → A: Prevents sulfur transfer from IscS and impairs FDH-H activity. 1 Publication
Mutagenesisi124 – 1241C → A: Does not affect sulfur transfer from IscS, but abolishes FDH-H activity. 1 Publication
Mutagenesisi171 – 1711H → A: Does not affect overall structural integrity, but cannot promote FDH activity. 1 Publication
Mutagenesisi240 – 2401S → D: Strongly impairs FDH activity. 1 Publication
Mutagenesisi260 – 2601F → D: Strongly impairs FDH activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Sulfurtransferase FdhDPRO_0000152899Add
BLAST

Proteomic databases

PaxDbiP32177.
PRIDEiP32177.

Expressioni

Inductioni

Repressed by aerobiosis.1 Publication

Interactioni

Subunit structurei

Homodimer (PubMed:25649206). Interacts with IscS (PubMed:22194618).2 Publications

Protein-protein interaction databases

BioGridi4263324. 13 interactions.
DIPiDIP-9570N.
IntActiP32177. 19 interactions.
MINTiMINT-1228712.
STRINGi511145.b3895.

Structurei

Secondary structure

1
277
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 236Combined sources
Beta strandi29 – 313Combined sources
Beta strandi33 – 386Combined sources
Beta strandi41 – 477Combined sources
Beta strandi50 – 578Combined sources
Helixi62 – 7211Combined sources
Helixi79 – 813Combined sources
Beta strandi82 – 898Combined sources
Beta strandi91 – 10010Combined sources
Helixi102 – 1109Combined sources
Helixi147 – 1493Combined sources
Helixi150 – 1567Combined sources
Helixi157 – 1604Combined sources
Helixi162 – 1676Combined sources
Beta strandi171 – 1766Combined sources
Beta strandi182 – 1909Combined sources
Helixi191 – 20414Combined sources
Turni206 – 2083Combined sources
Beta strandi209 – 21810Combined sources
Helixi222 – 2309Combined sources
Beta strandi235 – 2406Combined sources
Helixi244 – 2518Combined sources
Turni252 – 2543Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi265 – 2684Combined sources
Helixi272 – 2743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PDEX-ray2.80A1-277[»]
ProteinModelPortaliP32177.
SMRiP32177. Positions 15-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni260 – 2656Molybdenum bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the FdhD family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4107H9G. Bacteria.
COG1526. LUCA.
HOGENOMiHOG000079468.
InParanoidiP32177.
KOiK02379.
OMAiPFTQTFS.
OrthoDBiEOG6DG2R8.
PhylomeDBiP32177.

Family and domain databases

HAMAPiMF_00187. FdhD.
InterProiIPR016193. Cytidine_deaminase-like.
IPR003786. FdhD.
[Graphical view]
PfamiPF02634. FdhD-NarQ. 1 hit.
[Graphical view]
PIRSFiPIRSF015626. FdhD. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00129. fdhD_narQ. 1 hit.

Sequencei

Sequence statusi: Complete.

P32177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTQRKEIE NVTNITGVRQ IELWRRDDLQ HPRLDEVAEE VPVALVYNGI
60 70 80 90 100
SHVVMMASPK DLEYFALGFS LSEGIIESPR DIFGMDVVPS CNGLEVQIEL
110 120 130 140 150
SSRRFMGLKE RRRALAGRTG CGVCGVEQLN DIGKPVQPLP FTQTFDLNKL
160 170 180 190 200
DDALRHLNDF QPVGQLTGCT HAAAWMLPSG ELVGGHEDVG RHVALDKLLG
210 220 230 240 250
RRSQEGESWQ QGAVLVSSRA SYEMVQKSAM CGVEILFAVS AATTLAVEVA
260 270
ERCNLTLVGF CKPGRATVYT HPQRLSN
Length:277
Mass (Da):30,560
Last modified:October 1, 1993 - v1
Checksum:i9E42BBDCB5B3D0F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03028.1.
U00096 Genomic DNA. Translation: AAC76877.1.
AP009048 Genomic DNA. Translation: BAE77414.1.
PIRiS40839.
RefSeqiNP_418331.1. NC_000913.3.
WP_000753617.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76877; AAC76877; b3895.
BAE77414; BAE77414; BAE77414.
GeneIDi948393.
KEGGiecj:JW3866.
eco:b3895.
PATRICi32123299. VBIEscCol129921_4010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03028.1.
U00096 Genomic DNA. Translation: AAC76877.1.
AP009048 Genomic DNA. Translation: BAE77414.1.
PIRiS40839.
RefSeqiNP_418331.1. NC_000913.3.
WP_000753617.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PDEX-ray2.80A1-277[»]
ProteinModelPortaliP32177.
SMRiP32177. Positions 15-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263324. 13 interactions.
DIPiDIP-9570N.
IntActiP32177. 19 interactions.
MINTiMINT-1228712.
STRINGi511145.b3895.

Proteomic databases

PaxDbiP32177.
PRIDEiP32177.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76877; AAC76877; b3895.
BAE77414; BAE77414; BAE77414.
GeneIDi948393.
KEGGiecj:JW3866.
eco:b3895.
PATRICi32123299. VBIEscCol129921_4010.

Organism-specific databases

EchoBASEiEB1805.
EcoGeneiEG11859. fdhD.

Phylogenomic databases

eggNOGiENOG4107H9G. Bacteria.
COG1526. LUCA.
HOGENOMiHOG000079468.
InParanoidiP32177.
KOiK02379.
OMAiPFTQTFS.
OrthoDBiEOG6DG2R8.
PhylomeDBiP32177.

Enzyme and pathway databases

BioCyciEcoCyc:EG11859-MONOMER.
ECOL316407:JW3866-MONOMER.

Miscellaneous databases

PROiP32177.

Family and domain databases

HAMAPiMF_00187. FdhD.
InterProiIPR016193. Cytidine_deaminase-like.
IPR003786. FdhD.
[Graphical view]
PfamiPF02634. FdhD-NarQ. 1 hit.
[Graphical view]
PIRSFiPIRSF015626. FdhD. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00129. fdhD_narQ. 1 hit.
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. "Mutants of Escherichia coli specifically deficient in respiratory formate dehydrogenase activity."
    Mandrand-Berthelot M.A., Couchoux-Luthaud G., Santini C.L., Giordano G.
    J. Gen. Microbiol. 134:3129-3139(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12.
  5. "Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase."
    Schlindwein C., Giordano G., Santini C.L., Mandrand M.A.
    J. Bacteriol. 172:6112-6121(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, SUBCELLULAR LOCATION.
    Strain: K12.
  6. "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: FUNCTION.
  7. "A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli."
    Thome R., Gust A., Toci R., Mendel R., Bittner F., Magalon A., Walburger A.
    J. Biol. Chem. 287:4671-4678(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ISCS, ACTIVE SITE, MUTAGENESIS OF CYS-121 AND CYS-124.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GDP, FUNCTION, SUBUNIT, MOLYBDENUM-BINDING, MUTAGENESIS OF HIS-171; SER-240 AND PHE-260.

Entry informationi

Entry nameiFDHD_ECOLI
AccessioniPrimary (citable) accession number: P32177
Secondary accession number(s): Q2M8J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 6, 2016
This is version 125 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

3D-structure, Complete proteome, 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.