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Q49118 (FHCD_METEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formyltransferase/hydrolase complex subunit D

Short name=Ftr complex
EC=2.3.1.101
Alternative name(s):
Formylmethanofuran--tetrahydromethanopterin formyltransferase
H4MPT formyltransferase
Gene names
Name:fhcD
Synonyms:ffsA
Ordered Locus Names:MexAM1_META1p1756
OrganismMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP]
Taxonomic identifier272630 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H4MPT) to methanofuran (MFR) and formate via the intermediate formylmethanofuran (formyl-MFR). Catalyzes the transfer of a formyl group from 5-formyl-H4MPT to MFR so as to produce tetrahydromethanopterin (H4MPT) and formyl-MFR, which is then hydrolyzed to formate and MFR. Ref.3 Ref.4

Catalytic activity

Formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin. Ref.3 Ref.4

Pathway

One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 4/5. HAMAP-Rule MF_00579

Subunit structure

Octaheteromer. Part of the formyltransferase/hydrolase complex fhc; composed of FhcA, FhcB, FhcC and FhcD. Ref.3 Ref.4

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00579.

Sequence similarities

Belongs to the FTR family.

Biophysicochemical properties

Kinetic parameters:

KM=30 µM for H4MPT Ref.3

KM=50 µM for formyl-MFR

Vmax=80 µmol/min/mg enzyme

pH dependence:

Optimum pH is 7.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processformaldehyde catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

one-carbon metabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionformylmethanofuran-tetrahydromethanopterin N-formyltransferase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 311310Formyltransferase/hydrolase complex subunit D HAMAP-Rule MF_00579
PRO_0000138124

Sequences

Sequence LengthMass (Da)Tools
Q49118 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F25FBE3918729428

FASTA31132,374
        10         20         30         40         50         60 
MSDFTLNGIK VEDTFAEAFD VAGTAIIVTN DTPKWAMIAA TVMTGFATSV IGCGAEAGID 

        70         80         90        100        110        120 
AELSPDETPD GRPGVRILLF GFEPNGLKDQ LLKRVGQCIL TCPGTACFAG VEGPTKIKLG 

       130        140        150        160        170        180 
GAIRYFGDGF AVAKRLPDHE GKMRRYWRIP VMDGEFLCED SVRAVDGAVG GGNLLFLGRK 

       190        200        210        220        230        240 
HADTLIVAEI AVEAAKAIPG AILPFPGGIV RSGSKVGGRT KGMMASTNDA YCPTLKGRAG 

       250        260        270        280        290        300 
SALPPECGVV LEIVIDALTS AAVAESMRAA LHAATEIGAQ HGLVAVTAGN YGGNLGRHHY 

       310 
HLRDLLEKPA A 

« Hide

References

« Hide 'large scale' references
[1]"C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic Archaea."
Chistoserdova L.V., Vorholt J.A., Thauer R.K., Lidstrom M.E.
Science 281:99-102(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources."
Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. expand/collapse author list , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E.
PLoS ONE 4:E5584-E5584(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14718 / DSM 1338 / AM1.
[3]"Characterization of the formyltransferase from Methylobacterium extorquens AM1."
Pomper B.K., Vorholt J.A.
Eur. J. Biochem. 268:4769-4775(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, FUNCTION AS A FORMYLTRANSFERASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[4]"Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1."
Pomper B.K., Saurel O., Milon A., Vorholt J.A.
FEBS Lett. 523:133-137(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF032114 Genomic DNA. Translation: AAC26972.1.
CP001510 Genomic DNA. Translation: ACS39600.1.
PIRT45153.
RefSeqYP_002962877.1. NC_012808.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS39600; ACS39600; MexAM1_META1p1756.
GeneID7991719.
KEGGmea:Mex_1p1756.
PATRIC22509342. VBIMetExt101010_1746.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2037.
HOGENOMHOG000230959.
KOK00672.
OMACPAEAGI.
OrthoDBEOG664CDN.
ProtClustDBPRK02114.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-4065.
MEXT272630:GBY6-1680-MONOMER.
UniPathwayUPA00562; UER00704.

Family and domain databases

Gene3D3.30.70.520. 2 hits.
HAMAPMF_00579. FTR.
InterProIPR014053. ForMFR_H4MPT_ForTrfase.
IPR002770. ForMFR_H4MPT_ForTrfase_C.
IPR023447. ForMFR_H4MPT_ForTrfase_fd-like.
IPR022667. ForMFR_H4MPT_ForTrfase_N.
[Graphical view]
PfamPF01913. FTR. 1 hit.
PF02741. FTR_C. 1 hit.
[Graphical view]
PIRSFPIRSF006414. Ftr_formyl_trnsf. 1 hit.
SUPFAMSSF55112. SSF55112. 2 hits.
TIGRFAMsTIGR03119. one_C_fhcD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFHCD_METEA
AccessionPrimary (citable) accession number: Q49118
Secondary accession number(s): C5B136
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 96 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways