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O28076 (FTR_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Formylmethanofuran--tetrahydromethanopterin formyltransferase

EC=2.3.1.101
Alternative name(s):
H4MPT formyltransferase
Gene names
Name:ftr
Ordered Locus Names:AF_2207
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a formyl group from 5-formyl tetrahydromethanopterin (5-formyl-H4MPT) to methanofuran (MFR) so as to produce formylmethanofuran (formyl-MFR) and tetrahydromethanopterin (H4MPT). Ref.3

Catalytic activity

Formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin. HAMAP-Rule MF_00579

Pathway

Metabolic intermediate metabolism; lactate oxidation. HAMAP-Rule MF_00579

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00579.

Sequence similarities

Belongs to the FTR family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processlactate oxidation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

one-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionformylmethanofuran-tetrahydromethanopterin N-formyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Formylmethanofuran--tetrahydromethanopterin formyltransferase HAMAP-Rule MF_00579
PRO_0000138115

Experimental info

Sequence conflict321Missing AA sequence Ref.2
Sequence conflict321Missing AA sequence Ref.3
Sequence conflict341W → I AA sequence Ref.2
Sequence conflict341W → I AA sequence Ref.3
Sequence conflict431F → T AA sequence Ref.3

Secondary structure

...................................................... 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O28076 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1466551AFFE97E4C

FASTA29731,762
        10         20         30         40         50         60 
MKVNGVEVEE TFAEAFDIKI ARVLITGYDY YWAWVAANEA TGFGTSVIMC PAEAGIEIKA 

        70         80         90        100        110        120 
KPSETPDGRP GYYIQICHMS KKGLEEQLLA RLGQCVLTAP TTAVFNGLPD AEEKFDTGFK 

       130        140        150        160        170        180 
LKFFADGYEK EVEVGGRKCW AVPMMEGDFI IENDIGYTNG IAGGNFFIMA ETQPSALAAA 

       190        200        210        220        230        240 
KAAVDAISDV EGVITPFPGG IVASGSKVGA NKYKFLKAST NEKFAPSIRD QVEGTQIPEG 

       250        260        270        280        290 
VKAVYEIVIN GLNADAIKEA TRVGILAATK IPGVVKITAG NYGGKLGKHI INLNELF 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. expand/collapse author list , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]"Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri."
Breitung J., Borner G., Scholz S., Linder D., Stetter K.O., Thauer R.K.
Eur. J. Biochem. 210:971-981(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-48.
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[3]"Formylmethanofuran: tetrahydromethanopterin formyltransferase and N5,N10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea."
Schworer B., Breitung J., Klein A.R., Stetter K.O., Thauer R.K.
Arch. Microbiol. 159:225-232(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-48, FUNCTION.
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[4]"Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship."
Mamat B., Roth A., Grimm C., Ermler U., Tziatzios C., Schubert D., Thauer R.K., Shima S.
Protein Sci. 11:2168-2178(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB89046.1.
PIRG69525.
RefSeqNP_071032.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5HX-ray2.00A/B/C/D/E/F/G/H1-297[»]
ProteinModelPortalO28076.
SMRO28076. Positions 1-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF2207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB89046; AAB89046; AF_2207.
GeneID1485436.
KEGGafu:AF2207.

Phylogenomic databases

eggNOGCOG2037.
KOK00672.
OMACPAEAGI.
ProtClustDBPRK02114.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-2252-MONOMER.
UniPathwayUPA00701.

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...

Other

EvolutionaryTraceO28076.

Entry information

Entry nameFTR_ARCFU
AccessionPrimary (citable) accession number: O28076
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 97 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways