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Protein

Formylmethanofuran--tetrahydromethanopterin formyltransferase

Gene

ftr

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Requires high salt concentrations for thermostability.

Pathwayi: methanogenesis from CO(2)

This protein is involved in step 2 of the subpathway that synthesizes 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Tungsten-containing formylmethanofuran dehydrogenase 2 subunit G (fwdG)
  2. Formylmethanofuran--tetrahydromethanopterin formyltransferase (ftr)
  3. Methenyltetrahydromethanopterin cyclohydrolase (mch)
This subpathway is part of the pathway methanogenesis from CO(2), which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2), the pathway methanogenesis from CO(2) and in One-carbon metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Methanogenesis, One-carbon metabolism

Enzyme and pathway databases

BRENDAi2.3.1.101. 3274.
UniPathwayiUPA00640; UER00693.

Names & Taxonomyi

Protein namesi
Recommended name:
Formylmethanofuran--tetrahydromethanopterin formyltransferase (EC:2.3.1.101)
Alternative name(s):
H4MPT formyltransferase
Gene namesi
Name:ftr
Ordered Locus Names:MK0116
OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifieri190192 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
Proteomesi
  • UP000001826 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi261R → E: Weakens dimer-dimer association. Thermolabile. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001381201 – 296Formylmethanofuran--tetrahydromethanopterin formyltransferaseAdd BLAST296

Interactioni

Subunit structurei

Homotetramer composed of two dimers. Dimerization is sufficient for enzyme activity, but tetramerization is required for high thermostability.1 Publication

Protein-protein interaction databases

STRINGi190192.MK0116.

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Beta strandi12 – 26Combined sources15
Helixi30 – 41Combined sources12
Turni47 – 49Combined sources3
Beta strandi53 – 61Combined sources9
Helixi63 – 65Combined sources3
Beta strandi72 – 81Combined sources10
Helixi82 – 96Combined sources15
Turni97 – 99Combined sources3
Beta strandi104 – 107Combined sources4
Helixi111 – 113Combined sources3
Beta strandi116 – 118Combined sources3
Helixi120 – 125Combined sources6
Helixi126 – 128Combined sources3
Beta strandi133 – 137Combined sources5
Beta strandi140 – 147Combined sources8
Beta strandi150 – 156Combined sources7
Beta strandi158 – 175Combined sources18
Helixi176 – 190Combined sources15
Helixi201 – 203Combined sources3
Beta strandi205 – 207Combined sources3
Beta strandi209 – 212Combined sources4
Beta strandi220 – 223Combined sources4
Helixi225 – 227Combined sources3
Beta strandi242 – 252Combined sources11
Helixi253 – 267Combined sources15
Beta strandi273 – 277Combined sources5
Beta strandi287 – 291Combined sources5
Helixi292 – 295Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FTRX-ray1.70A/B/C/D1-296[»]
2FHJX-ray2.00A/B/C/D1-296[»]
2FHKX-ray2.00A/B/C/D1-296[»]
ProteinModelPortaliQ49610.
SMRiQ49610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ49610.

Family & Domainsi

Sequence similaritiesi

Belongs to the FTR family.Curated

Phylogenomic databases

eggNOGiarCOG02695. Archaea.
COG2037. LUCA.
HOGENOMiHOG000230959.
KOiK00672.
OMAiSVIMCPA.

Family and domain databases

Gene3Di3.30.70.520. 2 hits.
HAMAPiMF_00579. FTR. 1 hit.
InterProiIPR014053. ForMFR_H4MPT_ForTrfase.
IPR002770. ForMFR_H4MPT_ForTrfase_C.
IPR023447. ForMFR_H4MPT_ForTrfase_fd-like.
IPR022667. ForMFR_H4MPT_ForTrfase_N.
[Graphical view]
PfamiPF01913. FTR. 1 hit.
PF02741. FTR_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006414. Ftr_formyl_trnsf. 1 hit.
SUPFAMiSSF55112. SSF55112. 2 hits.
TIGRFAMsiTIGR03119. one_C_fhcD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q49610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEINGVEIED TFAEAFEAKM ARVLITAASH KWAMIAVKEA TGFGTSVIMC
60 70 80 90 100
PAEAGIDCGY VPPEETPDGR PGVTIMIGHN DEDELKEQLL DRIGQCVMTA
110 120 130 140 150
PTASAFDAMP EAEKEDEDRV GYKLSFFGDG YQEEDELDGR KVWKIPVVEG
160 170 180 190 200
EFIVEDSFGI TTGVAGGNFY IMAESQPAGL QAAEAAVDAI KGVEGAYAPF
210 220 230 240 250
PGGIVASASK VGSKQYDFLP ASTNDAYCPT VEDNELPEGV KCVYEIVING
260 270 280 290
LNEEAVKEAM RVGIEAACQQ PGVVKISAGN FGGKLGQYEI HLHDLF
Length:296
Mass (Da):31,662
Last modified:November 1, 1996 - v1
Checksum:iDDE02D3E7D98FC86
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30H → D AA sequence (PubMed:1483480).Curated1
Sequence conflicti32W → K AA sequence (PubMed:1483480).Curated1
Sequence conflicti39E → K AA sequence (PubMed:1483480).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85115 Genomic DNA. Translation: CAA59435.1.
AE009439 Genomic DNA. Translation: AAM01333.1.
PIRiS65950. S57647.

Genome annotation databases

EnsemblBacteriaiAAM01333; AAM01333; MK0116.
KEGGimka:MK0116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85115 Genomic DNA. Translation: CAA59435.1.
AE009439 Genomic DNA. Translation: AAM01333.1.
PIRiS65950. S57647.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FTRX-ray1.70A/B/C/D1-296[»]
2FHJX-ray2.00A/B/C/D1-296[»]
2FHKX-ray2.00A/B/C/D1-296[»]
ProteinModelPortaliQ49610.
SMRiQ49610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190192.MK0116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM01333; AAM01333; MK0116.
KEGGimka:MK0116.

Phylogenomic databases

eggNOGiarCOG02695. Archaea.
COG2037. LUCA.
HOGENOMiHOG000230959.
KOiK00672.
OMAiSVIMCPA.

Enzyme and pathway databases

UniPathwayiUPA00640; UER00693.
BRENDAi2.3.1.101. 3274.

Miscellaneous databases

EvolutionaryTraceiQ49610.

Family and domain databases

Gene3Di3.30.70.520. 2 hits.
HAMAPiMF_00579. FTR. 1 hit.
InterProiIPR014053. ForMFR_H4MPT_ForTrfase.
IPR002770. ForMFR_H4MPT_ForTrfase_C.
IPR023447. ForMFR_H4MPT_ForTrfase_fd-like.
IPR022667. ForMFR_H4MPT_ForTrfase_N.
[Graphical view]
PfamiPF01913. FTR. 1 hit.
PF02741. FTR_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006414. Ftr_formyl_trnsf. 1 hit.
SUPFAMiSSF55112. SSF55112. 2 hits.
TIGRFAMsiTIGR03119. one_C_fhcD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFTR_METKA
AccessioniPrimary (citable) accession number: Q49610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 119 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.