Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Formylmethanofuran--tetrahydromethanopterin formyltransferase

Gene

ftr

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processMethanogenesis, 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

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
OMAiCPAEAGI
OrthoDBiPOG093Z09PX

Family and domain databases

Gene3Di3.30.70.520, 3 hits
HAMAPiMF_00579 FTR, 1 hit
InterProiView protein in InterPro
IPR014053 ForMFR_H4MPT_ForTrfase
IPR002770 ForMFR_H4MPT_ForTrfase_C
IPR023447 ForMFR_H4MPT_ForTrfase_fd-like
IPR022667 ForMFR_H4MPT_ForTrfase_N
PfamiView protein in Pfam
PF01913 FTR, 1 hit
PF02741 FTR_C, 1 hit
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
PATRICifig|190192.8.peg.115

Similar proteinsi

Entry informationi

Entry nameiFTR_METKA
AccessioniPrimary (citable) accession number: Q49610
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 123 of the entry and version 1 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health