FTR_METKA
ID FTR_METKA Reviewed; 296 AA.
AC Q49610;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Formylmethanofuran--tetrahydromethanopterin formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579};
DE Short=Ftr {ECO:0000255|HAMAP-Rule:MF_00579, ECO:0000303|PubMed:7601152};
DE EC=2.3.1.101 {ECO:0000255|HAMAP-Rule:MF_00579, ECO:0000269|PubMed:1483480};
DE AltName: Full=H4MPT formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579};
GN Name=ftr {ECO:0000255|HAMAP-Rule:MF_00579, ECO:0000303|PubMed:7601152};
GN OrderedLocusNames=MK0116;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=7601152; DOI=10.1111/j.1432-1033.1995.tb20635.x;
RA Shima S., Weiss D.S., Thauer R.K.;
RT "Formylmethanofuran:tetrahydromethanopterin formyltransferase (Ftr) from
RT the hyperthermophilic Methanopyrus kandleri. Cloning, sequencing and
RT functional expression of the ftr gene and one-step purification of the
RT enzyme overproduced in Escherichia coli.";
RL Eur. J. Biochem. 230:906-913(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN [3]
RP PROTEIN SEQUENCE OF 1-49, FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=1483480; DOI=10.1111/j.1432-1033.1992.tb17502.x;
RA Breitung J., Borner G., Scholz S., Linder D., Stetter K.O., Thauer R.K.;
RT "Salt dependence, kinetic properties and catalytic mechanism of N-
RT formylmethanofuran:tetrahydromethanopterin formyltransferase from the
RT extreme thermophile Methanopyrus kandleri.";
RL Eur. J. Biochem. 210:971-981(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-261.
RX PubMed=11054114; DOI=10.1046/j.1432-1327.2000.01756.x;
RA Shima S., Thauer R.K., Ermler U., Durchschlag H., Tziatzios C.,
RA Schubert D.;
RT "A mutation affecting the association equilibrium of formyltransferase from
RT the hyperthermophilic Methanopyrus kandleri and its influence on the
RT enzyme's activity and thermostability.";
RL Eur. J. Biochem. 267:6619-6623(2000).
RN [5] {ECO:0007744|PDB:1FTR}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
RX PubMed=9195883; DOI=10.1016/s0969-2126(97)00219-0;
RA Ermler U., Merckel M., Thauer R., Shima S.;
RT "Formylmethanofuran: tetrahydromethanopterin formyltransferase from
RT Methanopyrus kandleri -- new insights into salt-dependence and
RT thermostability.";
RL Structure 5:635-646(1997).
CC -!- FUNCTION: Catalyzes the reversible transfer of a formyl group from
CC formylmethanofuran (formyl-MFR) to tetrahydromethanopterin (H(4)MPT) to
CC produce 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) and
CC methanofuran (MFR) (By similarity) (PubMed:11054114, PubMed:1483480,
CC PubMed:7601152). Acts via a ternary-complex mechanism. Uses N-
CC furfurylformamide much less efficiently, does not use N-methylformamide
CC or formamide (PubMed:1483480, PubMed:11054114, PubMed:7601152). Protein
CC overexpressed in E.coli has very similar properties to enzyme purified
CC from M.kandleri (PubMed:7601152). {ECO:0000255|HAMAP-Rule:MF_00579,
CC ECO:0000269|PubMed:11054114, ECO:0000269|PubMed:1483480,
CC ECO:0000269|PubMed:7601152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydromethanopterin + H(+) + N-formylmethanofuran
CC = methanofuran + N(5)-formyl-5,6,7,8-tetrahydromethanopterin;
CC Xref=Rhea:RHEA:18061, ChEBI:CHEBI:15378, ChEBI:CHEBI:57727,
CC ChEBI:CHEBI:58018, ChEBI:CHEBI:58103, ChEBI:CHEBI:58151;
CC EC=2.3.1.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00579,
CC ECO:0000269|PubMed:11054114, ECO:0000269|PubMed:1483480,
CC ECO:0000269|PubMed:7601152};
CC -!- ACTIVITY REGULATION: Requires high salt concentrations for activity and
CC thermostability; 1.5-1.8 M KH(2)PO(4) stimulates activity while
CC stabilizing the enzyme. {ECO:0000269|PubMed:1483480}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for N-formylmethanofuran {ECO:0000269|PubMed:1483480};
CC KM=100 uM for 5,6,7,8-tetrahydromethanopterin
CC {ECO:0000269|PubMed:1483480};
CC KM=20 mM for N-furfurylformamide {ECO:0000269|PubMed:1483480};
CC Vmax=2700 umol/min/mg enzyme reaction of N-formylmethanofuran and
CC 5,6,7,8-tetrahydromethanopterin {ECO:0000269|PubMed:1483480};
CC Vmax=68 umol/min/mg enzyme reaction of N-furfurylformamide
CC {ECO:0000269|PubMed:1483480};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:1483480};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius.
CC {ECO:0000269|PubMed:1483480};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10-
CC methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 2/3.
CC {ECO:0000255|HAMAP-Rule:MF_00579, ECO:0000305|PubMed:1483480}.
CC -!- SUBUNIT: Homotetramer composed of two dimers (PubMed:11054114,
CC PubMed:9195883). Dimerization is sufficient for enzyme activity, but
CC tetramerization is required for high thermostability (PubMed:11054114).
CC {ECO:0000269|PubMed:11054114, ECO:0000269|PubMed:9195883}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00579,
CC ECO:0000305|PubMed:1483480}.
CC -!- SIMILARITY: Belongs to the FTR family. {ECO:0000255|HAMAP-
CC Rule:MF_00579}.
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DR EMBL; X85115; CAA59435.1; -; Genomic_DNA.
DR EMBL; AE009439; AAM01333.1; -; Genomic_DNA.
DR PIR; S65950; S57647.
DR PDB; 1FTR; X-ray; 1.70 A; A/B/C/D=1-296.
DR PDB; 2FHJ; X-ray; 2.00 A; A/B/C/D=1-296.
DR PDB; 2FHK; X-ray; 2.00 A; A/B/C/D=1-296.
DR PDBsum; 1FTR; -.
DR PDBsum; 2FHJ; -.
DR PDBsum; 2FHK; -.
DR AlphaFoldDB; Q49610; -.
DR SMR; Q49610; -.
DR STRING; 190192.MK0116; -.
DR EnsemblBacteria; AAM01333; AAM01333; MK0116.
DR KEGG; mka:MK0116; -.
DR PATRIC; fig|190192.8.peg.115; -.
DR HOGENOM; CLU_081314_0_0_2; -.
DR OMA; VIMCPAE; -.
DR BRENDA; 2.3.1.101; 3274.
DR UniPathway; UPA00640; UER00693.
DR EvolutionaryTrace; Q49610; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030270; F:formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity; IDA:MENGO.
DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.520; -; 2.
DR HAMAP; MF_00579; FTR; 1.
DR InterPro; IPR014053; ForMFR_H4MPT_ForTrfase.
DR InterPro; IPR002770; ForMFR_H4MPT_ForTrfase_C.
DR InterPro; IPR023447; ForMFR_H4MPT_ForTrfase_fd-like.
DR InterPro; IPR022667; ForMFR_H4MPT_ForTrfase_N.
DR Pfam; PF01913; FTR; 1.
DR Pfam; PF02741; FTR_C; 1.
DR PIRSF; PIRSF006414; Ftr_formyl_trnsf; 1.
DR SUPFAM; SSF55112; SSF55112; 2.
DR TIGRFAMs; TIGR03119; one_C_fhcD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Methanogenesis; One-carbon metabolism; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Formylmethanofuran--tetrahydromethanopterin
FT formyltransferase"
FT /id="PRO_0000138120"
FT MUTAGEN 261
FT /note="R->E: Weakens dimer-dimer association.
FT Thermolabile."
FT /evidence="ECO:0000269|PubMed:11054114"
FT CONFLICT 30
FT /note="H -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="W -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="E -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 12..26
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:1FTR"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:1FTR"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 158..175
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 253..267
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:1FTR"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1FTR"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:1FTR"
SQ SEQUENCE 296 AA; 31662 MW; DDE02D3E7D98FC86 CRC64;
MEINGVEIED TFAEAFEAKM ARVLITAASH KWAMIAVKEA TGFGTSVIMC PAEAGIDCGY
VPPEETPDGR PGVTIMIGHN DEDELKEQLL DRIGQCVMTA PTASAFDAMP EAEKEDEDRV
GYKLSFFGDG YQEEDELDGR KVWKIPVVEG EFIVEDSFGI TTGVAGGNFY IMAESQPAGL
QAAEAAVDAI KGVEGAYAPF PGGIVASASK VGSKQYDFLP ASTNDAYCPT VEDNELPEGV
KCVYEIVING LNEEAVKEAM RVGIEAACQQ PGVVKISAGN FGGKLGQYEI HLHDLF
