ID FTR_ARCFU Reviewed; 297 AA. AC O28076; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=Formylmethanofuran--tetrahydromethanopterin formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579, ECO:0000303|PubMed:1483480}; DE Short=Ftr {ECO:0000255|HAMAP-Rule:MF_00579}; DE EC=2.3.1.101 {ECO:0000255|HAMAP-Rule:MF_00579}; DE AltName: Full=H4MPT formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579}; GN Name=ftr {ECO:0000255|HAMAP-Rule:MF_00579}; OrderedLocusNames=AF_2207; OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC OS 100126 / VC-16). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; OC Archaeoglobus. OX NCBI_TaxID=224325; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16; RX PubMed=9389475; DOI=10.1038/37052; RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F., RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., RA Smith H.O., Woese C.R., Venter J.C.; RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing RT archaeon Archaeoglobus fulgidus."; RL Nature 390:364-370(1997). RN [2] RP PROTEIN SEQUENCE OF 1-48. RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16; 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 [3] RP PROTEIN SEQUENCE OF 1-48, AND FUNCTION. RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16; RX PubMed=8481089; DOI=10.1007/bf00248476; RA Schworer B., Breitung J., Klein A.R., Stetter K.O., Thauer R.K.; RT "Formylmethanofuran: tetrahydromethanopterin formyltransferase and N5,N10- RT methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing RT Archaeoglobus fulgidus: similarities with the enzymes from methanogenic RT Archaea."; RL Arch. Microbiol. 159:225-232(1993). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=12192072; DOI=10.1110/ps.0211002; RA Mamat B., Roth A., Grimm C., Ermler U., Tziatzios C., Schubert D., RA Thauer R.K., Shima S.; RT "Crystal structures and enzymatic properties of three formyltransferases RT from archaea: environmental adaptation and evolutionary relationship."; RL Protein Sci. 11:2168-2178(2002). CC -!- FUNCTION: Catalyzes the transfer of a formyl group from 5-formyl CC tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) to CC produce formylmethanofuran (formyl-MFR) and tetrahydromethanopterin CC (H(4)MPT). {ECO:0000255|HAMAP-Rule:MF_00579, CC ECO:0000269|PubMed:8481089}. 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 -!- PATHWAY: Metabolic intermediate metabolism; lactate oxidation. CC {ECO:0000255|HAMAP-Rule:MF_00579}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00579}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00579}. CC -!- SIMILARITY: Belongs to the FTR family. {ECO:0000255|HAMAP- CC Rule:MF_00579}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000782; AAB89046.1; -; Genomic_DNA. DR PIR; G69525; G69525. DR RefSeq; WP_010879696.1; NC_000917.1. DR PDB; 1M5H; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-297. DR PDBsum; 1M5H; -. DR AlphaFoldDB; O28076; -. DR SMR; O28076; -. DR STRING; 224325.AF_2207; -. DR PaxDb; 224325-AF_2207; -. DR EnsemblBacteria; AAB89046; AAB89046; AF_2207. DR GeneID; 24795956; -. DR KEGG; afu:AF_2207; -. DR eggNOG; arCOG02695; Archaea. DR HOGENOM; CLU_081314_0_0_2; -. DR OrthoDB; 81373at2157; -. DR PhylomeDB; O28076; -. DR BioCyc; MetaCyc:AF_RS11105-MONOMER; -. DR BRENDA; 2.3.1.101; 414. DR UniPathway; UPA00701; -. DR EvolutionaryTrace; O28076; -. DR Proteomes; UP000002199; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030270; F:formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019516; P:lactate oxidation; 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 NCBIfam; TIGR03119; one_C_fhcD; 1. DR Pfam; PF01913; FTR; 1. DR Pfam; PF02741; FTR_C; 1. DR PIRSF; PIRSF006414; Ftr_formyl_trnsf; 1. DR SUPFAM; SSF55112; Formylmethanofuran:tetrahydromethanopterin formyltransferase; 2. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing; KW One-carbon metabolism; Reference proteome; Transferase. FT CHAIN 1..297 FT /note="Formylmethanofuran--tetrahydromethanopterin FT formyltransferase" FT /id="PRO_0000138115" FT CONFLICT 32 FT /note="Missing (in Ref. 2; AA sequence and 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 34 FT /note="W -> I (in Ref. 2; AA sequence and 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 43 FT /note="F -> T (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 12..26 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 30..41 FT /evidence="ECO:0007829|PDB:1M5H" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 53..60 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 71..80 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 81..95 FT /evidence="ECO:0007829|PDB:1M5H" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 103..107 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 112..115 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 117..121 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 122..125 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 130..134 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 145..153 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 155..172 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 173..188 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 229..232 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 243..253 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 254..268 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:1M5H" FT TURN 283..285 FT /evidence="ECO:0007829|PDB:1M5H" FT STRAND 288..292 FT /evidence="ECO:0007829|PDB:1M5H" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:1M5H" SQ SEQUENCE 297 AA; 31762 MW; 1466551AFFE97E4C CRC64; MKVNGVEVEE TFAEAFDIKI ARVLITGYDY YWAWVAANEA TGFGTSVIMC PAEAGIEIKA KPSETPDGRP GYYIQICHMS KKGLEEQLLA RLGQCVLTAP TTAVFNGLPD AEEKFDTGFK LKFFADGYEK EVEVGGRKCW AVPMMEGDFI IENDIGYTNG IAGGNFFIMA ETQPSALAAA KAAVDAISDV EGVITPFPGG IVASGSKVGA NKYKFLKAST NEKFAPSIRD QVEGTQIPEG VKAVYEIVIN GLNADAIKEA TRVGILAATK IPGVVKITAG NYGGKLGKHI INLNELF //