FTR_ARCFU
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 03-AUG-2022, entry version 134.
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}.
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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 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 OMA; VIMCPAE; -.
DR OrthoDB; 62652at2157; -.
DR PhylomeDB; O28076; -.
DR BioCyc; MetaCyc:AF_RS11105-MON; -.
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 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 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
