FTR_METBF
ID FTR_METBF Reviewed; 297 AA.
AC P55301; Q46DU0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Formylmethanofuran--tetrahydromethanopterin formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579};
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=Mbar_A0980;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8593103; DOI=10.1007/s002030050303;
RA Kunow J., Shima S., Vorholt J.A., Thauer R.K.;
RT "Primary structure and properties of the formyltransferase from the
RT mesophilic Methanosarcina barkeri: comparison with the enzymes from
RT thermophilic and hyperthermophilic methanogens.";
RL Arch. Microbiol. 165:97-105(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [3]
RP PROTEIN SEQUENCE OF 1-26.
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 X-RAY CRYSTALLOGRAPHY (1.85 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 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). {ECO:0000255|HAMAP-Rule:MF_00579}.
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: 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}.
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; X91143; CAA62582.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ69952.1; -; Genomic_DNA.
DR RefSeq; WP_011306001.1; NC_007355.1.
DR PDB; 1M5S; X-ray; 1.85 A; A/B/C/D=1-297.
DR PDBsum; 1M5S; -.
DR AlphaFoldDB; P55301; -.
DR SMR; P55301; -.
DR STRING; 269797.Mbar_A0980; -.
DR EnsemblBacteria; AAZ69952; AAZ69952; Mbar_A0980.
DR GeneID; 3625752; -.
DR KEGG; mba:Mbar_A0980; -.
DR eggNOG; arCOG02695; Archaea.
DR HOGENOM; CLU_081314_0_0_2; -.
DR OMA; VIMCPAE; -.
DR OrthoDB; 62652at2157; -.
DR BRENDA; 2.3.1.101; 3250.
DR UniPathway; UPA00640; UER00693.
DR EvolutionaryTrace; P55301; -.
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: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; Transferase.
FT CHAIN 1..297
FT /note="Formylmethanofuran--tetrahydromethanopterin
FT formyltransferase"
FT /id="PRO_0000138117"
FT CONFLICT 22..26
FT /note="RVLIT -> VIIAA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 12..26
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:1M5S"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1M5S"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:1M5S"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 155..172
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 254..268
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1M5S"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1M5S"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:1M5S"
SQ SEQUENCE 297 AA; 31697 MW; 1D584BA3006FD802 CRC64;
MEINGVEIED TYAEAFPIKI ARVLITAATK RWALVAATEA TGFATSVIMC PAEAGIERLA
SPSETPDGRP GVYVQICTFK YEALEEQLLE RIGQCVLTAP TTAVFNGLPE AEKQFNVGFK
LKFFADGMES ETQIAGRKVY KVPIMEGDFL AEENIGAIAG IAGGNFFIFG DSQMTALTAA
EAAVDTIAEL EGTITPFPGG IVASGSKSGA NKYKFLKATA NERFCPSIKD KIENTEIPAD
VNAVYEIVIN GLDEESIKAA MKAGIKAAVT VPGVKKISAG NYGGKLGKYQ FKLHELF
