ID   FTR_RHOBA               Reviewed;         334 AA.
AC   Q7UKZ8;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=ffsA {ECO:0000255|HAMAP-Rule:MF_00579}; OrderedLocusNames=RB9835;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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   -!- 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; formaldehyde degradation; formate from
CC       formaldehyde (H(4)MPT route): step 4/5. {ECO:0000255|HAMAP-
CC       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, ECO:0000305}.
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DR   EMBL; BX294150; CAD76482.1; -; Genomic_DNA.
DR   RefSeq; NP_869096.1; NC_005027.1.
DR   RefSeq; WP_007334456.1; NC_005027.1.
DR   AlphaFoldDB; Q7UKZ8; -.
DR   SMR; Q7UKZ8; -.
DR   STRING; 243090.RB9835; -.
DR   PRIDE; Q7UKZ8; -.
DR   EnsemblBacteria; CAD76482; CAD76482; RB9835.
DR   KEGG; rba:RB9835; -.
DR   PATRIC; fig|243090.15.peg.4732; -.
DR   eggNOG; COG2037; Bacteria.
DR   HOGENOM; CLU_081314_0_0_0; -.
DR   InParanoid; Q7UKZ8; -.
DR   OMA; VIMCPAE; -.
DR   OrthoDB; 895502at2; -.
DR   UniPathway; UPA00562; UER00704.
DR   Proteomes; UP000001025; 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:0046294; P:formaldehyde catabolic process; 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   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; One-carbon metabolism; Reference proteome;
KW   Transferase.
FT   CHAIN           1..334
FT                   /note="Formylmethanofuran--tetrahydromethanopterin
FT                   formyltransferase"
FT                   /id="PRO_0000138125"
SQ   SEQUENCE   334 AA;  35305 MW;  E8B65036967AE5EA CRC64;
     MADPAATPKS LSIACVSIKD TFAEAFDMKA TRLIVTADDR RWCDESARAM CGFGTSVIAC
     GLEIAVEQTL SPEQTPDGRP GVAILAFGMS GKDLEKQIPR RAGQCVLTCP TTALYGGIPG
     GREVHPKRVP IGKSLRYFGD GNQISKQIQH LDADGRSRPV RYWRIPVMDG EFVCQHDVGR
     VDAIGGGNFI LVGRTMQSVT IASRAAIDAM RELPGIITPF PGGTTRSGSK VGSKYAALFA
     STNDSFCPTL REVTPSELPS EANAAIEVVI DGLSFDEIAE SMRVGITAAC EAGASEGLLS
     VSAGNYGGKL GRHHFKLHEL LADASSASDS GAER