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Database: UniProt
Entry: F9UBR5_9GAMM
LinkDB: F9UBR5_9GAMM
Original site: F9UBR5_9GAMM 
ID   F9UBR5_9GAMM            Unreviewed;       321 AA.
AC   F9UBR5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00016014, ECO:0000256|HAMAP-Rule:MF_00182};
DE            EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261, ECO:0000256|HAMAP-Rule:MF_00182};
GN   Name=fmt {ECO:0000256|HAMAP-Rule:MF_00182};
GN   ORFNames=ThimaDRAFT_2367 {ECO:0000313|EMBL:EGV18383.1};
OS   Thiocapsa marina 5811.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocapsa.
OX   NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV18383.1, ECO:0000313|Proteomes:UP000005459};
RN   [1] {ECO:0000313|EMBL:EGV18383.1, ECO:0000313|Proteomes:UP000005459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5811 {ECO:0000313|EMBL:EGV18383.1,
RC   ECO:0000313|Proteomes:UP000005459};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA   Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA   Bryant D., Woyke T.J.;
RT   "The draft genome of Thiocapsa marina 5811.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Attaches a formyl group to the free amino group of methionyl-
CC       tRNA(fMet). The formyl group appears to play a dual role in the
CC       initiator identity of N-formylmethionyl-tRNA by promoting its
CC       recognition by IF2 and preventing the misappropriation of this tRNA by
CC       the elongation apparatus. {ECO:0000256|ARBA:ARBA00002606,
CC       ECO:0000256|HAMAP-Rule:MF_00182}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC         (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC         tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-
CC         COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; EC=2.1.2.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00036072, ECO:0000256|HAMAP-
CC         Rule:MF_00182};
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|ARBA:ARBA00010699,
CC       ECO:0000256|HAMAP-Rule:MF_00182}.
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DR   EMBL; AFWV01000007; EGV18383.1; -; Genomic_DNA.
DR   RefSeq; WP_007193242.1; NZ_AFWV01000007.1.
DR   AlphaFoldDB; F9UBR5; -.
DR   STRING; 768671.ThimaDRAFT_2367; -.
DR   PATRIC; fig|768671.3.peg.2507; -.
DR   eggNOG; COG0223; Bacteria.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000005459; Unassembled WGS sequence.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   CDD; cd08704; Met_tRNA_FMT_C; 1.
DR   Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   HAMAP; MF_00182; Formyl_trans; 1.
DR   InterPro; IPR005794; Fmt.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR037022; Formyl_trans_C_sf.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR001555; GART_AS.
DR   InterPro; IPR044135; Met-tRNA-FMT_C.
DR   InterPro; IPR041711; Met-tRNA-FMT_N.
DR   NCBIfam; TIGR00460; fmt; 1.
DR   PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS00373; GART; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00182}; Reference proteome {ECO:0000313|Proteomes:UP000005459};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          19..192
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          215..312
FT                   /note="Formyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02911"
FT   BINDING         121..124
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   321 AA;  34011 MW;  50E9C52F2568F382 CRC64;
     MKPLRIIFAG TPDFAVPSLA ALLDAPADRA QMPPLEVVAV YTQPDRPAGR GRQLQASPVK
     ALALTRGLPV VQPESLKKDP DAVARLAAFE ADLMVVVAYG LLLPVSVLDA PRLGCVNVHA
     SLLPRWRGAA PIQRALLAGD TETGVCIMQM EAGLDTGPVY HRVATPIGPR DTGADLHDRL
     AALGAGALID ALPGIADGSL MPEPQAEDRV TYAHKLTKDE AIIDWHQPAE HIGRMIRAYN
     PWPVAQTRLD AETLRIWSAE IDAERATQAA PGTVIGAGKS GIEVAAGRGI VRIVRLQPPG
     KRAMAAVDFL NARSLDGARL G
//
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