ID A0A1W6BCA0_9PROT Unreviewed; 336 AA.
AC A0A1W6BCA0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00016014};
DE EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261};
GN ORFNames=B5L73_01405 {ECO:0000313|EMBL:ARJ47474.1};
OS Candidatus Pelagibacter sp. RS39.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1977864 {ECO:0000313|EMBL:ARJ47474.1, ECO:0000313|Proteomes:UP000198240};
RN [1] {ECO:0000313|EMBL:ARJ47474.1, ECO:0000313|Proteomes:UP000198240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS39 {ECO:0000313|EMBL:ARJ47474.1,
RC ECO:0000313|Proteomes:UP000198240};
RA Jimenez-Infante F., Ngugi D.K., Stingl U.;
RT "Genomic Characterization of Two Novel SAR11 Isolates From the Red Sea,
RT Including the First Strain of the SAR11 Ib clade.";
RL Submitted (APR-2017) 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 -!- 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};
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DR EMBL; CP020777; ARJ47474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6BCA0; -.
DR STRING; 1977864.B5L73_01405; -.
DR OrthoDB; 5355061at2; -.
DR Proteomes; UP000198240; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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 InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR037022; Formyl_trans_C_sf.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
PE 4: Predicted;
FT DOMAIN 208..294
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
SQ SEQUENCE 336 AA; 39252 MW; 37B40DE5A9FA44C9 CRC64;
MIKNNKFYFN ELRNVVILGN LESLEVIKKI NDSLKLNTFL ITSPSFKNNS KNIKIKIFKK
LNNSFLNYIK SNFNIEKTLF VSFGPRWIFK KNIINKLFKK NLVNFHSSRL PIDAGGGGFS
WRIMRNDRLG NCLVHLVDEG IDTGPILKNN EFIFSNDCKT PMDFEKQNTK YFHAFYKSFI
MDLKLKKKIQ IKYQSQNLRR YNPRLDTKIN GWIDWFNSSN EIFNFINAFD EPYPGASTFV
GKNKVRLKQV HLHGGEINGH SFSTGIIIRK NKDWIIVSTT DNNCLIIEKV LNSKNQNIIK
TLREGDRFFT PVSQLVSSRS KRVFYNSISK KSFIKK
//
