ID A0A367Q4K1_9NOSO Unreviewed; 323 AA.
AC A0A367Q4K1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00016014};
DE EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261};
GN ORFNames=A6770_06630 {ECO:0000313|EMBL:RCJ18244.1};
OS Nostoc minutum NIES-26.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1844469 {ECO:0000313|EMBL:RCJ18244.1, ECO:0000313|Proteomes:UP000252107};
RN [1] {ECO:0000313|Proteomes:UP000252107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tabuchi Yagui T.R.;
RL Submitted (APR-2016) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCJ18244.1}.
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DR EMBL; LXQD01000350; RCJ18244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367Q4K1; -.
DR Proteomes; UP000252107; Unassembled WGS sequence.
DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:UniProt.
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; IPR002376; Formyl_transf_N.
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 Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000252107}.
FT DOMAIN 36..164
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 193..292
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
SQ SEQUENCE 323 AA; 35416 MW; 3E282EA730CFC326 CRC64;
MVNVLLIGIG TTTFSALESL LSKCNVQGVV RVDSESDDPV FSLAQQVGIP IFSDTSQQQI
KSLLLKFQPD CVVVSSYNQI LPAELIELSK FINVHYSPLP RYRGRANVNW AIINDETTAA
ITIHKISPGL DEGNILFQQL ISIGFDDTVA TIYDKLNKIQ GQHLGDTVVK AVRGYEGVPQ
NNAEATYGCT RLPEDGEISW SAATRSIDCF IRALVSPFPG AYTYFQGEKL LVWQAKPVDN
PPSYVGRVPG RIIGRSKTEG FVDVLTGDGV LRIFEVQFAG AERTAAANII KSVKSTLGLR
TSDLLNRIQI LEEQISKLKE NAK
//
