ID A0A0H4IXJ5_9PROT Unreviewed; 311 AA.
AC A0A0H4IXJ5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00012261, 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=VI33_02870 {ECO:0000313|EMBL:AKO65696.1};
OS Methylophilales bacterium MBRS-H7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=1623450 {ECO:0000313|EMBL:AKO65696.1, ECO:0000313|Proteomes:UP000066549};
RN [1] {ECO:0000313|EMBL:AKO65696.1, ECO:0000313|Proteomes:UP000066549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBRSH7 {ECO:0000313|EMBL:AKO65696.1,
RC ECO:0000313|Proteomes:UP000066549};
RA Jimenez-Infante F., Ngugi D.K., Vinu M., Alam I., Kamau A., Blom J.,
RA Bajic V.B., Stingl U.;
RT "Comparative analysis of the OM43 clade including a novel species from Red
RT Sea uncovers genomic and metabolic diversity among marine methylotrophs.";
RL Submitted (MAR-2015) 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|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|HAMAP-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; CP011002; AKO65696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4IXJ5; -.
DR PATRIC; fig|1623450.3.peg.569; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000066549; Chromosome.
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; 3.40.50.12230; -; 1.
DR HAMAP; MF_00182; Formyl_trans; 1.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
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.
PE 3: Inferred from homology;
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00182}; Reference proteome {ECO:0000313|Proteomes:UP000066549};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 4..176
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 204..300
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT BINDING 109..112
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 311 AA; 34992 MW; 0E2ED51B25AD3C7D CRC64;
MLKIVYAGTP EFALPCLKKI NDSDMEIIAV LTQPDRPAGR GMKIKESPIK KYAKDNQLLY
FQPEKIDEEF TKSIKELRPD VLIVAAYGII LPKHFIDIFP KKAFNIHASI LPKWRGAAPI
QRAIMYGDNQ IGVTIMEVVE KLDAGNIFLI KSFDRDPNKT SGDYFEILSN DGADLMMQHL
NNIQLGLRIE SIVQVEEAVT YAKKISKSEA YLNLENKAEN IVNTVMALNP FPVSRISFRQ
KEVKIFHAEL TNISSVENQP GSINLSDDLL VATSDFYIKI NSIQISGGHT LTGKDFIKNY
QLKPAENFSN V
//
