ID A0A089YU77_STRGA Unreviewed; 314 AA.
AC A0A089YU77;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ECO:0000313|EMBL:AIR97205.1};
GN ORFNames=SGLAU_05910 {ECO:0000313|EMBL:AIR97205.1};
OS Streptomyces glaucescens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR97205.1, ECO:0000313|Proteomes:UP000029482};
RN [1] {ECO:0000313|Proteomes:UP000029482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL J. Biotechnol. 194:81-83(2015).
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; CP009438; AIR97205.1; -; Genomic_DNA.
DR RefSeq; WP_043498948.1; NZ_CP009438.1.
DR AlphaFoldDB; A0A089YU77; -.
DR STRING; 1907.SGLAU_05910; -.
DR KEGG; sgu:SGLAU_05910; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_0_11; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000029482; 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:UP000029482};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 1..177
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 110..113
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 314 AA; 32977 MW; 968D22B587AA92C9 CRC64;
MKLVFAGTPE VAVPALDALL ASGRHEVAAV VTRPDAPAGR GRRLVASPVA ERAEEAGIEV
LKPAKPRDPE FLDRLRAIAP DCCPVVAYGA LLPRVALDIP AHGWVNLHFS LLPAWRGAAP
VQHSVMAGDE ITGATTFLIE EGLDSGPVYG TVTEEIRPTD TSGDLLTRLA FAGAGLLAAT
MDGIEDGTLK AVPQPADGVT LAPKITVEDA RIDWTAPALR VDRVVRGCTP APGAWTTFRG
ERLKLVQVAV VPERTDLAPG RLSVGKNNVY VGTGSHAVEL LWVQAQGKKP MRAADWARGV
RIADGETVGE AAGV
//
