ID A0A1M5SYR8_9BURK Unreviewed; 321 AA.
AC A0A1M5SYR8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN04488135_103223 {ECO:0000313|EMBL:SHH43615.1};
OS Pollutimonas bauzanensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pollutimonas.
OX NCBI_TaxID=658167 {ECO:0000313|EMBL:SHH43615.1, ECO:0000313|Proteomes:UP000184226};
RN [1] {ECO:0000313|EMBL:SHH43615.1, ECO:0000313|Proteomes:UP000184226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10190 {ECO:0000313|EMBL:SHH43615.1,
RC ECO:0000313|Proteomes:UP000184226};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 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; FQXE01000003; SHH43615.1; -; Genomic_DNA.
DR RefSeq; WP_073102403.1; NZ_FQXE01000003.1.
DR AlphaFoldDB; A0A1M5SYR8; -.
DR STRING; 658167.SAMN04488135_103223; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000184226; 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:UP000184226};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 1..188
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 211..317
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT BINDING 117..120
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; 33514 MW; 152E826C936A2308 CRC64;
MRIVFAGTPE FARLALDAII AAGHQVPLVL TQPDRPSGRG LKLTPSAVKQ AALAANIPVC
QPRSLRLDGK YPQEAQAARQ ALLAAEPELL VVAAYGLILP QWLLSLPSYG CFNIHASLLP
RWRGAAPIQR AIEAGDAQTG VTIMLMDAGL DTGAMLFTRA LPITPEHNAA SLHDELAALG
ARAIVQAIEE LQLGTLVSQP QPGEGVTYAA KLDKAEAPLD FTQPAALLER RIRAFDPAPG
ASLMLPGLSA PVKVWKAQAI DAPQTASAAG GGAPAPGQVL HAGASGIDIA TADGVLRLLE
LQKAGGKRQH VAAFVQGWQS R
//
