ID Q4BWW2_CROWT Unreviewed; 331 AA.
AC Q4BWW2;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 24-JAN-2024, entry version 85.
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=CwatDRAFT_1044 {ECO:0000313|EMBL:EAM48392.1};
OS Crocosphaera watsonii WH 8501.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM48392.1, ECO:0000313|Proteomes:UP000003922};
RN [1] {ECO:0000313|EMBL:EAM48392.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48392.1,
RC ECO:0000313|Proteomes:UP000003922};
RG DOE Joint Genome Institute;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAM48392.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48392.1,
RC ECO:0000313|Proteomes:UP000003922};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M.;
RT "Annotation of the draft genome assembly of Crocosphaera watsonii WH
RT 8501.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAM48392.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48392.1,
RC ECO:0000313|Proteomes:UP000003922};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Crocosphaera watsonii WH
RT 8501.";
RL Submitted (JUN-2005) 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}.
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:EAM48392.1}.
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DR EMBL; AADV02000149; EAM48392.1; -; Genomic_DNA.
DR RefSeq; WP_007307831.1; NZ_AADV02000149.1.
DR AlphaFoldDB; Q4BWW2; -.
DR KEGG; cwa:CwatDRAFT_1044; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000003922; 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; 3.40.50.12230; -; 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; 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:UP000003922};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 2..182
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 206..321
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT BINDING 111..114
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 331 AA; 37014 MW; 3999C04B4E24BFA1 CRC64;
MQVIFFGTPQ FAVPTLQKLL DHSRFNVIGV VTQPDKRRGR GKQLIPSAVK KIALNHNIPI
WQPKRIKKDQ DTLSQLKNSQ ADAFVVVAYG QILSLEILQM PKVGAINVHG SILPQYRGAA
PIQWCLYNGD RQTGITTMLM DEGMDTGDML LKAYTDINLF ENAYQIAEKL ANQGADLLIE
TLEKLESNEI QAVPQNNEEA TYASLINKDD FIVDWNKSAI AIHNQIRGFY PNCFTSFRDD
KLKIMATIPM DDDHLQSLDE SYQELNNQLK SLDKTIGKPG EVIGLIKNFG PVIKTGKGLL
LLSEIQRSGK RPQSGWDLVN GTHLKVGELL S
//
