GenomeNet

Database: UniProt
Entry: A0A0M0I3R6_9VIBR
LinkDB: A0A0M0I3R6_9VIBR
Original site: A0A0M0I3R6_9VIBR 
ID   A0A0M0I3R6_9VIBR        Unreviewed;       315 AA.
AC   A0A0M0I3R6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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   ECO:0000313|EMBL:KOO08767.1};
GN   ORFNames=AKJ31_05260 {ECO:0000313|EMBL:KOO08767.1};
OS   Vibrio hepatarius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=171383 {ECO:0000313|EMBL:KOO08767.1, ECO:0000313|Proteomes:UP000037530};
RN   [1] {ECO:0000313|Proteomes:UP000037530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19134 {ECO:0000313|Proteomes:UP000037530};
RA   Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT   "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT   isolated from the Solomon Islands.";
RL   Submitted (AUG-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|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}.
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:KOO08767.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LHPI01000002; KOO08767.1; -; Genomic_DNA.
DR   RefSeq; WP_053408062.1; NZ_LHPI01000002.1.
DR   AlphaFoldDB; A0A0M0I3R6; -.
DR   STRING; 171383.AKJ31_05260; -.
DR   PATRIC; fig|171383.3.peg.1091; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000037530; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          6..183
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          207..304
FT                   /note="Formyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02911"
FT   BINDING         113..116
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   315 AA;  34135 MW;  5E4605D6B036233B CRC64;
     MSKPLKIVFA GTPDFAARHL AALLSSEHDV IAVYTNPDRP AGRGKKLTAS AVKNVALEHN
     IPVYQPENFK SDEAKQELAD LNADIMVVVA YGMLLPQAVL DTPKLGCINV HGSILPRWRG
     AAPIQRSIWA GDKETGVTIM QMDIGLDTGD MLKVATLPIE ATDTSASMYE KLAELGPQAL
     VECLADIASG SAVAVKQDDE LANYAKKLSK EEALINWSDD AEHIERCVRA FNPWPMSHFV
     AADNSIKVWQ SRVEKQATDK PAGTILQADK TGIYVATGNG VLVLEQLQVP GKKAMHVQDI
     LNSRADWFAV GTQLV
//
DBGET integrated database retrieval system