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Database: UniProt
Entry: A0A223VAB8_9FLAO
LinkDB: A0A223VAB8_9FLAO
Original site: A0A223VAB8_9FLAO 
ID   A0A223VAB8_9FLAO        Unreviewed;       315 AA.
AC   A0A223VAB8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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:GGD94681.1};
GN   ORFNames=CJ263_19995 {ECO:0000313|EMBL:ASV32323.1}, GCM10011412_35870
GN   {ECO:0000313|EMBL:GGD94681.1};
OS   Maribacter cobaltidurans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1178778 {ECO:0000313|EMBL:ASV32323.1, ECO:0000313|Proteomes:UP000215244};
RN   [1] {ECO:0000313|EMBL:ASV32323.1, ECO:0000313|Proteomes:UP000215244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|EMBL:ASV32323.1,
RC   ECO:0000313|Proteomes:UP000215244};
RA   Wu Y.-H., Cheng H., Xu X.-W.;
RT   "The complete genome sequence of Maribacter sp. B1, isolated from deep-sea
RT   sediment.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GGD94681.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD94681.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [3] {ECO:0000313|EMBL:GGD94681.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD94681.1};
RA   Sun Q., Zhou Y.;
RL   Submitted (DEC-2022) 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; CP022957; ASV32323.1; -; Genomic_DNA.
DR   EMBL; BMJL01000011; GGD94681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223VAB8; -.
DR   KEGG; marb:CJ263_19995; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000215244; Chromosome.
DR   Proteomes; UP000603042; 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; 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:UP000215244};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          5..175
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          206..306
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   315 AA;  35431 MW;  DFBCF78DE28CB0FF CRC64;
     MKKLRIVFMG TPDFAVGILD SILNTNYNVV GVITAPDRPA GRGRKLNESS VKKYAMEKGL
     HILQPTNLKS EEFLNELKLL KANLQVVVAF RMLPRVVWQM PAYGTFNLHA SLLPQYRGAA
     PINWAIINGE TKTGVTTFFI DEKIDTGAII LQKEIEIDPE ENAGSLHDKL MVLGSVVVLD
     TIQRIANDNF ETEEQENPKE LKLAHKIHRD TCRIDWDQPM DNIFNFIRGL SPYPAAWTML
     HDGKDETITK IYKVSKEPGR HGLKNGTLIN EKNELRVAVT GGYLNILEVQ LQGKRKMPIK
     DLLNGLNLSK NAHLG
//
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