GenomeNet

Database: UniProt
Entry: A0A370G5Y1_GLULI
LinkDB: A0A370G5Y1_GLULI
Original site: A0A370G5Y1_GLULI 
ID   A0A370G5Y1_GLULI        Unreviewed;       305 AA.
AC   A0A370G5Y1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=C7453_106178 {ECO:0000313|EMBL:RDI37453.1}, HLH32_14210
GN   {ECO:0000313|EMBL:MBB2187510.1};
OS   Gluconacetobacter liquefaciens (Acetobacter liquefaciens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=89584 {ECO:0000313|EMBL:RDI37453.1, ECO:0000313|Proteomes:UP000254958};
RN   [1] {ECO:0000313|EMBL:RDI37453.1, ECO:0000313|Proteomes:UP000254958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5603 {ECO:0000313|EMBL:RDI37453.1,
RC   ECO:0000313|Proteomes:UP000254958};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB2187510.1, ECO:0000313|Proteomes:UP000562982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 1382 {ECO:0000313|EMBL:MBB2187510.1,
RC   ECO:0000313|Proteomes:UP000562982};
RA   Sombolestani A.;
RT   "Description of novel Gluconacetobacter.";
RL   Submitted (APR-2020) 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:RDI37453.1}.
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; JABEQI010000009; MBB2187510.1; -; Genomic_DNA.
DR   EMBL; QQAW01000006; RDI37453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370G5Y1; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000254958; Unassembled WGS sequence.
DR   Proteomes; UP000562982; 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          1..180
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          201..295
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   305 AA;  31769 MW;  246E57436A534574 CRC64;
     MRLAFMGTPD FAVPALLALH AAGHEIAAVY SQPPRPAGRG QSVRLSPVHQ AAETLGLPVR
     TPARLRTNAD EHAAFRDLNL DAAVVAAYGL ILPAAMLDAP RLGCLNIHAS LLPRWRGAAP
     IQAAILAGDS ESGVTIMRMD EGLDTGAMLL SDQVALTPTT TATTLHDALA AMGARLIVTT
     LSQPVGPGQP QPEQGVTYAG RLTREDGRID WSRDAAALDR QIRALTPWPG TFTTLDGQVL
     KIGGAALVSA PRSAPPGTIL DDALTVACGQ GALRITRIQR PGRGMMDADS FLRGQAVAPG
     TVLGS
//
DBGET integrated database retrieval system