ID A0A0K2JG58_SPIKU Unreviewed; 319 AA.
AC A0A0K2JG58;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:ALA97413.1};
GN ORFNames=SKUN_00512 {ECO:0000313|EMBL:ALA97413.1};
OS Spiroplasma kunkelii CR2-3x.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=273035 {ECO:0000313|EMBL:ALA97413.1, ECO:0000313|Proteomes:UP000062963};
RN [1] {ECO:0000313|EMBL:ALA97413.1, ECO:0000313|Proteomes:UP000062963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR2-3x {ECO:0000313|EMBL:ALA97413.1,
RC ECO:0000313|Proteomes:UP000062963};
RX PubMed=26494665;
RA Davis R.E., Shao J., Dally E.L., Zhao Y., Gasparich G.E., Gaynor B.J.,
RA Athey J.C., Harrison N.A., Donofrio N.;
RT "Complete Genome Sequence of Spiroplasma kunkelii Strain CR2-3x, Causal
RT Agent of Corn Stunt Disease in Zea mays L.";
RL Genome Announc. 3:e01216-e01215(2015).
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; CP010899; ALA97413.1; -; Genomic_DNA.
DR RefSeq; WP_053390699.1; NZ_CP010899.1.
DR AlphaFoldDB; A0A0K2JG58; -.
DR STRING; 273035.SKUN_00512; -.
DR KEGG; skn:SKUN_00512; -.
DR PATRIC; fig|273035.7.peg.611; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000062963; Chromosome.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 5..173
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 206..305
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT BINDING 112..115
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 319 AA; 35953 MW; 4A75AAE42C3E19F3 CRC64;
MQKYRVIFMG TPIFATAVLK ALQNLAPTIE IIGIVTQPDR KIGRQHLVQF SPVKEFALTN
QIPVFQPEKI NDLYTELGTL QPDVIVTCAY GQFIPERILK LARINCINVH ASLLPKLRGG
APIHKAIIYG ERETGITLMK MIKKMDAGEM YVQTAIPISA AETASSLHDR LMVLAGTMIE
KYLLDIITGK IKGTPQDDSQ ATFAYNITRD EEKVNWFLPK QKIVDQIRGL YAWPIAHTTV
NNIYYKLHQA MITLHPLEEK DADFVNGTII DISKLGIKVK VEDGYLLITR LQREGKKVTD
AKNYYHNASS EIMVGNIFI
//
