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LACF3:FMT

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Species (Taxon ID) Lactobacillus fermentum (strain NBRC 3956 / LMG 18251). (334390)
Gene Name(s) fmt (ECO:0000255 with HAMAP-Rule:MF_00182)
Protein Name(s) Methionyl-tRNA formyltransferase (ECO:0000255 with HAMAP-Rule:MF_00182)
External Links
UniProt B2GD55
EMBL AP008937
RefSeq YP_001844067.1
ProteinModelPortal B2GD55
STRING 334390.LAF_1251
EnsemblBacteria BAG27587
GeneID 6232119
KEGG lfe:LAF_1251
PATRIC 22226780
eggNOG COG0223
HOGENOM HOG000261177
KO K00604
OMA KVWQSRV
OrthoDB EOG6B09WV
BioCyc LFER334390:GJ2S-1298-MONOMER
Proteomes UP000001697
GO GO:0004479
GO:0008168
Gene3D 3.10.25.10
3.40.50.170
HAMAP MF_00182
InterPro IPR005794
IPR005793
IPR002376
IPR011034
IPR001555
IPR015518
PANTHER PTHR11138
Pfam PF02911
PF00551
SUPFAM SSF50486
SSF53328
TIGRFAMs TIGR00460
PROSITE PS00373

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009058

biosynthetic process

PMID:10694387[1]

ECO:0000315

P

The formylation of initiator methionyl-tRNA by methionyl-tRNA formyltransferase (MTF) is important for the initiation of protein synthesis in eubacteria.

complete

involved_in

GO:0006413

translational initiation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004479

P

Seeded From UniProt

complete

involved_in

GO:0006413

translational initiation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004479

P

Seeded From UniProt

complete

involved_in

GO:0006413

translational initiation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004479

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011034

F

Seeded From UniProt

complete

enables

GO:0004479

methionyl-tRNA formyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005794

F

Seeded From UniProt

complete

involved_in

GO:0009058

biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002376
InterPro:IPR005793
InterPro:IPR036477
InterPro:IPR037022

P

Seeded From UniProt

complete

enables

GO:0016742

hydroxymethyl-, formyl- and related transferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002376
InterPro:IPR005793
InterPro:IPR036477
InterPro:IPR037022

F

Seeded From UniProt

complete

involved_in

GO:0071951

conversion of methionyl-tRNA to N-formyl-methionyl-tRNA

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005794

P

Seeded From UniProt

complete

enables

GO:0004479

methionyl-tRNA formyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.1.2.9

F

Seeded From UniProt

complete

involved_in

GO:0019988

charged-tRNA amino acid modification

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001456

P

Seeded From UniProt

complete

enables

GO:0004479

methionyl-tRNA formyltransferase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001456

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0006412

translation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0648

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Gite, S et al. (2000) Escherichia coli methionyl-tRNA formyltransferase: role of amino acids conserved in the linker region and in the C-terminal domain on the specific recognition of the initiator tRNA. Biochemistry 39 2218-26 PubMed GONUTS page