ACL_RS01625

Uniprot: A9NF17
Description: methionyl-tRNA formyltransferase
EC number: 2.1.2.9
Annotation score: 2 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00325839}.
Cofactor:
Enzyme regulation:
Function [CC]: FUNCTION: Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP. {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00381978}.
Pathway:
Active site:
Binding site:
Calcium binding:
DNA binding:
Metal binding:
Nucleotide binding:
Site:
Gene names (primary): fmt
Gene names (synonym):
Mass: 34,113
Subunit structure [CC]:
Gene ontology (GO): methionyl-tRNA formyltransferase activity [GO:0004479]
Gene ontology IDs: GO:0004479
Chain:
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the Fmt family. {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00569886}.
Protein families: Fmt family
Coiled coil:
Domain [FT]: DOMAIN 3 171 Formyl_trans_N. {ECO:0000259|Pfam:PF00551}.; DOMAIN 199 293 Formyl_trans_C. {ECO:0000259|Pfam:PF02911}.
Motif:
Region: REGION 104 107 Tetrahydrofolate (THF) binding. {ECO:0000256|HAMAP-Rule:MF_00182}.
EMBL: CP000896
ProteinModelPortal: A9NF17
MEROPS:
EnsemblBacteria KO: ABX80947
UniPathway: K00604
CDD:
Gene3D:
HAMAP: 3.10.25.10;3.40.50.170
InterPro: MF_00182
PANTHER: IPR005794;IPR005793;IPR002376;IPR011034
PIRSF:
PRINTS:
PROSITE:
Pfam:
ProDom: PF02911;PF00551
SMART:
SUPFAM:
TIGRFAMs: SSF50486;SSF53328

335447-336365(+)

>nucleotide sequence
ATTATGATTGTATTTATGGGTACCCCAGAGTTTTCAGTACCAATTCTAGAAATGTTGATT
GAAGAAAAATATCCGGTTGGGCTAGTTGTTACACAACCAGATAGATTTGTTGGTAGAAAA
AAGATATTAACACCATCACCAGTTAAGTCGCTTGCTTTAGCACATAACATTGAGGTTTTT
CAACCTGAAAAATTACGTCAGGATTATCAACACATCATTGATTTAAAGCCCAGCTTAATT
ATTACAGCAAGCTATGGTCAAATACTTCCTAAAGCCCTTTTAGAAGCAATACCAGCAATT
AACATTCATGGTTCATTATTACCTAAATACCGTGGTGGTGCACCCATTCAATATGCATTA
TTTAATGGGGACGATAAAACCGGTATTACCTTAATGGAAATGGTCTATAAAATGGATGCC
GGTGCTATGATTAAAAAGGTAGAAGTAGACATAGAACCTCTAGATGATTACGGCACTTTA
TCTAATAAGTTATCACTAGCAGGTAGAGATCTATTAAAAGAAAATCTAATGAGTGTTTTA
AATAAAACGTATCAAAGCACACCGCAAAATGAGGATGAAGTGACGTTTGCATTTACACTT
AAATATAGTGATGAAGCACTTGATTTTAACAAGTCAGCATCATGGAATCATAACCGTATT
AGAGGTTTAAGTCCTAACGTTGGTGCACATTTTAACATCAAAAACACTACGGTTAAGGTG
TTTAAATCAGCAATAAGTGATATAATAGACATTCAAAGAGGTGAAATTCGTATAGAAAAT
AAAAGAATATTTATTGGTACGAGTGATAGAGCCATAGAGTTAATTGAATTACAACAATCA
GGTAAAAAACAAATGAAGGTTAAAGATTATTTAAATGGGCAAAGCCTATTTATTAACGGA
GGAAAAATAGATGAGTAA

>protein sequence
IMIVFMGTPEFSVPILEMLIEEKYPVGLVVTQPDRFVGRKKILTPSPVKSLALAHNIEVF
QPEKLRQDYQHIIDLKPSLIITASYGQILPKALLEAIPAINIHGSLLPKYRGGAPIQYAL
FNGDDKTGITLMEMVYKMDAGAMIKKVEVDIEPLDDYGTLSNKLSLAGRDLLKENLMSVL
NKTYQSTPQNEDEVTFAFTLKYSDEALDFNKSASWNHNRIRGLSPNVGAHFNIKNTTVKV
FKSAISDIIDIQRGEIRIENKRIFIGTSDRAIELIELQQSGKKQMKVKDYLNGQSLFING
GKIDE