SPM_000260


  Uniprot: A0A037UKU8
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:SAAS00381977}.
Pathway: 
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): fmt
Gene names (synonym): 
Mass: 35,844
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 5 172 Formyl_trans_N. {ECO:0000259|Pfam:PF00551}.; DOMAIN 206 306 Formyl_trans_C. {ECO:0000259|Pfam:PF02911}.
Motif: 
Region: REGION 112 115 Tetrahydrofolate (THF) binding. {ECO:0000256|HAMAP-Rule:MF_00182}.
EMBL: AGBZ02000001
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92549
UniPathway: 
CDD: 
Gene3D: 
HAMAP: 3.10.25.10;3.40.50.170
InterPro: MF_00182
PANTHER: IPR005794;IPR005793;IPR002376;IPR011034;IPR001555
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: PS00373
ProDom: PF02911;PF00551
SMART: 
SUPFAM: 
TIGRFAMs: SSF50486;SSF53328
51353-52313(-)

>nucleotide sequence
TTAAATAAAAATATTTCCAACTATGATTTCTGACGATGCATTATGATAATAATTTTTAGC
ATCAGTTGCTTTTTTACCTTCGCGTTGTAAACGCGTAATTAATAAATAACCATCTTCAAC
TTTAACTTTAATCCCTAATTTTGAAATATCAATAATTGTTCCATTTACAAAATCAGCGTC
TTTTTCAGCTAATGGTTCTAAGGTAATCACTGCTTGATGCAATTTATAATGAATATTATT
AACAGTTGTGTAAGCAATTGGTCATGCATATAAACCACGAATTTGATCAACAATTTTTTG
TTTTGGTAAAAATCAATTCACTTTTTCTTCATCGCGGGTAATGTTATAAGCAAATGTTGC
TTGACTATCATCTTGTGGTGTTCCCTTAATTTTGCCAGTAATAATATCTAATAAATGCTT
TTCAATCATTGTTCCTGCTAAAACCATTAAACGGTCATGCAAAGATGAAGCTGTTTCCGT
TGGACTAATTGGAATTGCTGTTTGAACATACATTTCGCCCGCATCCATTTTTTTAATCAT
TTGCATTAGCGTAATCCCAGTTTCTTGTTCACCATAAATAATAGCTTTATGAATGGGAGC
ACCACCACGTAATTTTGGTAATAACGAAGCATGAACATTAATACAATTAATCCGGGCTAA
TTTTAAAATTCGCTCTGGAATAAACTGCCCATAAGCACATGTCACAATAACATCTGGTTG
CAAAGTGACTAACTCTGCATAAAGATCATTAATTTTTTCTGGTTGAAAAACAGGAATTTG
ATTTGTTAAAGCAAATTCTTTTACTGGGGAAAATTGAACAAGTTGTTGCCGTCCAATTTT
TCGATCAGGTTGGGTAACAATCCCAATTATTTCAATTGTTGGACTTAACTTTTGCAAAGC
CTTTAAAACAGCTGTCGCAAAGATTGGTGTTCCCATAAAAATCACTCTATATTTTTGCAT


>protein sequence
MQKYRVIFMGTPIFATAVLKALQKLSPTIEIIGIVTQPDRKIGRQQLVQFSPVKEFALTN
QIPVFQPEKINDLYAELVTLQPDVIVTCAYGQFIPERILKLARINCINVHASLLPKLRGG
APIHKAIIYGEQETGITLMQMIKKMDAGEMYVQTAIPISPTETASSLHDRLMVLAGTMIE
KHLLDIITGKIKGTPQDDSQATFAYNITRDEEKVNWFLPKQKIVDQIRGLYAWPIAYTTV
NNIHYKLHQAVITLEPLAEKDADFVNGTIIDISKLGIKVKVEDGYLLITRLQREGKKATD
AKNYYHNASSEIIVGNIFI






















© Fisunov Lab of Proteomics, 2016.