Q8DZX5 (TRMFO_STRA5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO
EC=2.1.1.74

Alternative name(s):
Folate-dependent tRNA (uracil-5-)-methyltransferase
Folate-dependent tRNA(M-5-U54)-methyltransferase

Gene names

Name:	trmFO
Synonyms:	gid
Ordered Locus Names:	SAG0969

Organism

Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R) [Complete proteome] [HAMAP]

Taxonomic identifier

208435 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus agalactiae › Streptococcus agalactiae serogroup V

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs By similarity. HAMAP-Rule MF_01037
Catalytic activity	5,10-methylenetetrahydrofolate + uridine54 in tRNA + FADH2 = tetrahydrofolate + 5-methyluridine54 in tRNA + FAD. HAMAP-Rule MF_01037
Cofactor	FAD By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the MnmG family. TrmFO subfamily.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity Inferred from electronic annotation. Source: HAMAP flavin adenine dinucleotide binding Inferred from electronic annotation. Source: HAMAP methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO HAMAP-Rule MF_01037		PRO_0000117270
Regions
	Nucleotide binding	10 – 15	6	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8DZX5 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: CA438676C26001C4	FASTA	444	49,511
	10 20 30 40 50 60 MSQSYINVIG AGLAGSEAAY QIAKRGIPVK LYEMRGVKST PQHKTDNFAE LVCSNSFRGD 70 80 90 100 110 120 SLTNAVGLLK EEMRRLDSII MRNGEAHRVP AGGAMAVDRE GYSEAVTEEI HKHPLIEVIR 130 140 150 160 170 180 DEITDIPGDA ITVIATGPLT SDSLAAKIHE LNGGDGFYFY DAAAPIVDKN TIDINKVYLK 190 200 210 220 230 240 SRYDKGEAAY LNCPMTKEEF MAFHEALTTA EEAPLNSFEK EKYFEGCMPI EVMAKRGIKT 250 260 270 280 290 300 MLYGPMKPVG LEYPEDYKGP RDGEFKTPYA VVQLRQDNAA GSLYNIVGFQ THLKWGEQKR 310 320 330 340 350 360 VFQMIPGLEN AEFVRYGVMH RNSYMDSPNL LNQTFATRKN PNLFFAGQMT GVEGYVESAA 370 380 390 400 410 420 SGLVAGINAV RRFNGESEVV FPQTTAIGAL PHYITHTDSK HFQPMNVNFG IIKELEGPRI 430 440 RDKKERYEAI ATRALKDLEK FLNY

References

[1]

"Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae." Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N., Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D., Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F. , Madupu R., Lewis M.R., Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-611 / 2603 V/R.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009948 Genomic DNA. Translation: AAM99853.1.
RefSeq	NP_687981.1. NC_004116.1.
3D structure databases
ProteinModelPortal	Q8DZX5.
ModBase	Search...
Protein-protein interaction databases
STRING	208435.SAG0969.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM99853; AAM99853; SAG0969.
GeneID	1013773.
KEGG	sag:SAG0969.
PATRIC	19628768. VBIStrAga72745_0975.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1206.
HOGENOM	HOG000252054.
KO	K04094.
OMA	RFAGQIT.
ProtClustDB	PRK05335.
Enzyme and pathway databases
BioCyc	SAGA208435:GHVY-970-MONOMER.
Family and domain databases
HAMAP	MF_01037. TrmFO.
InterPro	IPR004417. Folate-dep_Ribothymidyl_synth. IPR002218. GIDA-rel. IPR020595. GIDA-rel_CS. [Graphical view]
Pfam	PF01134. GIDA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00137. gid_trmFO. 1 hit.
PROSITE	PS01280. GIDA_1. False negative. PS01281. GIDA_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRMFO_STRA5

Accession

Primary (citable) accession number: Q8DZX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program