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A9WMW3 (FTHS_RENSM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formate--tetrahydrofolate ligase

EC=6.3.4.3
Alternative name(s):
Formyltetrahydrofolate synthetase
Short name=FHS
Short name=FTHFS
Gene names
Name:fhs
Ordered Locus Names:RSal33209_1710
OrganismRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP]
Taxonomic identifier288705 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeRenibacterium

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01543

Sequence similarities

Belongs to the formate--tetrahydrofolate ligase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfolic acid-containing compound biosynthetic process

Inferred from electronic annotation. Source: InterPro

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

formate-tetrahydrofolate ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 564564Formate--tetrahydrofolate ligase HAMAP-Rule MF_01543
PRO_0000333316

Regions

Nucleotide binding69 – 768ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9WMW3 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: DC6559FB43FE7A3D

FASTA56459,860
        10         20         30         40         50         60 
MTSTTEPMTD LHIAQQAVLH PIFDIADAAG IPEEALEQYG RYKAKVDVRK VPDSGRAGRV 

        70         80         90        100        110        120 
VLVTAVSPTP AGEGKSTTTV GLADSLNRAF EQEGTGRRSM IALREPSLGP TLGMKGGATG 

       130        140        150        160        170        180 
GGYSQVLPMD EINLHFTGDL HAINSANNAL CALIDNHIYQ GNVLNIDPRR ITFKRVLDMN 

       190        200        210        220        230        240 
DRALREVVIG LGGPTQGVPR QDGFDITVAS EIMAVFCLAT DLNDLKSRIG KITFGYNYDR 

       250        260        270        280        290        300 
QPLTVAGLGV EGVLTLLLKE AIKPNLVQTL AGTAALVHGG PFANIAHGCN SVIATSLARR 

       310        320        330        340        350        360 
RADVVVTEAG FGADLGAEKY MDIKSRFADV APSAVVIVAT IRALKMHGGV PKTELSVSDV 

       370        380        390        400        410        420 
AALRRGVTNL ARHISNVRQF GLDPVVSINR FTSDSEEELD WLVSWCESQG VSIAIADVWG 

       430        440        450        460        470        480 
RGGGGDDLAA KVLAALDAPS DFRHLYELEL PVKEKIELIA QKIYGAERVE FSSSALKRIA 

       490        500        510        520        530        540 
EISANGWDSL PVCMAKTQYS FSDDASLLGA PSGFVLHVRD LVPKTGAGFI VALTGAVMTM 

       550        560 
PGLPKQPAAL KMDVDAEGNS VGLS 

« Hide

References

[1]"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
J. Bacteriol. 190:6970-6982(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000910 Genomic DNA. Translation: ABY23446.1.
RefSeqYP_001624860.1. NC_010168.1.

3D structure databases

ProteinModelPortalA9WMW3.
SMRA9WMW3. Positions 10-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288705.RSal33209_1710.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY23446; ABY23446; RSal33209_1710.
GeneID5822435.
KEGGrsa:RSal33209_1710.
PATRIC23076715. VBIRenSal21953_1777.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2759.
HOGENOMHOG000040280.
KOK01938.
OMACGEIMTM.
OrthoDBEOG6PCPSP.
ProtClustDBPRK13505.

Enzyme and pathway databases

BioCycRSAL288705:GHX1-1710-MONOMER.
UniPathwayUPA00193.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_01543. FTHFS.
InterProIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01268. FTHFS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFTHS_RENSM
AccessionPrimary (citable) accession number: A9WMW3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways