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Q05865 (FOLC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Folylpolyglutamate synthase
EC=6.3.2.17
Alternative name(s):
Folylpoly-gamma-glutamate synthetase
Short name=FPGS
Tetrahydrofolate synthase
Tetrahydrofolylpolyglutamate synthase
Gene names
Name:folC
Ordered Locus Names:BSU28080
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Conversion of folates to polyglutamate derivatives. It preferes 5,10-methylenetetrahydrofolate, rather than 10-formyltetrahydrofolate as folate substrate.

Catalytic activity

ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).

Pathway

Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis.

Sequence similarities

Belongs to the folylpolyglutamate synthase family.

Sequence caution

The sequence AAA83364.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

tetrahydrofolylpolyglutamate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Folylpolyglutamate synthase
PRO_0000168299

Regions

Nucleotide binding48 – 547ATP By similarity

Experimental info

Sequence conflict2951V → M in AAA83364. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q05865 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 8AD1DF9151D51160

FASTA43048,165
        10         20         30         40         50         60 
MFTAYQDARS WIHGRLKFGV KPGLGRMKQL MARLGHPEKK IRAFHVAGTN GKGSTVAFIR 

        70         80         90        100        110        120 
SMLQEAGYTV GTFTSPYIIT FNERISVNGI PISDEEWTAL VNQMKPHVEA LDQTEYGQPT 

       130        140        150        160        170        180 
EFEIMTACAF LYFAEFHKVD FVIFETGLGG RFDSTNVVEP LLTVITSIGH DHMNILGNTI 

       190        200        210        220        230        240 
EEIAGEKAGI IKEGIPIVTA VTQPEALQVI RHEAERHAAP FQSLHDACVI FNEEALPAGE 

       250        260        270        280        290        300 
QFSFKTEEKC YEDIRTSLIG THQRQNAALS ILAAEWLNKE NIAHISDEAL RSGLVKAAWP 

       310        320        330        340        350        360 
GRLELVQEHP PVYLDGAHNE EGVEKLAETM KQRFANSRIS VVFSALKDKP YQNMIKRLET 

       370        380        390        400        410        420 
IAHAIHFASF DFPRASLAKD LYDASEISNK SWSEDPDDVI KFIESKKGSN EIVLITGSLY 

       430 
FISDIRKRLK

« Hide

References

« Hide 'large scale' references
[1]"Sporulation gene spoIIB from Bacillus subtilis."
Margolis P.S., Driks A., Losick R.
J. Bacteriol. 175:528-540(1993) [PubMed: 8419299] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / PY79.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Molecular cloning and characterization of comC, a late competence gene of Bacillus subtilis."
Mohan S., Aghion J., Guillen N., Dubnau D.A.
J. Bacteriol. 171:6043-6051(1989) [PubMed: 2553669] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-429.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L04520 Genomic DNA. Translation: AAB59021.1.
AL009126 Genomic DNA. Translation: CAB14768.1.
M30805 Genomic DNA. Translation: AAA83364.1. Different initiation.
PIRB40646.
RefSeqNP_390686.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ05865.
SMRQ05865. Positions 2-430.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001837; EBBACP00000001837; EBBACG00000001834.
GeneID936327.
GenomeReviewsGene locus BSU28080 in contig AL009126_GR.
KEGGbsu:BSU28080.
NMPDRfig|224308.1.peg.2811.
PATRIC18977490. VBIBacSub10457_2934.

Organism-specific databases

GenoListBSU28080. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000631.
HOGENOMHBG744947.
OMAAVERISI.
PhylomeDBQ05865.
ProtClustDBCLSK2460946.

Enzyme and pathway databases

BioCycBSUB:BSU28080-MONOMER.

Family and domain databases

InterProIPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]
Gene3DG3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KOK11754.
PANTHERPTHR11136. Fpolygl_synthtse. 1 hit.
PfamPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
PIRSFPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMSSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01499. FolC. 1 hit.
PROSITEPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFOLC_BACSU
AccessionPrimary (citable) accession number: Q05865
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1994
Last modified: January 25, 2012
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents