Folylpolyglutamate synthase
     (EC 6.3.2.17)
     (Folylpoly-gamma-glutamate synthetase)
     (FPGS)
     (Tetrahydrofolylpolyglutamate synthase)
     (Tetrahydrofolate synthase)
Dihydrofolate synthase
     (EC 6.3.2.12)

Gene name

	Name:	folC
	OrderedLocusNames:	BUsg_161

From

Buchnera aphidicola subsp. Schizaphis graminum

[TaxID: 98794]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).

Comments

FUNCTION: Conversion of folates to polyglutamate derivatives.
CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
CATALYTIC ACTIVITY: ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate.
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2 .
SIMILARITY: Belongs to the folylpolyglutamate synthase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE013218; AAM67729.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660518.1; -.

3D structure databases

HSSP

P15925; 1FGS. [HSSP ENTRY / PDB]

ModBase

Q8K9X3.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG161-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008841;	Molecular function: dihydrofolate synthase activity (inferred from electronic annotation from EC).
GO:0004326;	Molecular function: tetrahydrofolylpolyglutamate synthase activity (inferred from electronic annotation from InterPro).
GO:0046656;	Biological process: folic acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001645; Fpolygl_synthtse.
IPR004101; Mur_ligase_C.
IPR013221; Mur_ligase_cen.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.190.20; Mur_ligase_C; 1.
G3DSA:3.40.1190.10; Mur_ligase_cen; 1.

PANTHER

PTHR11136; Fpolygl_synthtse; 1.

Pfam

PF08245; Mur_ligase_M; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01499; folC; 1.

PROSITE

PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PS01012; FOLYLPOLYGLU_SYNT_2; 1.

ProtoNet

Q8K9X3.

Genome annotation databases

GeneID

1005359; -.

GenomeReviews

AE013218_GR; BUsg_161.

KEGG

bas:BUsg161; -.

Phylogenomic databases

HOGENOM

Q8K9X3; -.

Genome annotation databases

CMR

Q8K9X3; BUsg_161.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Folate biosynthesis; Ligase; Multifunctional enzyme; Nucleotide-binding; One-carbon metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 418`	`418`	`Bifunctional protein folC.`	`PRO_0000168301`
`NP_BIND`	`50 56`	`7`	`ATP (By similarity).`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 47631 Da [This is the MW of the unprocessed precursor]

CRC64: 6F644AFF9144AED4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHKKKYTFSM WMKYLEKFDK KDRKNLFELK LIAKKLGLLN LKSFFFTVGG TNGKGTTCAM 

        70         80         90        100        110        120 
LEKLLLDSGY QVGLYTSPHL INYSERIKVN GLYLSEKDHI FSFLIIDAEK GNVSLTYFEF 

       130        140        150        160        170        180 
ITLSALFLFS QYSLDIIILE VGLGGRLDAT NIIDSDLSVI TNIGIDHTSC LGTDRISIGR 

       190        200        210        220        230        240 
EKSGIFRKGK IAVIGEKNIP ISVDEIAKEK KTILKKIDVD WFWTRTKIDS WNFIHSNIEL 

       250        260        270        280        290        300 
YNLPVSRIPL SNTAIALASL FYSGLEVNLK KLKSSISKVQ LSGRFQTVFN SPRIILDVAH 

       310        320        330        340        350        360 
NVHAALYLSE KIDEIDTEGQ IYAVFGILKD KDVAGVVQVL QKKINYWYVV NLKTNRSASI 

       370        380        390        400        410 
NYLKKKLSLN NALFFNNINE SWQAIKKVIT KKDIILVFGS FFTVSEFMSI KDRRLTLY

Q8K9X3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools