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:	bbp_157

From

Buchnera aphidicola subsp. Baizongia pistaciae

[TaxID: 135842]

[HAMAP proteome]

Taxonomy

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

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).

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

AE016826; AAO26891.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_777786.1; -.

3D structure databases

HSSP

P15925; 1FGS. [HSSP ENTRY / PDB]

ModBase

Q89AT2.

Enzyme and pathway databases

BioCyc

BAPH224915:BBP_157-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

PF02875; Mur_ligase_C; 1.
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.

Genome annotation databases

GeneID

1058567; -.

GenomeReviews

AE016826_GR; bbp_157.

KEGG

bab:bbp157; -.

Phylogenomic databases

HOGENOM

Q89AT2; -.

Genome annotation databases

CMR

Q89AT2; bbp_157.

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`	`1 426`	`426`	`Bifunctional protein folC.`	`PRO_0000168302`
`NP_BIND`	`55 61`	`7`	`ATP (By similarity).`

Sequence information

Length: 426 AA [This is the length of the unprocessed precursor]

Molecular weight: 48571 Da [This is the MW of the unprocessed precursor]

CRC64: 0D4446A212458EB7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MINKKLARSF SLYEWLYYLD HFMLDNIDPT LNRVFYVAKK LGVLKSKAFV FIVGGTNGKG 

        70         80         90        100        110        120 
STCHVLENLL LNSGYRVGLY TSPHLMRYTE RVRINGFELE HLYHISAFND VKYFQNDVLL 

       130        140        150        160        170        180 
TRFEFITLSA LILFKSYNLD IIILEVGLGG RLDATNILSA DVSVITNIDI DHSKILGVNR 

       190        200        210        220        230        240 
SSISVEKSGI FRKNKIAIVA DNNFPKVAQY LAKKKKVRLR IVNIDWIYKK IEFEWSFCSS 

       250        260        270        280        290        300 
KITWLHLPLP RNVSLDSVAT ALSAVSESGI KINQKVFRSC ISEITLCGRF ETISYNPIII 

       310        320        330        340        350        360 
LDVAHNPHSA RYLFKKMSSF KKNGNIFAVV GILKEKNIKD IVSPLIPIVD YWYCITLLTH 

       370        380        390        400        410        420 
RSATSSEIIK YLPNHNSQIS KNMTVALEKI FDKVTNNDIV LIFGSFITVC EANKFLANKV 


KNFKLL

Q89AT2 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