Reviewed, UniProtKB/Swiss-Prot Q89AT2 (FOLC_BUCBP)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folC
Including the following 2 domains:
    1- Recommended name:
            Folylpolyglutamate synthase
              EC=6.3.2.17
        Alternative name(s):
            Folylpoly-gamma-glutamate synthetase
              Short name=FPGS
            Tetrahydrofolylpolyglutamate synthase
              Short name=Tetrahydrofolate synthase
    2- Recommended name:
            Dihydrofolate synthase
              EC=6.3.2.12

Gene names

Name:	folC
Ordered Locus Names:	bbp_157

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	426 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Conversion of folates to polyglutamate derivatives.
Catalytic activity	ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1). 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.
Sequence similarities	Belongs to the folylpolyglutamate synthase family.

Ontologies

Keywords
Biological process	Folate biosynthesis One-carbon metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW dihydrofolate synthase activity Inferred from electronic annotation. Source: EC tetrahydrofolylpolyglutamate synthase 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 – 426	426	Bifunctional protein folC		PRO_0000168302
Regions
	Nucleotide binding	55 – 61	7	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89AT2-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 0D4446A212458EB7	FASTA	426	48,571
	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

References

[1]

"Reductive genome evolution in Buchnera aphidicola." 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. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26891.1.
RefSeq	NP_777786.1.
3D structure databases
HSSP	HSSP built from PDB template 1FGS based on UniProtKB P15925.
ModBase	Search...
Genome annotation databases
GeneID	1058567.
GenomeReviews	Gene locus bbp_157 in contig AE016826_GR.
KEGG	bab:bbp157.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89AT2.
OMA	Q89AT2. FEIYCKK.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_157-MON.
Family and domain databases
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR001645. Fpolygl_synthtse. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
PANTHER	PTHR11136. Fpolygl_synthtse. 1 hit.
Pfam	PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01499. folC. 1 hit.
PROSITE	PS01011. FOLYLPOLYGLU_SYNT_1. 1 hit. PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLC_BUCBP

Accession

Primary (citable) accession number: Q89AT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)