ID   FOLC_BUCAP              Reviewed;         418 AA.
AC   Q8K9X3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Bifunctional protein folC;
DE   Includes:
DE     RecName: Full=Folylpolyglutamate synthase;
DE              EC=6.3.2.17;
DE     AltName: Full=Folylpoly-gamma-glutamate synthetase;
DE              Short=FPGS;
DE     AltName: Full=Tetrahydrofolylpolyglutamate synthase;
DE              Short=Tetrahydrofolate synthase;
DE   Includes:
DE     RecName: Full=Dihydrofolate synthase;
DE              EC=6.3.2.12;
GN   Name=folC; OrderedLocusNames=BUsg_161;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Conversion of folates to polyglutamate derivatives.
CC   -!- CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-
CC       glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
CC   -!- CATALYTIC ACTIVITY: ATP + 7,8-dihydropteroate + L-glutamate = ADP
CC       + phosphate + 7,8-dihydropteroylglutamate.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC       dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC       dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
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DR   EMBL; AE013218; AAM67729.1; -; Genomic_DNA.
DR   RefSeq; NP_660518.1; -.
DR   HSSP; P15925; 1FGS.
DR   GeneID; 1005359; -.
DR   GenomeReviews; AE013218_GR; BUsg_161.
DR   KEGG; bas:BUsg161; -.
DR   HOGENOM; Q8K9X3; -.
DR   OMA; Q8K9X3; SIHPTEI.
DR   BioCyc; BAPH198804:BUSG161-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008841; F:dihydrofolate synthase activity; IEA:EC.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:EC.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR001645; Fpolygl_synthtse.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   PANTHER; PTHR11136; Fpolygl_synthtse; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   TIGRFAMs; TIGR01499; folC; 1.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Folate biosynthesis; Ligase;
KW   Multifunctional enzyme; Nucleotide-binding; One-carbon metabolism.
FT   CHAIN         1    418       Bifunctional protein folC.
FT                                /FTId=PRO_0000168301.
FT   NP_BIND      50     56       ATP (By similarity).
SQ   SEQUENCE   418 AA;  47631 MW;  6F644AFF9144AED4 CRC64;
     MHKKKYTFSM WMKYLEKFDK KDRKNLFELK LIAKKLGLLN LKSFFFTVGG TNGKGTTCAM
     LEKLLLDSGY QVGLYTSPHL INYSERIKVN GLYLSEKDHI FSFLIIDAEK GNVSLTYFEF
     ITLSALFLFS QYSLDIIILE VGLGGRLDAT NIIDSDLSVI TNIGIDHTSC LGTDRISIGR
     EKSGIFRKGK IAVIGEKNIP ISVDEIAKEK KTILKKIDVD WFWTRTKIDS WNFIHSNIEL
     YNLPVSRIPL SNTAIALASL FYSGLEVNLK KLKSSISKVQ LSGRFQTVFN SPRIILDVAH
     NVHAALYLSE KIDEIDTEGQ IYAVFGILKD KDVAGVVQVL QKKINYWYVV NLKTNRSASI
     NYLKKKLSLN NALFFNNINE SWQAIKKVIT KKDIILVFGS FFTVSEFMSI KDRRLTLY
//