ID FOLC_BUCAI Reviewed; 411 AA. AC P57265; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 18-APR-2012, entry version 73. 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=BU167; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OS (Acyrthosiphon pisum symbiotic bacterium). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX MEDLINE=20445173; PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids RT Buchnera sp. APS."; RL Nature 407:81-86(2000). 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 7,8-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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000003; BAB12885.1; -; Genomic_DNA. DR RefSeq; NP_239999.1; NC_002528.1. DR ProteinModelPortal; P57265; -. DR EnsemblBacteria; EBBUCT00000002830; EBBUCP00000002606; EBBUCG00000002830. DR GeneID; 1109611; -. DR GenomeReviews; BA000003_GR; BU167. DR KEGG; buc:BU167; -. DR PATRIC; 21243850; VBIBucAph127364_0177. DR eggNOG; COG0285; -. DR HOGENOM; HBG744947; -. DR KO; K11754; -. DR OMA; TYFEFIT; -. DR ProtClustDB; CLSK315624; -. DR BioCyc; BSP107806:BU167-MONOMER; -. 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 metabolic process; IEA:UniProtKB-KW. DR Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1. DR Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1. DR InterPro; IPR001645; Folylpolyglutamate_synth. DR InterPro; IPR018109; Folylpolyglutamate_synth_CS. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR PANTHER; PTHR11136; Fpolygl_synthtse; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR PIRSF; PIRSF001563; Folylpolyglu_synth; 1. DR SUPFAM; SSF53244; Mur_ligase_C; 1. DR SUPFAM; SSF53623; Mur_ligase_cen; 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; KW Reference proteome. FT CHAIN 1 411 Bifunctional protein folC. FT /FTId=PRO_0000168300. FT NP_BIND 50 56 ATP (By similarity). SQ SEQUENCE 411 AA; 46970 MW; 5DDC2DC66539935A CRC64; MINKNYSLSL WLKYLEQLDK KRIYNLTELK FLAKKLGLLK SESFIFTVAG TNGKGTTCAV LERLLLDSGY QVGLYTSPHL INFVERVRIN GFVLHEEEHI DSFQNVELVR NGVLLTYFEF ITLAALILFK RYSLDCIILK VGLGGRLDAT NIIDSDISII TNIGIDHTSI LGRDRISIAR EKCGVFRKNK ISVIGETDIP CSMYQIAKEK KTILKKIDID WSWEKKRNYW NFFHSTIQLY NLPETQVPLS SAATALSTLY YSRFKIKEKI IRKSISNVQL PGRFQVISTF PYIIVDVAHN PNAAFYLSQK IDEINITGKI YAVVGILKDK DILGIIDPLA NKIHHWFTAP LKTIRTATKH ELKKFFPIHN TSILKSIEIA YKKALILVKK EDAIIIFGSF LTVSEFLSLK I //