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 23-MAY-2018, entry version 102. DE RecName: Full=Dihydrofolate synthase/folylpolyglutamate synthase; DE Short=DHFS / FPGS; DE EC=6.3.2.12; DE EC=6.3.2.17; DE AltName: Full=Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase; DE AltName: Full=Folylpolyglutamate synthetase; DE AltName: Full=Tetrahydrofolylpolyglutamate synthase; GN Name=folC; OrderedLocusNames=BU167; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OS (Acyrthosiphon pisum symbiotic bacterium). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX 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: Functions in two distinct reactions of the de novo CC folate biosynthetic pathway. Catalyzes the addition of a glutamate CC residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form CC dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also CC catalyzes successive additions of L-glutamate to tetrahydrofolate CC or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, CC leading to folylpolyglutamate derivatives. CC {ECO:0000250|UniProtKB:P08192}. CC -!- CATALYTIC ACTIVITY: ATP + 7,8-dihydropteroate + L-glutamate = ADP CC + phosphate + 7,8-dihydropteroylglutamate. CC {ECO:0000250|UniProtKB:P08192}. CC -!- CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L- CC glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1). CC {ECO:0000250|UniProtKB:P08192}. CC -!- CATALYTIC ACTIVITY: ATP + 10-formyl-tetrahydropteroyl-(gamma- CC Glu)(n) + L-glutamate = ADP + phosphate + 10-formyl- CC tetrahydropteroyl-(gamma-Glu)(n+1). CC {ECO:0000250|UniProtKB:P08192}. CC -!- CATALYTIC ACTIVITY: ATP + 5,10-methylene-tetrahydropteroyl-(gamma- CC Glu)(n) + L-glutamate = ADP + phosphate + 5,10-methylene- CC tetrahydropteroyl-(gamma-Glu)(n+1). CC {ECO:0000250|UniProtKB:P08192}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P08192}; CC Note=Binds 2 Mg(2+) ions per subunit. CC {ECO:0000250|UniProtKB:P08192}; 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 {ECO:0000250|UniProtKB:P08192}. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate CC biosynthesis. {ECO:0000250|UniProtKB:P08192}. CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P08192}. CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family. CC {ECO:0000305}. 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 RefSeq; WP_010895983.1; NC_002528.1. DR ProteinModelPortal; P57265; -. DR SMR; P57265; -. DR STRING; 107806.BU167; -. DR PRIDE; P57265; -. DR EnsemblBacteria; BAB12885; BAB12885; BAB12885. DR GeneID; 1109611; -. DR KEGG; buc:BU167; -. DR PATRIC; fig|107806.10.peg.177; -. DR eggNOG; ENOG4105DPM; Bacteria. DR eggNOG; COG0285; LUCA. DR HOGENOM; HOG000019982; -. DR KO; K11754; -. DR OMA; YFEMGTL; -. DR UniPathway; UPA00077; UER00157. DR UniPathway; UPA00850; -. DR Proteomes; UP000001806; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008841; F:dihydrofolate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-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 GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR InterPro; IPR001645; Folylpolyglutamate_synth. DR InterPro; IPR018109; Folylpolyglutamate_synth_CS. DR InterPro; IPR036565; Mur-like_cat_sf. DR InterPro; IPR036615; Mur_ligase_C_dom_sf. DR InterPro; IPR013221; Mur_ligase_cen. DR PANTHER; PTHR11136; PTHR11136; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR PIRSF; PIRSF001563; Folylpolyglu_synth; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 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 Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism; KW Reference proteome. FT CHAIN 1 411 Dihydrofolate synthase/folylpolyglutamate FT synthase. FT /FTId=PRO_0000168300. FT NP_BIND 53 56 ATP. {ECO:0000250|UniProtKB:P08192}. FT REGION 116 119 7,8-dihydropteroate binding. FT {ECO:0000250|UniProtKB:P08192}. FT REGION 147 149 7,8-dihydropteroate binding. FT {ECO:0000250|UniProtKB:P08192}. FT METAL 77 77 Magnesium 1. FT {ECO:0000250|UniProtKB:P08192}. FT METAL 167 167 Magnesium 2. FT {ECO:0000250|UniProtKB:P08192}. FT BINDING 283 283 ATP. {ECO:0000250|UniProtKB:P08192}. FT BINDING 296 296 ATP. {ECO:0000250|UniProtKB:P08192}. 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 //