ID FOLC_BACSU Reviewed; 430 AA. AC Q05865; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 2. DT 16-JUN-2009, entry version 68. DE RecName: Full=Folylpolyglutamate synthase; DE EC=6.3.2.17; DE AltName: Full=Folylpoly-gamma-glutamate synthetase; DE Short=FPGS; DE AltName: Full=Tetrahydrofolate synthase; DE AltName: Full=Tetrahydrofolylpolyglutamate synthase; GN Name=folC; OrderedLocusNames=BSU28080; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / PY79; RX MEDLINE=93123172; PubMed=8419299; RA Margolis P.S., Driks A., Losick R.; RT "Sporulation gene spoIIB from Bacillus subtilis."; RL J. Bacteriol. 175:528-540(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-429. RX MEDLINE=90036690; PubMed=2553669; RA Mohan S., Aghion J., Guillen N., Dubnau D.A.; RT "Molecular cloning and characterization of comC, a late competence RT gene of Bacillus subtilis."; RL J. Bacteriol. 171:6043-6051(1989). CC -!- FUNCTION: Conversion of folates to polyglutamate derivatives. It CC preferes 5,10-methylenetetrahydrofolate, rather than 10- CC formyltetrahydrofolate as folate substrate. CC -!- CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L- CC glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1). CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate CC biosynthesis. CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L04520; AAB59021.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14768.1; -; Genomic_DNA. DR EMBL; M30805; AAA83364.1; ALT_INIT; Genomic_DNA. DR PIR; B40646; B40646. DR RefSeq; NP_390686.1; -. DR HSSP; P15925; 1FGS. DR GeneID; 936327; -. DR GenomeReviews; AL009126_GR; BSU28080. DR KEGG; bsu:BSU28080; -. DR NMPDR; fig|224308.1.peg.2811; -. DR SubtiList; BG10322; folC. DR HOGENOM; Q05865; -. DR OMA; Q05865; QRWPETK. DR BioCyc; BSUB224308:BSU2804-MON; -. DR BRENDA; 6.3.2.17; 150. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:EC. DR GO; GO:0009396; P:folic acid and derivative biosynthetic process; IEA:InterPro. 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; PF02875; Mur_ligase_C; 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; Ligase; Nucleotide-binding; KW One-carbon metabolism. FT CHAIN 1 430 Folylpolyglutamate synthase. FT /FTId=PRO_0000168299. FT NP_BIND 48 54 ATP (By similarity). FT CONFLICT 295 295 V -> M (in Ref. 2; AAA83364). SQ SEQUENCE 430 AA; 48165 MW; 8AD1DF9151D51160 CRC64; MFTAYQDARS WIHGRLKFGV KPGLGRMKQL MARLGHPEKK IRAFHVAGTN GKGSTVAFIR SMLQEAGYTV GTFTSPYIIT FNERISVNGI PISDEEWTAL VNQMKPHVEA LDQTEYGQPT EFEIMTACAF LYFAEFHKVD FVIFETGLGG RFDSTNVVEP LLTVITSIGH DHMNILGNTI EEIAGEKAGI IKEGIPIVTA VTQPEALQVI RHEAERHAAP FQSLHDACVI FNEEALPAGE QFSFKTEEKC YEDIRTSLIG THQRQNAALS ILAAEWLNKE NIAHISDEAL RSGLVKAAWP GRLELVQEHP PVYLDGAHNE EGVEKLAETM KQRFANSRIS VVFSALKDKP YQNMIKRLET IAHAIHFASF DFPRASLAKD LYDASEISNK SWSEDPDDVI KFIESKKGSN EIVLITGSLY FISDIRKRLK //