ID Q9FVZ0_ORYSJ Unreviewed; 546 AA. AC Q9FVZ0; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 05-JUN-2019, entry version 93. DE RecName: Full=Folylpolyglutamate synthase {ECO:0000256|PIRNR:PIRNR038895}; DE EC=6.3.2.17 {ECO:0000256|PIRNR:PIRNR038895}; DE AltName: Full=Folylpoly-gamma-glutamate synthetase {ECO:0000256|PIRNR:PIRNR038895}; DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|PIRNR:PIRNR038895}; GN Name=OSJNBb0073N24.10 {ECO:0000313|EMBL:AAG13624.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947 {ECO:0000313|EMBL:AAG13624.1}; RN [1] {ECO:0000313|EMBL:AAG13624.1} RP NUCLEOTIDE SEQUENCE. RA Buell C.R., Yuan Q., Moffat K.S., Hill J.N., Jenkins C.N., Burr P.C., RA Hsiao J., Zismann V., Pai G., Bowman C.L., Fujii C.Y., VanAken S.E., RA Bowman C.L., Craven B., Utterback T.R., Khalak H., Feldblyum T.V., RA Quackenbush J., White O., Salzberg S.L., Fraser C.M.; RT "Oryza sativa chromosome 10 BAC OSJNBb0073N24 genomic sequence."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAG13624.1} RP NUCLEOTIDE SEQUENCE. RA Buell R.; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes conversion of folates to polyglutamate CC derivatives allowing concentration of folate compounds in the cell CC and the intracellular retention of these cofactors, which are CC important substrates for most of the folate-dependent enzymes that CC are involved in one-carbon transfer reactions involved in purine, CC pyrimidine and amino acid synthesis. CC {ECO:0000256|PIRNR:PIRNR038895}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)n + ATP + L- CC glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)n+1 + ADP CC + H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738, CC Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005, CC ChEBI:CHEBI:456216; EC=6.3.2.17; CC Evidence={ECO:0000256|PIRNR:PIRNR038895}; CC -!- COFACTOR: CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; CC Evidence={ECO:0000256|PIRNR:PIRNR038895}; CC Note=A monovalent cation. {ECO:0000256|PIRNR:PIRNR038895}; CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate CC biosynthesis. {ECO:0000256|PIRNR:PIRNR038895}. CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family. CC {ECO:0000256|PIRNR:PIRNR038895}. 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; AC078840; AAG13624.1; -; Genomic_DNA. DR InParanoid; Q9FVZ0; -. DR UniPathway; UPA00850; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. 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; IPR023600; Folylpolyglutamate_synth_euk. 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; PIRSF038895; FPGS; 2. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01499; folC; 1. DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRSR:PIRSR038895-1}; KW Ligase {ECO:0000256|PIRNR:PIRNR038895}; KW Magnesium {ECO:0000256|PIRSR:PIRSR038895-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038895-2}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR038895-1}; KW One-carbon metabolism {ECO:0000256|PIRNR:PIRNR038895}. FT DOMAIN 123 270 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT REGION 23 47 Disordered. {ECO:0000256|MobiDB-lite: FT Q9FVZ0}. FT METAL 152 152 Magnesium 1. {ECO:0000256|PIRSR: FT PIRSR038895-2}. FT METAL 221 221 Magnesium 1. {ECO:0000256|PIRSR: FT PIRSR038895-2}. FT METAL 248 248 Magnesium 2. {ECO:0000256|PIRSR: FT PIRSR038895-2}. FT BINDING 350 350 ATP. {ECO:0000256|PIRSR:PIRSR038895-1}. FT BINDING 372 372 ATP. {ECO:0000256|PIRSR:PIRSR038895-1}. SQ SEQUENCE 546 AA; 60109 MW; 673296EE35FA5464 CRC64; MPPPRLAHLR RRSSSLLLLH HNHHHHRGGG SAPPHPLLRP PPPPQSHPFQ LLTPRAAMAS VAQPGVAAGS AEYEEVLGCI SSLITQKVRA DTGNRGNQWE LMAKYLQILE LEEPIARLKV VHVAGTKGKG STCTFAESIL RSCGFRTGLF TSPHLMDVRE RFRLNGLDIS EEKFIRYFWW CWNKLKDKTG GDIPMPAYFR FLALLAFKIF SDEQVDVAVL EVGLGGKYDA TNVVKAPVVC GISSLGYDHM EILGNTLGEI AGEKAGILKK GVPAYTVPQP EEAMSVLKHR ASELGVPLQV VQPLDPQQLD DQPLGLHGEH QYMNAGLAVA LVTLPDQFIE GLSSACLQGR AQIVPDPEVL SKDSSSLIFY LDGAHSPESM EICAKWFSCV TRKDEQQPGP LDQLHIGTNS RKILLFNCMS VRDPQRLLPC LLATCAQNGL QFDHALFVPN QSQYNKLGSH ASPPSERVQI DLSWQLSLQR VWEGLLHSNK GLNGSNSSTA SSVFESLPLA IKWLRETAQQ NQSTSYQVLV TGSLHLVGDV LRLLKE //