ID Q9FVZ0_ORYSJ Unreviewed; 546 AA. AC Q9FVZ0; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 11-DEC-2019, entry version 95. 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; Magnoliopsida; 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 derivatives CC allowing concentration of folate compounds in the cell and the CC intracellular retention of these cofactors, which are important CC substrates for most of the folate-dependent enzymes that are involved CC in one-carbon transfer reactions involved in purine, pyrimidine and CC amino acid synthesis. {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 FT /note="Mur_ligase_M" FT /evidence="ECO:0000259|Pfam:PF08245" FT REGION 23..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 152 FT /note="Magnesium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2" FT METAL 221 FT /note="Magnesium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2" FT METAL 248 FT /note="Magnesium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2" FT BINDING 350 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR038895-1" FT BINDING 372 FT /note="ATP" FT /evidence="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 //