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Database: UniProt
Entry: J3N3W2_ORYBR
LinkDB: J3N3W2_ORYBR
Original site: J3N3W2_ORYBR 
ID   J3N3W2_ORYBR            Unreviewed;       509 AA.
AC   J3N3W2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
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};
OS   Oryza brachyantha (malo sina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB10G22100.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB10G22100.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB10G22100.1};
RX   PubMed=23481403;
RA   Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA   Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA   Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA   An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA   Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA   Chen M.;
RT   "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT   Oryza genome evolution.";
RL   Nat. Commun. 4:1595-1595(2013).
RN   [2] {ECO:0000313|EnsemblPlants:OB10G22100.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2013) to UniProtKB.
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|ARBA:ARBA00029332,
CC         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|ARBA:ARBA00005150,
CC       ECO:0000256|PIRNR:PIRNR038895}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276, ECO:0000256|PIRNR:PIRNR038895}.
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DR   AlphaFoldDB; J3N3W2; -.
DR   STRING; 4533.J3N3W2; -.
DR   EnsemblPlants; OB10G22100.1; OB10G22100.1; OB10G22100.
DR   Gramene; OB10G22100.1; OB10G22100.1; OB10G22100.
DR   eggNOG; KOG2525; Eukaryota.
DR   HOGENOM; CLU_015869_0_2_1; -.
DR   OMA; HALFCTN; -.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000006038; Chromosome 10.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 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   NCBIfam; TIGR01499; folC; 1.
DR   PANTHER; PTHR11136:SF6; FOLYLPOLYGLUTAMATE SYNTHASE; 1.
DR   PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR   PIRSF; PIRSF038895; FPGS; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 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|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR038895-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038895-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR038895-1};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|PIRNR:PIRNR038895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006038}.
FT   BINDING         95
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT   BINDING         313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
SQ   SEQUENCE   509 AA;  55943 MW;  F4A282723F1A2D36 CRC64;
     MAGVAQPGVA AGSAEYEEVL GCLSSLITQR VRADTGNRGD QWELMAKYLQ ILELEEPIAK
     LKVVHVAGTK GKGSTCTFAE SILRSCGFRT GLFTSPHLMN VRERFRLDGL DISEEKFVRY
     FWWCWNKLKD STGGDIPMPA YFRFLALLAF KIFSDEKQVD VAVLEVGLGG RYDATNVVKA
     PVVCGISSLG YDHMEILGNT LGEIAGEKAG ILKKGVPAYT VPQPEEAMSV LKHRASELGV
     PLQVVQPLDP HQLGDQPLGL HGEHQYMNAG LAVALVNTWL QRQGHFNILH AKHSITLPDQ
     FIKGLSSACL QGRAQIVPDP EMLSKDSSSL IFYLDGAHSP ESMEICARWF SCVTKKDGEQ
     PGSLDQPHFG SNSRKILLFN CMSVRDPQRL LPCLLATCAQ NGLQFDHALF VPNQSQYNKL
     GSHASPPSER VQIDLSWQLS LQRVWEGLLH SNKGSNGANP STASSVFESL PLAIKWLRET
     AQQNQSTSFQ VLVTGSLHLV GDVLRLLKN
//
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