ID I3K406_ORENI Unreviewed; 608 AA.
AC I3K406;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=fpgs {ECO:0000313|Ensembl:ENSONIP00000015851.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000015851.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000015851.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004273}. Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00008276, ECO:0000256|PIRNR:PIRNR038895}.
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DR AlphaFoldDB; I3K406; -.
DR STRING; 8128.ENSONIP00000015851; -.
DR Ensembl; ENSONIT00000015866.2; ENSONIP00000015851.1; ENSONIG00000012592.2.
DR eggNOG; KOG2525; Eukaryota.
DR GeneTree; ENSGT00390000016526; -.
DR HOGENOM; CLU_015869_0_3_1; -.
DR InParanoid; I3K406; -.
DR OMA; ESLDCCM; -.
DR OrthoDB; 7073at2759; -.
DR TreeFam; TF313956; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000005207; Linkage group LG7.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:SF5; FOLYLPOLYGLUTAMATE SYNTHASE, MITOCHONDRIAL; 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; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR038895-1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|PIRNR:PIRNR038895};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR038895-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038895-2};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR038895-1};
KW One-carbon metabolism {ECO:0000256|PIRNR:PIRNR038895};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
FT BINDING 409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
SQ SEQUENCE 608 AA; 67296 MW; 1B3B7D63143D08EA CRC64;
MTGACSDVIT LEKRAFHIWC PLPGTASRFM MLCMSRMLRR GSGIAARLAR RDRALSLAGL
SCRHYSTETA PHIPGMEYQD AICTLNTLQT NASALEQVRR ERSNPQLQLN AMRAFLERAG
LAVDELDHLN IIHVTGTKGK GSTCAFTEQI LRNYGFRTGF YSSPHLVQVR ERIRINGQPI
GKDLFTKYFW QVYGRLDETK DAHGGTMPAY FRFLTILAFH VFLQEKVDLA VIEVGIGGAY
DCTNIIRRPW VCGISSLGID HTQILGDTIE KIAWQKGGIF KPGVPGFTVR QPEGAMPVLK
ERAKEIGCPL WVCPQLEDYQ PDCGPLHLGL AGQHQRSNAS LALQLSHTWL QRRCLPADHS
FPITTVENNG TLQAPAFSPS PIMVKGLADA QWPGRTQTLK HGEVTYFLDG AHTMRSMQAC
VQWFRETAAQ HERSASGAVA RVLLFNATGE RDSAAMLKLL VTCHFDFAVF CPNITEAIAS
CNADQQNFNV SVENMLTRCL DNERSWRLHN RLGDDKGTQL LIQDSLPRLP EHRGDTLVFP
CILSALQWIT QGRDSVLADP AKTTLAVKQS VTAKAAPLRE AAEIHVLITG SLHLVGGALK
HLDPASSK
//
