ID F2UCR7_SALR5 Unreviewed; 527 AA.
AC F2UCR7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ORFNames=PTSG_06385 {ECO:0000313|EMBL:EGD74374.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) 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|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 EMBL; GL832968; EGD74374.1; -; Genomic_DNA.
DR RefSeq; XP_004993274.1; XM_004993217.1.
DR AlphaFoldDB; F2UCR7; -.
DR STRING; 946362.F2UCR7; -.
DR EnsemblProtists; EGD74374; EGD74374; PTSG_06385.
DR GeneID; 16073849; -.
DR KEGG; sre:PTSG_06385; -.
DR eggNOG; KOG2525; Eukaryota.
DR InParanoid; F2UCR7; -.
DR OMA; ESLDCCM; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
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; 2.
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 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:UP000007799}.
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
SQ SEQUENCE 527 AA; 58352 MW; 1610A668A1EE6516 CRC64;
MASHTWTYDE AIEKLNSFQT NASVLQQQRK HGIDLTKAIP LTRDFLQRIN CTQDDLRRLQ
VIHIAGSKGK GSVAAFCESL LRARGFKTGL FTSPHLIEAR ERIRINGAPI SQQQFAQHMQ
DTCALYDATQ PDDGVSKYPT YFKATFLLAL KVFLAEKVDV AVVEVGLGGL YDATNVIDHP
VVCGITHIGY EHTSVLGDTL TKIAHQKCGV LKPGVPSFVT PQTPETLAEF KRSAELRKVN
HMRVYVPNTH THTRTHTHTH THTHTPPGLS GTHQRINAAL AVQLCRTWEA YTRDHQYPVP
QTATDPTQDV LPEVSLQPLT PLESQALQSC AWPGRAQVLQ DGDITYYLDG AHTVDSCKPA
GLPIFVMFHD RPAGLPIFVM FHDRAMAEWL ESVLDRKSPS LRVLIFNCTG DREPEQLLRQ
VLEKHAFDVG IFCPNVASLK STRADQVNHN ASSTACQRMQ RRARDTFARV CTNDATTHLF
PSIEDAITHV RELKAENEAS GKRVDVIVTG SLHLVGGVLG VLGAPVA
//
