ID Q0CLN6_ASPTN Unreviewed; 518 AA.
AC Q0CLN6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, 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 ORFNames=ATEG_05398 {ECO:0000313|EMBL:EAU34467.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU34467.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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; CH476600; EAU34467.1; -; Genomic_DNA.
DR RefSeq; XP_001214576.1; XM_001214576.1.
DR AlphaFoldDB; Q0CLN6; -.
DR STRING; 341663.Q0CLN6; -.
DR EnsemblFungi; EAU34467; EAU34467; ATEG_05398.
DR GeneID; 4320778; -.
DR VEuPathDB; FungiDB:ATEG_05398; -.
DR eggNOG; KOG2525; Eukaryota.
DR HOGENOM; CLU_015869_0_1_1; -.
DR OMA; HALFCTN; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000007963; 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; 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|ARBA:ARBA00022563,
KW ECO:0000256|PIRNR:PIRNR038895};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
SQ SEQUENCE 518 AA; 56896 MW; 0FF5D24D05BB4C1F CRC64;
MTRNYEDAIT ALNSLQSNFA IVQEVAKSVS RVDMNLRSIP ETVEWLRRIG YKPSDLNRMN
PVHVAGTKGK GSTSAFIASI LSQYTAAQSN DTSAKLNKVG LYTSPHLRFA RERIKIDNEP
LSEEKFAKYF FEVWDRLEDA ARAAGEDPAE RRTKPQYFRY LTLMAFHTYL SEGVDAAVIE
CGIGGEYDCT NVLEKPAAAA ITSLGIDHTN ILGTTIEEIA WHKGGIIKPG VKAFSAPQPG
GAEKVLHDRA ADKKTEVEIV SGHPDLVRGG DIKLGLAGDF QYTNAAIAVA TAAEFLRKVG
IEDVPADILS KPLPPKFRKG LETARLGGRC ETRYEKNIAW YIDGGHTLES IKLAGQWFAS
QIHANSSSNA AASKKLRLLI FNQQTRDSNA LARALHETLS EALNAEQPFT HAIFCTNVTY
KESGYRPDLV SMNTNASDVE RLAVQNSLAK TWQSIDPSAE VKVYATIEEA VDYARELANE
ERNRIGNDEA PVMTFVTGSL HLVGGFLDVI ETKPSPYA
//
