ID A0A1C1CC06_9EURO Unreviewed; 492 AA.
AC A0A1C1CC06;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=tetrahydrofolate synthase {ECO:0000256|ARBA:ARBA00013025};
DE EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE AltName: Full=Folylpoly-gamma-glutamate synthetase {ECO:0000256|ARBA:ARBA00030876};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN ORFNames=CLCR_11240 {ECO:0000313|EMBL:OCT46054.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT46054.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005150}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00008276}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCT46054.1}.
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DR EMBL; LGRB01000017; OCT46054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CC06; -.
DR STRING; 86049.A0A1C1CC06; -.
DR VEuPathDB; FungiDB:CLCR_11240; -.
DR VEuPathDB; FungiDB:G647_10368; -.
DR eggNOG; KOG2525; Eukaryota.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; 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 SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526}.
SQ SEQUENCE 492 AA; 54426 MW; A42B6798E6351F8C CRC64;
MSEAPTDMCC KRTYERGTKH NRHEGLAAKD RLHGTSPKLL SHDDGINVLK SKDIDLAALN
IIHVAGTKGK GSTCAFARSL LQERGKRTGF PNKIGLYTSP DLTCIRERIQ IDGQPISEDL
FTRYFFEIWD PLFSQQDRVT PDASKQPRFL QFMALLAIHT FCREGTQANI FETHHGGEYD
ATNVIAAPVV TGITSIGLDH LAQLGPEIED VAWHKAGIFK NGSPAFSASQ TPTVEAVLRA
RASQKGVQFE IIPVDPSLPR HANALRPHVQ RINCSLAIAL VNTFLSAKSP VDKSQLSEQD
IERGIENFSW PGRFEIIKTP RCTWFLDGAH NELSIGQAVG WFAEMTSSSS DRDGGPQESP
RLVIFSHVSE ERDGLSLLRA LGTALERNTI RCPEMVFTSY QERRDGKVRF DKTLKAPDSS
LADLPKQYPG LWESIQPAAS SRYVPSIEDA LEYADEASHK HGNLQVLVTG SLHLVGGALY
LLQRRKCDAT EG
//
