ID S3JGI8_MICAE Unreviewed; 415 AA.
AC S3JGI8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=tetrahydrofolate synthase {ECO:0000256|ARBA:ARBA00013025};
DE EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN ORFNames=MAESPC_00717 {ECO:0000313|EMBL:EPF24165.1};
OS Microcystis aeruginosa SPC777.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=482300 {ECO:0000313|EMBL:EPF24165.1, ECO:0000313|Proteomes:UP000014617};
RN [1] {ECO:0000313|EMBL:EPF24165.1, ECO:0000313|Proteomes:UP000014617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPC 777 {ECO:0000313|Proteomes:UP000014617};
RX PubMed=23908289;
RA Fiore M.F., Alvarenga D.O., Varani A.M., Hoff-Risseti C., Crespim E.,
RA Ramos R.T., Silva A., Schaker P.D., Heck K., Rigonato J., Schneider M.P.;
RT "Draft Genome Sequence of the Brazilian Toxic Bloom-Forming Cyanobacterium
RT Microcystis aeruginosa Strain SPC777.";
RL Genome Announc. 1:e00547-13(2013).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|PIRNR:PIRNR001563}.
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:EPF24165.1}.
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DR EMBL; ASZQ01000103; EPF24165.1; -; Genomic_DNA.
DR RefSeq; WP_016514709.1; NZ_ASZQ01000103.1.
DR AlphaFoldDB; S3JGI8; -.
DR PATRIC; fig|482300.6.peg.821; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000014617; Unassembled WGS sequence.
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 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; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR NCBIfam; TIGR01499; folC; 1.
DR PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR PIRSF; PIRSF001563; Folylpolyglu_synth; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Ligase {ECO:0000256|PIRNR:PIRNR001563, ECO:0000313|EMBL:EPF24165.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
FT DOMAIN 41..253
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 279..347
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 415 AA; 45486 MW; FB54B949D9B89A1D CRC64;
MTIDSLLQSF QRFGVNLGLE RIKNLLEILG NPQDKIPIIH VTGTNGKGSV CAYLSSILST
AGYKVGRYIS PHLIDWTERI SINGENIETA TLENLLKYIQ SLIDPQQESP TQFEVITAAA
WLYFAREKVD IAVMEVGLGG RLDATNVCAQ PLVTVITSIS REHWQNLGPT VADIAGEKAG
ILKANCPAVI GQLPESAQGV VRERIKLLNC PTVWVEAAEK IADNRAKYQG LEYPLSLAGD
FQLTNSAIAI AVVNILRRQG WQISDEVVQE GMAKTRWLGR LQTVNWCQRE ILIDGAHNPA
AAIGLRQYVD SLKAPKIIWV MGILSTKDHR EIFQALLRKG DSLYLVPVPD HSSANPETLA
ELAASICPEL SHLETCSDAF LGLKKAIQES ADSQIILCGS LYLVGYFLGS LFQGK
//
