ID C1CYP7_DEIDV Unreviewed; 418 AA.
AC C1CYP7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 2.
DT 24-JAN-2024, entry version 66.
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 OrderedLocusNames=Deide_20591 {ECO:0000313|EMBL:ACO47077.2};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47077.2, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47077.2, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001114; ACO47077.2; -; Genomic_DNA.
DR AlphaFoldDB; C1CYP7; -.
DR STRING; 546414.Deide_20591; -.
DR PaxDb; 546414-Deide_20591; -.
DR KEGG; ddr:Deide_20591; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_2_0; -.
DR Proteomes; UP000002208; Chromosome.
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:InterPro.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT DOMAIN 44..258
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 277..349
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 418 AA; 44199 MW; D3F8DD6324EEB60D CRC64;
MRLEADLEWL FSRQRFGMHP GLTRVHSLLT RLGEPQRAFR VVLVGGTNGK GSTAASLASM
LRAQGRRVGL FTSPHLTRFA ERFVVGGELL PDDVVLRSLH QVRPHAEAIE ASFFEIVTAL
GCLVFAEAGV QDAVMEVGLG GRLDATNALD PVLSVITNVA LDHTEVLGNT VELIAAEKAG
ILRPGRPAVT GAAPDVWPML EAEGADLWSL ENRVRRQSLG WDGEQVVVRL PAGVELTFRT
PLLGAHGAQN AALAAAAAYR LGVSPEAISR GAQTTQWPGR MEVLTVGEGR VLLDGAHNPA
GAEAVVRALR DLGVGKLPLV FGAAADKDLS GVAAALEPVA SQVVLTRARL SPRSADPAAL
APLFPGHQVT LTESPEQAIA ALRALGAPLA LVCGSLYLIG EVRPLLLGTV SEERERWQ
//
