ID F9YTH1_CAPCC Unreviewed; 404 AA.
AC F9YTH1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=Ccan_07130 {ECO:0000313|EMBL:AEK22833.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK22833.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK22833.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
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};
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DR EMBL; CP002113; AEK22833.1; -; Genomic_DNA.
DR RefSeq; WP_013996824.1; NC_015846.1.
DR AlphaFoldDB; F9YTH1; -.
DR STRING; 860228.Ccan_07130; -.
DR KEGG; ccm:Ccan_07130; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_1_10; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000008895; Chromosome.
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: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; 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; 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.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:AEK22833.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895}.
FT DOMAIN 51..226
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 404 AA; 44814 MW; 044D150363379044 CRC64;
MNYKETLAWM FNRLPMYQNK GREALNHKLD NIRLLSEHLG NPHQQFKSIH VAGTNGKGSS
SHMLASVLQQ AGYRVGLYTS PHLRDFRERI KINGVEISEQ YVVDFVARHQ SFFESTSLSF
FEMTVGLAFE YFASENVDIA VIEVGLGGRF DSTNIITPQV SLITNISKDH TDILGHTLAE
IAFEKAGIIK QGIPVVISEN DQQTAVVFVN QAQEKQAPIT FASTLSCNYI TDLQGIYQAK
NIKGVVAVLE ILKNKGWKIT SGNITLGLQN VVKNTGLKGR WQTLSETPKI ICDTAHNLAG
LSLVMQQLQN QQFEKLHIVL GFVKDKDVQQ VLEVFPKSAT YYFCSPAIPR GLEVETLKAL
AETKGLQGQV YPSVQKALEK AKENAHPADF IFVGGSTFVV AEVV
//
