ID A0A097IHQ2_9CORY Unreviewed; 485 AA.
AC A0A097IHQ2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, 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=CDOO_10510 {ECO:0000313|EMBL:AIT61650.1};
OS Corynebacterium doosanense CAU 212 = DSM 45436.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT61650.1, ECO:0000313|Proteomes:UP000029914};
RN [1] {ECO:0000313|EMBL:AIT61650.1, ECO:0000313|Proteomes:UP000029914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAU 212 {ECO:0000313|EMBL:AIT61650.1,
RC ECO:0000313|Proteomes:UP000029914};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT 45436(T)), isolated from activated sludge.";
RL Submitted (SEP-2013) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR EMBL; CP006764; AIT61650.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097IHQ2; -.
DR STRING; 558173.CDOO_10510; -.
DR KEGG; cdo:CDOO_10510; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_2_11; -.
DR Proteomes; UP000029914; 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: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 SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029914}.
FT DOMAIN 77..315
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 342..419
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 485 AA; 51945 MW; FE28A7115EDD0B49 CRC64;
MSVEEHGLTL NLGESHEHNP EVIARPVTDE HRAELARVEQ ALNARWPETA IDPTLDRIEM
LLDFLGNPER TFKSIHVAGT NGKTSTVRMI ESLLGAFHRR TGRTTSPHLQ SVTERIGIDG
EPIHPEDFVR IYDEIAPFVE LVDSKSEHPM STFEVLVAMA YSAFADAPVD VAVVEVGMGG
RWDATNVISS DVAVIMPVGM DHTDYLGETI EEIAGEKAGI IKSRWDTDDL LAPPDNVAVV
AEQEPEALGV ILERAVEVDA SVARAGSEFG VVTSAIAVGG QMLTLRGLGG DYEEIFLPLA
GEHQAKNAAM ALAAVEALFG AGPGRSLDLE TVRAGFARAS SPGRLERVRN SPSTFVDAAH
NPHGARALGA ALERDYDFSR LIGVVAVLGD KDSANILREL EPHLSEVVIT QNSSPRALDA
YDLAETARDI FGEERVHVVD TLVGAYDLAV ELAEDADIQS GSGIVITGSV VTAGDARAMF
GKDPQ
//
