ID A0A088QEM4_9CORY Unreviewed; 497 AA.
AC A0A088QEM4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 Name=folC {ECO:0000313|EMBL:AIN81877.1};
GN ORFNames=DR71_1714 {ECO:0000313|EMBL:AIN81877.1};
OS Corynebacterium sp. ATCC 6931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN81877.1, ECO:0000313|Proteomes:UP000029247};
RN [1] {ECO:0000313|EMBL:AIN81877.1, ECO:0000313|Proteomes:UP000029247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6931 {ECO:0000313|Proteomes:UP000029247};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (JUL-2014) 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}.
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; CP008913; AIN81877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A088QEM4; -.
DR STRING; 1487956.DR71_1714; -.
DR KEGG; coa:DR71_1714; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_2_11; -.
DR Proteomes; UP000029247; 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; PS01011; FOLYLPOLYGLU_SYNT_1; 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:UP000029247}.
FT DOMAIN 170..323
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 350..426
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 497 AA; 53449 MW; E7C83E3AD134FCE1 CRC64;
MRLSEVSVSE EGLSLPVDVD RPVNEPAPLE ATAEELRALA EVEAELDQRW PETKIDPSLE
RIEMLMDILG HPERATPVIH VAGTNGKTST VRMIESLVRA LGRRTGRTTS PHLQLVTERI
AIDGQPIHPR DYVRIWREIQ PYVEMVDAKS AEKGGPQMSK FEVLTAMAYA AFADAPVDVA
VVEVGMGGTW DATNVVEADV AVICPIGLDH TEYLGDTLAE IAAEKAGIIK SRWNKDDLLT
PPDNVAIVGE QEPEAMDVVL RRAVEMDASV ARAGVEYGVV SHQLAVGGQN LTLKGLAGEY
DDIHLPLHGP HQARNAATAL AAVEAFFGAG PGRPLNIDAV REGFATVASP GRLERVRSTP
TVFIDAAHNP HGARALRTAL SAEFDFRRVI GVLSVLGEKD ARGLLVELEP YFEEVVITQN
TSPRALHYDD LADLAEEIFG EERVHRVPTL PSAVELAVAL AEETDTGDGI VSGSGVIVTG
SVVTAGEART LFGKDPQ
//