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Database: UniProt
Entry: A0A088QEM4_9CORY
LinkDB: A0A088QEM4_9CORY
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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}.
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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
//
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