ID C7RHW8_ANAPD Unreviewed; 425 AA.
AC C7RHW8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=Apre_1051 {ECO:0000313|EMBL:ACV29079.1};
OS Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806
OS / PC1) (Peptostreptococcus prevotii) (Peptococcus prevotii).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525919 {ECO:0000313|EMBL:ACV29079.1, ECO:0000313|Proteomes:UP000002294};
RN [1] {ECO:0000313|EMBL:ACV29079.1, ECO:0000313|Proteomes:UP000002294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806 / PC1
RC {ECO:0000313|Proteomes:UP000002294};
RX PubMed=21304652; DOI=10.4056/sigs.24194;
RA Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Detter J.C., Han C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Anaerococcus prevotii type strain (PC1).";
RL Stand. Genomic Sci. 1:159-165(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}.
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DR EMBL; CP001708; ACV29079.1; -; Genomic_DNA.
DR AlphaFoldDB; C7RHW8; -.
DR STRING; 525919.Apre_1051; -.
DR KEGG; apr:Apre_1051; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_1_9; -.
DR Proteomes; UP000002294; 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; PS01012; FOLYLPOLYGLU_SYNT_2; 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}.
FT DOMAIN 45..265
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 290..367
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 425 AA; 48187 MW; 4881754B6F43E69E CRC64;
MENFNQYYEF ILNRGSTSGG HSLEKIKNLL EYFDNPQDKI KVIHIAGTNG KGSTANMIAN
TLSRENRVGL FTSPYMTKIN EAISISGVDI SDSDFAEIID RLKKPLEELD KKGLHNSYFE
VLTAIMYIYF YEKKVDVAVV EVGLGGSLDS TNIIKSPLAC VITTISKDHI QILGDSLEEI
AQNKAGIIKD KSEVFLYPKE GTVKEVFIKK IENTSSRLHT FDKEEINIIK TGPDYNEFSF
RSYKNIKTRL VGIHQIYNAV TALITLDFLK DEFSICERDI YEGLLTTRNP GRLELINKNP
RVLVDGSHNR EAIDALIDSI SSYKYRKLIV GFSILKDKDY DYVIDSLAKI ADEIIVTKIK
DNPRAFDTDE LYSLVKDKAK KAIEIVDLVK AYEYSKELAH EDDLVLWCGS LYLVGDILKN
EKAPR
//
