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Database: UniProt
Entry: R4KE96_CLOPA
LinkDB: R4KE96_CLOPA
Original site: R4KE96_CLOPA 
ID   R4KE96_CLOPA            Unreviewed;       438 AA.
AC   R4KE96;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=Clopa_3125 {ECO:0000313|EMBL:AGK97940.1};
OS   Clostridium pasteurianum BC1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK97940.1, ECO:0000313|Proteomes:UP000013523};
RN   [1] {ECO:0000313|EMBL:AGK97940.1, ECO:0000313|Proteomes:UP000013523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC1 {ECO:0000313|EMBL:AGK97940.1,
RC   ECO:0000313|Proteomes:UP000013523};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA   Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT   "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL   Submitted (JAN-2012) 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   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001563}.
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DR   EMBL; CP003261; AGK97940.1; -; Genomic_DNA.
DR   RefSeq; WP_015616228.1; NC_021182.1.
DR   AlphaFoldDB; R4KE96; -.
DR   STRING; 86416.Clopa_3125; -.
DR   KEGG; cpas:Clopa_3125; -.
DR   PATRIC; fig|86416.3.peg.3110; -.
DR   eggNOG; COG0285; Bacteria.
DR   HOGENOM; CLU_015869_1_2_9; -.
DR   OrthoDB; 9809356at2; -.
DR   Proteomes; UP000013523; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001563};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001563};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013523}.
FT   DOMAIN          44..273
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          299..377
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   438 AA;  49315 MW;  097D1F336A6F706B CRC64;
     MDYKETMDYI KNTAKFGSNY GLSRTKKILE LLGNPEEKLK CIHIAGTNGK GSTTAMVSKI
     LIEAGYKVGM YTSPFIEEFE ERIRIDEKNI PKEELCEVVT ELSTAVNEVI KLGYEHPTEF
     EIITCTAFLY FYKKQVDYAV IEVGLGGRLD STNVITPLVS VITSISYDHM NILGNTLTEI
     AHEKAGIIKN NVPVILYPQE AECEVVIRET CAKHNSKIIS VSRESAEFIN TFKSQEESKY
     YQQIRVKTSK DIYNIKLSLL GKYQLLNCST AIHCIEELKD KGINVTKACI ERALKSVIWR
     GRLEVLSDSP LVVLDGAHNI DGIKNLSESV DKYFKYNNIV LILGILADKQ VEAMVKIIAP
     KAKYIIAVTP NSDRAEISKD LAKIVKRFNS NCESFDDYKE AFIKAKGYCK NGDLLLVSGS
     LYMIGDMRKI INNAREFV
//
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