ID A0A0U1QRJ6_9BACL Unreviewed; 438 AA.
AC A0A0U1QRJ6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SINU_03125 {ECO:0000313|EMBL:KLI03372.1};
OS Sporolactobacillus inulinus CASD.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI03372.1, ECO:0000313|Proteomes:UP000035553};
RN [1] {ECO:0000313|EMBL:KLI03372.1, ECO:0000313|Proteomes:UP000035553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CASD {ECO:0000313|EMBL:KLI03372.1,
RC ECO:0000313|Proteomes:UP000035553};
RX PubMed=21952540; DOI=10.1128/JB.05934-11;
RA Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.;
RT "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an
RT efficient D-lactic acid-producing bacterium with high-concentration lactate
RT tolerance capability.";
RL J. Bacteriol. 193:5864-5865(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLI03372.1}.
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DR EMBL; AFVQ02000041; KLI03372.1; -; Genomic_DNA.
DR RefSeq; WP_047034828.1; NZ_AFVQ02000041.1.
DR AlphaFoldDB; A0A0U1QRJ6; -.
DR STRING; 1069536.SINU_03125; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000035553; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000035553}.
FT DOMAIN 46..274
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 300..378
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 438 AA; 48865 MW; FE07F0E28D38C46A CRC64;
MFETIDETLN WIHGLIPHGI KPGTKRMEWM LAELGNPEQK IRAVHVGGTN GKGSTVCYLW
HIYQASGMTV GTFISPYITS FNERIMVNGK PISDQDLIKA ANLVYPLTLA VDRETNLGLP
TEFEVVTMLS FVYFGMIHPC DLVIYEVGLG GRLDSTNVIQ PLVSVITNVA MDHMKQLGTT
IKQIAFEKAG IIKQGTAIVT TAEHPDAQAV IRDKAREKNA ELYLLNTAFS YDSLGHDEDG
EHFNFTAGMF HLHDLVLHMR GEHQLKNASA ALMAVRYLAE CRGLPITEAA IREGLLKAAW
PGRFERMKND PLVIIDGAHN VQGTEALVCT LNSYYEGRTI HLLYAALKDK QYEQMIHLIE
SAVHDVTFTS FNYPRAASSD LLFDASQHHI KKKDPDWMHA LNDLIARTEP GEMVLVCGSL
YFISAVRHAL GDEKSKDM
//
