ID I7L8S1_9LACO Unreviewed; 414 AA.
AC I7L8S1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-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=BN55_02995 {ECO:0000313|EMBL:CCI80889.1};
OS Lactobacillus hominis DSM 23910 = CRBIP 24.179.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423758 {ECO:0000313|EMBL:CCI80889.1, ECO:0000313|Proteomes:UP000009320};
RN [1] {ECO:0000313|EMBL:CCI80889.1, ECO:0000313|Proteomes:UP000009320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.179T {ECO:0000313|Proteomes:UP000009320};
RA Cousin S., Ma L., Bizet C., Loux V., Bouchier C., Clermont D., Creno S.;
RT "Draft Genome Sequence of Lactobacillus hominis Strain CRBIP 24.179T,
RT isolated from human intestine.";
RL Submitted (JUN-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}.
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:CCI80889.1}.
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DR EMBL; CAKE01000001; CCI80889.1; -; Genomic_DNA.
DR RefSeq; WP_008469446.1; NZ_CAKE01000001.1.
DR AlphaFoldDB; I7L8S1; -.
DR STRING; 1423758.FC41_GL000346; -.
DR GeneID; 82846178; -.
DR PATRIC; fig|1423758.3.peg.349; -.
DR eggNOG; COG0285; Bacteria.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000009320; 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:UniProtKB-EC.
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 Ligase {ECO:0000256|PIRNR:PIRNR001563, ECO:0000313|EMBL:CCI80889.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
FT DOMAIN 44..246
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 284..358
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 414 AA; 47366 MW; D842571230B77E0F CRC64;
MQVQEVIHNI ETLPRLHEKN DLSYIKKVLA FLDNPQDKVK TIHITGTNGK GSTSYYLSNL
IKKAGCKTGL FVSPYVERFN ERIQLNNEQI SDSDLIKGYN AISNAVTELK KADPKFNLVT
FEFETALAFW YFSYKKCDYA VIEVGIGGQH DKTNVITPEV SIITTVGLDH EKIIGPTIED
IAREKSGVIK PRVPVVLGNV PDSVLDILID KAKKESASVY LLGKDFVVSD QKNIVYQDQD
EKMIFDKRPR SESYDLAVAY RVFKLLHLSL SPKKVQEALN NTQIPGRFDV IQKKPLIILD
GAHNIQAITQ LLNYVHELPA KKYKFLVGMM KDKDLKEVLA LFNPQDQLYL TRIDYPRAAK
WEDFKDAIKQ KAIYDEDYKK LFDQLVNELQ DDEVLVVTGS FYLVGALLNY WRHR
//
