ID B0G560_9FIRM Unreviewed; 439 AA.
AC B0G560;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:EDR47434.1};
GN ORFNames=DORFOR_01400 {ECO:0000313|EMBL:EDR47434.1};
OS Dorea formicigenerans ATCC 27755.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=411461 {ECO:0000313|EMBL:EDR47434.1, ECO:0000313|Proteomes:UP000005359};
RN [1] {ECO:0000313|EMBL:EDR47434.1, ECO:0000313|Proteomes:UP000005359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27755 {ECO:0000313|EMBL:EDR47434.1,
RC ECO:0000313|Proteomes:UP000005359};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Dorea formicigenerans(ATCC 27755).";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDR47434.1, ECO:0000313|Proteomes:UP000005359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27755 {ECO:0000313|EMBL:EDR47434.1,
RC ECO:0000313|Proteomes:UP000005359};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Wang C., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (OCT-2007) 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:EDR47434.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAXA02000012; EDR47434.1; -; Genomic_DNA.
DR RefSeq; WP_005332467.1; NZ_AAXA02000012.1.
DR AlphaFoldDB; B0G560; -.
DR STRING; 411461.DORFOR_01400; -.
DR PaxDb; 411461-DORFOR_01400; -.
DR GeneID; 42421988; -.
DR eggNOG; COG0285; Bacteria.
DR Proteomes; UP000005359; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 134..275
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 299..370
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 439 AA; 49632 MW; 31E7D04E34126593 CRC64;
MNSKPVNYKE AVEYIESIPK FTQKHTQEHT REFLERLGRP AFDRKVVHVA GTNGKGSVCA
YIQAILEAEG KKTGFFTSPH LISINERIQI GREPIDNEKF YQVFEHVYDV VKKMEEEGIP
HPSYFEFLFG MGLSAFEKSD VEYIVLETGL GGRLDATNAF PCPALTVITS ISLDHTMILG
NTIEQIAAEK AGIIKEGTPV IFDGNDEAAA EIIRNTAREH HAPCREIGKN AFEIREVTRK
HIAFSRTNAY HKDVIWQVPI CGIYQVKNAE IAIEAVQCLL GNKPEHEEMW RDAVAKIQWQ
GRMEECADHF IIDGAHNPGA IEAFVESVRA LKEEEPPILI FSAVSDKKYE QMIEYLCRHL
QTKAFVVTEI EDKRRVPAGE LGEIFKRYAT CPVYVKADVK DAIACAYEMR TKETYIYCIG
SLYLAGMVEK ALQEVETSC
//
