ID Q2RL26_MOOTA Unreviewed; 440 AA.
AC Q2RL26;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=Moth_0533 {ECO:0000313|EMBL:ABC18863.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC18863.1};
RN [1] {ECO:0000313|EMBL:ABC18863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC18863.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) 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; CP000232; ABC18863.1; -; Genomic_DNA.
DR RefSeq; YP_429406.1; NC_007644.1.
DR AlphaFoldDB; Q2RL26; -.
DR STRING; 264732.Moth_0533; -.
DR EnsemblBacteria; ABC18863; ABC18863; Moth_0533.
DR KEGG; mta:Moth_0533; -.
DR PATRIC; fig|264732.11.peg.575; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_2_9; -.
DR OrthoDB; 9809356at2; -.
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|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 44..271
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 297..375
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 440 AA; 48052 MW; 809AAFFCD5AB5EC6 CRC64;
MNYQEALEFL RQLTKFGFNL GLGRIKELMR RVGSPQERLR FIHIGGTNGK GSVSAMVASI
LKAAGYRVGL FTSPHLHSYT ERIQINGQNI PEERLAALLT WFKPLLTAMV ADGYEHPTEF
EVGTAVALKY FADEGVDLVV LEVGLGGAID STNVINTSLV SVITNVGMDH MQYLGNTIAE
IARVKAGIIK PGGIVVTASR LPEALEVIST TCREKGATLY QVGRDVTWRE RRVSLAGGEF
DCRGLLATYE GLKVHLLGRH QLENAATAVA VIEAAVRHHG LKVTPDHLRQ GLAAATWPAR
LEIIQREPMV IIDGAHNFDG AVSLRLALEE IFRYRRLILV LGMLADKERE KVVAVLAPLA
AAVIVTRPNN PRAGNWQSLA DSVRRYVGVV EVIEAIPAAV ERALALAEPS DLICVTGSLY
MVADAREWLK KFKKEESPGG
//
