ID B7IE99_THEAB Unreviewed; 420 AA.
AC B7IE99;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=THA_1900 {ECO:0000313|EMBL:ACJ76326.1};
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=484019 {ECO:0000313|EMBL:ACJ76326.1, ECO:0000313|Proteomes:UP000002453};
RN [1] {ECO:0000313|EMBL:ACJ76326.1, ECO:0000313|Proteomes:UP000002453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B {ECO:0000313|EMBL:ACJ76326.1,
RC ECO:0000313|Proteomes:UP000002453};
RX PubMed=19124572; DOI=10.1128/JB.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ76326.1; -; Genomic_DNA.
DR AlphaFoldDB; B7IE99; -.
DR STRING; 484019.THA_1900; -.
DR KEGG; taf:THA_1900; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_1_0; -.
DR Proteomes; UP000002453; Chromosome.
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 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 45..270
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 292..365
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 420 AA; 48168 MW; D19C2C38CA120DE1 CRC64;
MEYLDALKYL YFKRPYGKIK IGLYRIEELL KRLNNPEKNY KCFHITGSNG KGSTTTFLHY
LAKNHGYKVG GYLSPHLSSI LERFPINGKY ISKERFLNAF NLVKKYSEEM DKKGEEFSPS
FFEFATALAF EIDKEENVEI STIEVGLGGR FDATNVIIPE VSIITTVSLE HTKILGNSLE
KIAYEKAGII KENRPVVIGN VPKEAKKVIY NIAADKNAKV YELGKDFDYE VVEYQFGKNI
INYYGETTIK GLEVNLNGTH QPINAAIALK AYELFEKIDL NNTFVAFKEA FIPGRFEMFN
GFLLDGSHNP QAAEKFLENL NIYFKNDSKI ALFGILDDKD KISVISKLIP EFEHVIVTCP
PSHRAINCLE TYELVKDFSK SCEFIDDPIH AIEKLKEMEA DLKVVNWFIL SCWFHKKLFR
//
