ID A0A1H0TQU0_9MICC Unreviewed; 452 AA.
AC A0A1H0TQU0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN04487914_11745 {ECO:0000313|EMBL:SDP56349.1};
OS Arthrobacter sp. ok909.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1761746 {ECO:0000313|EMBL:SDP56349.1, ECO:0000313|Proteomes:UP000199538};
RN [1] {ECO:0000313|EMBL:SDP56349.1, ECO:0000313|Proteomes:UP000199538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK909 {ECO:0000313|EMBL:SDP56349.1,
RC ECO:0000313|Proteomes:UP000199538};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNJS01000017; SDP56349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0TQU0; -.
DR SMR; A0A1H0TQU0; -.
DR STRING; 1761746.SAMN04487914_11745; -.
DR Proteomes; UP000199538; 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; 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 137..279
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 305..383
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 452 AA; 48234 MW; 19799BBA2BE48397 CRC64;
MTDEFSVESV YAELLGRAPE NKMEPRLAPL YRAMEILGEP NKAFPIIHVT GTNGKTSTAR
MIEAGLRAHG LSTGRYTSPH LSKVTERISI DGAPVPDETF VRIWDEIRPY LQIVDSELEA
EGQPRLTYFE CLTILGFAVF ADQPVNVAVI EVGLGGITDA TNVGDGQVSV VTPISLDHTE
LLGDTTGDIA YEKAGIIKPG GFLISAAQPV DAAQVLLEKA KEVNVPFRFE GVEFGVESRT
VAVGGQMVTI QGIAGRYEDL LVPLHGAHQA ENAAVAIAAL EAFFGAEKAI DAEILQEAFA
SVTSPGRLEV VRTAPTIIVD AAHNPEGIRV SAEAIHEAFN FTKLVVVVGV LREKDAEEIL
RQLKESLGGL ATEYCFTESN SPRAVPAEDL AEIAMDLGFG EDNIHVAAKL DDALEWAVER
AEADDELAGG VLVTGSITLV ADARILLGKA DA
//
