ID A0A1S9M3J4_9MICC Unreviewed; 453 AA.
AC A0A1S9M3J4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=BMF89_19410 {ECO:0000313|EMBL:OOP59845.1};
OS Arthrobacter sp. SRS-W-1-2016.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1930254 {ECO:0000313|EMBL:OOP59845.1, ECO:0000313|Proteomes:UP000190514};
RN [1] {ECO:0000313|EMBL:OOP59845.1, ECO:0000313|Proteomes:UP000190514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS-W-1-2016 {ECO:0000313|EMBL:OOP59845.1,
RC ECO:0000313|Proteomes:UP000190514};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OOP59845.1}.
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DR EMBL; MTPV01000071; OOP59845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9M3J4; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000190514; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000190514}.
FT DOMAIN 138..279
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 306..380
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 453 AA; 48200 MW; D1647E8326381D2F CRC64;
MSDEFSVESV YAELLGRAPE NKMEPRLAPL YRAMDVLGEP NKAFPIIHIT GTNGKTSTAR
MIEAGLRAHG LSTGRYTSPH LSKVTERISI DGEPVSDETF VRIWDEIRPY LEIVDKELEA
DGQPRLTYFE CLTILGFAIF ADQPVNVAVI EVGLGGITDA TNVGDGQVSV VTPISLDHTD
LLGDTTEDIA HEKAGIIKPG GFLISAAQPV DAAQVLLEKA REVGVPFRFE GVEFGVESRS
VAVGGQVLTI QGIAGRYEDL LLPLHGAHQA ENAAVAVAAL EAFFGGGEKE LDGDVLREAF
GNVTSPGRLE VVRTAPTIIV DAAHNPEGIR VSAEAIEEAF SFSKLVVVLG VLKEKDAEEI
LRQLKESLGG LAEEFCFTQS SSPRAIPAAQ LADLAVDLGF GADNVHIAEK LDDAIEWAVE
RAEANDDLAG GVLVTGSITV VAEARMLLGK VGS
//
