ID A0A1G9TV40_9ACTO Unreviewed; 620 AA.
AC A0A1G9TV40;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN04487766_103155 {ECO:0000313|EMBL:SDM51586.1};
OS Actinomyces ruminicola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=332524 {ECO:0000313|EMBL:SDM51586.1, ECO:0000313|Proteomes:UP000199671};
RN [1] {ECO:0000313|EMBL:SDM51586.1, ECO:0000313|Proteomes:UP000199671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPR-7B {ECO:0000313|EMBL:SDM51586.1,
RC ECO:0000313|Proteomes:UP000199671};
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}.
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DR EMBL; FNHU01000003; SDM51586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9TV40; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000199671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 212..454
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 478..556
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 65016 MW; 07CAA1C3660A54DA CRC64;
MSSEQQHEQR APIGETRENH PGAAFGIPAG ASGEDVVDAV YGPGGTHSGI DPELLPFLEA
ADSPEGKSLA QAAEDDAAAE RSREQAEAED LAALRELVAA NMVPGGDLER LDALLAEVDA
DDSDDWEEWE PVLSDVVADM EADDAEYSET ERHRADLTAA AHAVEVSARM RQVEAEILSR
APEHQVQPSL DRVAAVLDIL GNPERNYRIV HVAGTNGKTS TARMTERLLA ATGMRTGRFT
SPHLATIRER IALDGEPISE EGFIAAWEDV APYIEMVDAR SQADGGPRLS FFEVLTVMAL
AAFADHPVDV AVIEVGMGGT WDSTNVVPGD VEVITPIGLD HAAWLGTTLA EVAANKAGIV
KDGATLITAL QPEPAQSVIA EAAQAHQVLW RRELDPEEDP DAPDAGVLRV LDRTLGVGGQ
MVTFATAAAV YEDVFIPLHG GYQAHNALLA LAAAEAVFGG GPLPAKIVED GFASVTSPGR
LEVLRSSPTV IVDAGHNPHG VAALVGAVEE AFGFQHLVAV VGLMKDKDAE GILSVLEPTC
DAVVCVPVES PRAMDADDLG AVARDVFGSE RVTVAPILMS GVEQAVNLSE GFDAPLTASG
VLIVGSVVLA AEARALFGRP
//