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Database: UniProt
Entry: A0A1G9TV40_9ACTO
LinkDB: A0A1G9TV40_9ACTO
Original site: A0A1G9TV40_9ACTO 
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
//
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