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Database: UniProt
Entry: K0V0R9_MYCVA
LinkDB: K0V0R9_MYCVA
Original site: K0V0R9_MYCVA 
ID   K0V0R9_MYCVA            Unreviewed;       476 AA.
AC   K0V0R9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=MVAC_00225 {ECO:0000313|EMBL:EJZ12927.1};
OS   Mycolicibacterium vaccae ATCC 25954.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ12927.1, ECO:0000313|Proteomes:UP000006072};
RN   [1] {ECO:0000313|EMBL:EJZ12927.1, ECO:0000313|Proteomes:UP000006072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ12927.1,
RC   ECO:0000313|Proteomes:UP000006072};
RX   PubMed=23105074; DOI=10.1128/JB.01462-12;
RA   Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA   Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT   "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL   J. Bacteriol. 194:6339-6340(2012).
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   -!- 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:EJZ12927.1}.
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DR   EMBL; ALQA01000001; EJZ12927.1; -; Genomic_DNA.
DR   RefSeq; WP_003928422.1; NZ_JH814683.1.
DR   AlphaFoldDB; K0V0R9; -.
DR   PATRIC; fig|1194972.3.peg.47; -.
DR   eggNOG; COG0285; Bacteria.
DR   HOGENOM; CLU_015869_1_2_11; -.
DR   Proteomes; UP000006072; 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   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.
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          147..300
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          327..404
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   476 AA;  49676 MW;  C58A317DC53CA697 CRC64;
     MSPAEPTPDE VAALLQVEHL LDQRWPETKI EPSTARISAL LELLGSPQRG YPSIHIAGTN
     GKTSVARMVD SLLTALHRRT GRTTSPHLQS AVERISIDGK PISPAAYVET YREIEPFVEL
     VDQQSEAGVL GDGPGPRMSK FEVVTAMAFA AFADAPIDVA VVEVGLGGRW DATNVVNAPV
     AVITPIGVDH TDYLGDTIAE IAGEKAGIIT RQADDLVPTD TVAVLARQVP EAMEVLLAQA
     VRSDAAVARE DSEFAVLGRQ VAIGGQLLRL QGLGGVYEEI FLPLHGEHQA HNAVLALAAV
     EAFFGAGADR QLDVDAVRAG FAAVTSPGRL ERMRSAPTVF IDAAHNPGGA LALAEALRDE
     FDFRYLVGVV SVMGDKDVDG ILAALEPVLD QIVVTHNGSP RALEVAALAV KAEEIFGPER
     VITASTLPDA IETATALVED SGSDGDGAGL SGAGIVITGS VVTAGAARTL FGKDPA
//
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