ID A0A0A7JI09_9PSED Unreviewed; 435 AA.
AC A0A0A7JI09;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=NJ69_03930 {ECO:0000313|EMBL:AIZ32218.1};
OS Pseudomonas parafulva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157782 {ECO:0000313|EMBL:AIZ32218.1, ECO:0000313|Proteomes:UP000030632};
RN [1] {ECO:0000313|EMBL:AIZ32218.1, ECO:0000313|Proteomes:UP000030632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRS01-1 {ECO:0000313|EMBL:AIZ32218.1,
RC ECO:0000313|Proteomes:UP000030632};
RA Liu Q.;
RT "Genome sequence of Pseudomonas parafulva CRS01-1, an antagonistic
RT bacterium isolated from rice field.";
RL Submitted (OCT-2014) 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 -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005150}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|PIRNR:PIRNR001563}.
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DR EMBL; CP009747; AIZ32218.1; -; Genomic_DNA.
DR RefSeq; WP_039576350.1; NZ_CP009747.1.
DR AlphaFoldDB; A0A0A7JI09; -.
DR KEGG; ppv:NJ69_03930; -.
DR UniPathway; UPA00077; UER00157.
DR Proteomes; UP000030632; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008841; F:dihydrofolate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; 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|ARBA:ARBA00022598, 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 47..187
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 435 AA; 47224 MW; AEFB2D723BF0A2D8 CRC64;
MSERTLGEWL AYLEQLHPSA IDMGLERCRQ VLARLDLGRL AARVVTVTGT NGKGSTCAFV
AALLRAQGLK VGVYSSPHLV RYNERVQIDG NQASDRDLCR AFAAVEAARG EISLTYFEMG
TLAAFWLFRQ SSLDAVVLEV GLGGRLDAVN LIDADLSLVT SIGVDHVDYL GDTREQVAFE
KAGIFRQGTP ALCGDLDPPQ PLLDKVSELA CPFFLRGRDF DLASTDAHWQ WRGTTLRGEA
VELVDLPQLD LPMENAALAV QAYLLMDLPW VASDIAQALL GTRMTGRLDR RTVTWRGQRL
ELLLDVGHNP HAAEYLARRL ATRPVSGRRL AVFGLLADKD LEGVVAPLLP LVDSWAVAPL
ETPRSRTGQE LAMALTNHGA TVKSYASVAA ALEGQCAQAT ADDQILLFGS FFCVGQALEW
LERQALEDGV DGSAG
//
