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Database: UniProt
Entry: A0A101KR69_RHILI
LinkDB: A0A101KR69_RHILI
Original site: A0A101KR69_RHILI 
ID   A0A101KR69_RHILI        Unreviewed;       441 AA.
AC   A0A101KR69;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Dihydrofolate synthase/folylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00019357};
DE            EC=6.3.2.12 {ECO:0000256|ARBA:ARBA00013023};
DE            EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE   AltName: Full=Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase {ECO:0000256|ARBA:ARBA00032510};
DE   AltName: Full=Folylpolyglutamate synthetase {ECO:0000256|ARBA:ARBA00030048};
DE   AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN   ORFNames=AU467_26850 {ECO:0000313|EMBL:KUM25444.1};
OS   Rhizobium loti (Mesorhizobium loti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=381 {ECO:0000313|EMBL:KUM25444.1, ECO:0000313|Proteomes:UP000053176};
RN   [1] {ECO:0000313|EMBL:KUM25444.1, ECO:0000313|Proteomes:UP000053176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM25444.1,
RC   ECO:0000313|Proteomes:UP000053176};
RA   Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA   Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT   "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT   efficient symbiont and plant-growth promoting strain isolated from Zn-
RT   mining soil using Leucaena leucocephala as a trap plant.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions in two distinct reactions of the de novo folate
CC       biosynthetic pathway. Catalyzes the addition of a glutamate residue to
CC       dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate
CC       (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes
CC       successive additions of L-glutamate to tetrahydrofolate or 10-
CC       formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to
CC       folylpolyglutamate derivatives. {ECO:0000256|ARBA:ARBA00002714}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC         glutamate = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) +
CC         ADP + H(+) + phosphate; Xref=Rhea:RHEA:51912, Rhea:RHEA-COMP:13257,
CC         Rhea:RHEA-COMP:13258, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:136572,
CC         ChEBI:CHEBI:456216; EC=6.3.2.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000809};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-formyltetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate
CC         = 10-formyltetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:51904, Rhea:RHEA-COMP:13088, Rhea:RHEA-
CC         COMP:14300, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:134413, ChEBI:CHEBI:456216;
CC         EC=6.3.2.17; Evidence={ECO:0000256|ARBA:ARBA00000058};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate +
CC         ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216;
CC         EC=6.3.2.12; Evidence={ECO:0000256|ARBA:ARBA00000104};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC       dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC       dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004799}.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00005150}.
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:KUM25444.1}.
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DR   EMBL; LPWA01000119; KUM25444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101KR69; -.
DR   OrthoDB; 9809356at2; -.
DR   UniPathway; UPA00077; UER00157.
DR   Proteomes; UP000053176; Unassembled WGS sequence.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; IPR018109; Folylpolyglutamate_synth_CS.
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.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
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   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   DOMAIN          48..270
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   441 AA;  47247 MW;  CC14FBCE6D605EC6 CRC64;
     MTTLAADREI EHLMTLHPKG FDLSLDRITR LLERLGNPQD RLPPVIHIAG TNGKGSCAAF
     SRALLEAAGH LVHVHTSPHL VNWHERYRLA AEGGGKLVDD DVFAEAIARV AKANQGQKIT
     VFEILTAVTF ILFSEHPAEA AIIEVGLGGR FDATNVIARP AVSVIMPVSL DHEAYLGDRV
     ELIAAEKAGI MKRGCPVVIG AQESETALEV LIETAERLDC PTVVYGQDFL AFEENGRMVY
     QDEDGLMDLP LPRLPGRHQF ANAAAAIAAV KAAGFEISHR AAERAMVDAA WPARMQKLTQ
     GRLVDLAPKG AEIWLDGGHN PGAGIVIAEA LAEQEEKNPR PLILISGMIN TKDQSGYFSA
     FKGLARHVYT VPVSKSDAGV PNDELALRAT EAGLSAEPVS SVANALMLLR DSWDGPAPRI
     LIGGSLYFAG AVLDENGTPP T
//
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