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Dihydrofolate synthase/folylpolyglutamate synthase (DHFS / FPGS) (EC 6.3.2.12) (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase) (Folylpolyglutamate synthetase) (Tetrahydrofolylpolyglutamate synthase)

 FOLC_BUCAI              Reviewed;         411 AA.
P57265;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 1.
25-OCT-2017, entry version 100.
RecName: Full=Dihydrofolate synthase/folylpolyglutamate synthase;
Short=DHFS / FPGS;
EC=6.3.2.12;
EC=6.3.2.17;
AltName: Full=Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase;
AltName: Full=Folylpolyglutamate synthetase;
AltName: Full=Tetrahydrofolylpolyglutamate synthase;
Name=folC; OrderedLocusNames=BU167;
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
(Acyrthosiphon pisum symbiotic bacterium).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Erwiniaceae; Buchnera.
NCBI_TaxID=107806;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=APS;
PubMed=10993077; DOI=10.1038/35024074;
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids
Buchnera sp. APS.";
Nature 407:81-86(2000).
-!- FUNCTION: Functions in two distinct reactions of the de novo
folate biosynthetic pathway. Catalyzes the addition of a glutamate
residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form
dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also
catalyzes successive additions of L-glutamate to tetrahydrofolate
or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate,
leading to folylpolyglutamate derivatives.
{ECO:0000250|UniProtKB:P08192}.
-!- CATALYTIC ACTIVITY: ATP + 7,8-dihydropteroate + L-glutamate = ADP
+ phosphate + 7,8-dihydropteroylglutamate.
{ECO:0000250|UniProtKB:P08192}.
-!- CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-
glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
{ECO:0000250|UniProtKB:P08192}.
-!- CATALYTIC ACTIVITY: ATP + 10-formyl-tetrahydropteroyl-(gamma-
Glu)(n) + L-glutamate = ADP + phosphate + 10-formyl-
tetrahydropteroyl-(gamma-Glu)(n+1).
{ECO:0000250|UniProtKB:P08192}.
-!- CATALYTIC ACTIVITY: ATP + 5,10-methylene-tetrahydropteroyl-(gamma-
Glu)(n) + L-glutamate = ADP + phosphate + 5,10-methylene-
tetrahydropteroyl-(gamma-Glu)(n+1).
{ECO:0000250|UniProtKB:P08192}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P08192};
Note=Binds 2 Mg(2+) ions per subunit.
{ECO:0000250|UniProtKB:P08192};
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
{ECO:0000250|UniProtKB:P08192}.
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
biosynthesis. {ECO:0000250|UniProtKB:P08192}.
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P08192}.
-!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
{ECO:0000305}.
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EMBL; BA000003; BAB12885.1; -; Genomic_DNA.
RefSeq; NP_239999.1; NC_002528.1.
RefSeq; WP_010895983.1; NC_002528.1.
ProteinModelPortal; P57265; -.
SMR; P57265; -.
STRING; 107806.BU167; -.
EnsemblBacteria; BAB12885; BAB12885; BAB12885.
GeneID; 1109611; -.
KEGG; buc:BU167; -.
PATRIC; fig|107806.10.peg.177; -.
eggNOG; ENOG4105DPM; Bacteria.
eggNOG; COG0285; LUCA.
HOGENOM; HOG000019982; -.
KO; K11754; -.
OMA; LTYFEMG; -.
UniPathway; UPA00077; UER00157.
UniPathway; UPA00850; -.
Proteomes; UP000001806; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008841; F:dihydrofolate synthase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
InterPro; IPR001645; Folylpolyglutamate_synth.
InterPro; IPR018109; Folylpolyglutamate_synth_CS.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
PANTHER; PTHR11136; PTHR11136; 1.
Pfam; PF08245; Mur_ligase_M; 1.
PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
TIGRFAMs; TIGR01499; folC; 1.
PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Folate biosynthesis; Ligase;
Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism;
Reference proteome.
CHAIN 1 411 Dihydrofolate synthase/folylpolyglutamate
synthase.
/FTId=PRO_0000168300.
NP_BIND 53 56 ATP. {ECO:0000250|UniProtKB:P08192}.
REGION 116 119 7,8-dihydropteroate binding.
{ECO:0000250|UniProtKB:P08192}.
REGION 147 149 7,8-dihydropteroate binding.
{ECO:0000250|UniProtKB:P08192}.
METAL 77 77 Magnesium 1.
{ECO:0000250|UniProtKB:P08192}.
METAL 167 167 Magnesium 2.
{ECO:0000250|UniProtKB:P08192}.
BINDING 283 283 ATP. {ECO:0000250|UniProtKB:P08192}.
BINDING 296 296 ATP. {ECO:0000250|UniProtKB:P08192}.
SEQUENCE 411 AA; 46970 MW; 5DDC2DC66539935A CRC64;
MINKNYSLSL WLKYLEQLDK KRIYNLTELK FLAKKLGLLK SESFIFTVAG TNGKGTTCAV
LERLLLDSGY QVGLYTSPHL INFVERVRIN GFVLHEEEHI DSFQNVELVR NGVLLTYFEF
ITLAALILFK RYSLDCIILK VGLGGRLDAT NIIDSDISII TNIGIDHTSI LGRDRISIAR
EKCGVFRKNK ISVIGETDIP CSMYQIAKEK KTILKKIDID WSWEKKRNYW NFFHSTIQLY
NLPETQVPLS SAATALSTLY YSRFKIKEKI IRKSISNVQL PGRFQVISTF PYIIVDVAHN
PNAAFYLSQK IDEINITGKI YAVVGILKDK DILGIIDPLA NKIHHWFTAP LKTIRTATKH
ELKKFFPIHN TSILKSIEIA YKKALILVKK EDAIIIFGSF LTVSEFLSLK I


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