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Database: UniProt
Entry: C1GBY4_PARBD
LinkDB: C1GBY4_PARBD
Original site: C1GBY4_PARBD 
ID   C1GBY4_PARBD            Unreviewed;       426 AA.
AC   C1GBY4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Dihydrofolate synthetase {ECO:0000256|PIRNR:PIRNR001563};
DE            EC=6.3.2.12 {ECO:0000256|PIRNR:PIRNR001563};
GN   ORFNames=PADG_04506 {ECO:0000313|EMBL:EEH48427.1};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH48427.1, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH48427.1, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH48427.1,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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|PIRNR:PIRNR001563};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC       biosynthesis. {ECO:0000256|PIRNR:PIRNR001563}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276, ECO:0000256|PIRNR:PIRNR001563}.
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DR   EMBL; KN275961; EEH48427.1; -; Genomic_DNA.
DR   RefSeq; XP_010760279.1; XM_010761977.1.
DR   AlphaFoldDB; C1GBY4; -.
DR   SMR; C1GBY4; -.
DR   STRING; 502780.C1GBY4; -.
DR   GeneID; 22583613; -.
DR   KEGG; pbn:PADG_04506; -.
DR   VEuPathDB; FungiDB:PADG_04506; -.
DR   eggNOG; KOG2525; Eukaryota.
DR   HOGENOM; CLU_015869_2_0_1; -.
DR   InParanoid; C1GBY4; -.
DR   OMA; YFEMGTL; -.
DR   OrthoDB; 7073at2759; -.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000001628; 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:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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   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   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|PIRNR:PIRNR001563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT   DOMAIN          25..188
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   426 AA;  46413 MW;  0AC1581A0D368327 CRC64;
     MIELGLSRIS RLVQHSHLPW RAIHVAGTNG KGSITAYLSA LLAAAGVRCG SFTSPHLIDR
     WDCITINERV IQESFFRRVE NEVKLRSQML GVNASEFELL TATAFEIFTN QNVEVGIIEV
     GMGGRLDATN VLSNVLVSVI AKIGYDHQAI LGDTIEKITR EKAGIMKAGV PCVVDGTNEP
     LVQQVLRAAA VKAHTPITFA RPDIIQQTFP ELVGIFQHLH LEPHQLANIS CALTGLQQAL
     PQLKPNSTLP SLFPYISKTP RPGRLQEISL NPLIPRKQPV LLDGAHNPQS ATVLCAYVDR
     NLRKQTPEHA GITWVISASQ GKDIKELFSC IVKPGDNVAV VEFGPVDGMP WMRSVQAAEL
     LSVVKAFIPD IARFEIFSRD VLSGLKWADE ISGGGPLVIA GSLYLVSDVL RLLRGVNSDV
     DILKSS
//
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