ID A0A0A8LCL2_9SACH Unreviewed; 421 AA.
AC A0A0A8LCL2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Dihydrofolate synthetase {ECO:0000256|PIRNR:PIRNR001563};
DE EC=6.3.2.12 {ECO:0000256|PIRNR:PIRNR001563};
GN ORFNames=KLDO_g4142 {ECO:0000313|EMBL:CDO95920.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO95920.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO95920.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00008276, 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:CDO95920.1}.
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DR EMBL; CCBQ010000045; CDO95920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8LCL2; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000031516; 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 NCBIfam; TIGR01499; folC; 1.
DR PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 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; PS01011; FOLYLPOLYGLU_SYNT_1; 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}.
SQ SEQUENCE 421 AA; 46326 MW; 2D526FEEEC2724D3 CRC64;
MSIDLGLLRI TQLLSHLGNP HLNLKVLHVA GTNGKGSVCS YLSSVLQQSK YKIGKFTSPH
LCHVRDSITI NQKPIPSQEY QSIKTQLKQL DEKYSLKCTE FELMTATALS FFHQAECSWC
ILEVGLGGRL DATNVIPGIN KICGITKIGL DHESFLGTDL ASIAREKAGI LVEDTPFVAV
DGTNDAAVLK VVEEKAKHVG AEIVKTNPDT AAQFASTSSW GHVDLTQLPL NGEYQTTNVQ
VAVQMLDFMQ RTKLISLNSS QVEHGIRGAE WPGRLQFLDY HYSPRKSTPV LFDGAHNGSA
AIELAKYLNS EFRFSEEEPL TFVLAITNGK NLEPLLSHII RPHDNVICTE FGSVEGMPWI
NAMHADELAS RVKKYTENVK VDTDMLGILP QLAQSGPETK VVVCGSLYLV GQLLNVHYEN
T
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