ID G8BVZ7_TETPH Unreviewed; 435 AA.
AC G8BVZ7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Dihydrofolate synthetase {ECO:0000256|PIRNR:PIRNR001563};
DE EC=6.3.2.12 {ECO:0000256|PIRNR:PIRNR001563};
GN Name=TPHA0G02400 {ECO:0000313|EMBL:CCE64075.1};
GN OrderedLocusNames=TPHA_0G02400 {ECO:0000313|EMBL:CCE64075.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE64075.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE64075.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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 -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00008276, ECO:0000256|PIRNR:PIRNR001563}.
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DR EMBL; HE612862; CCE64075.1; -; Genomic_DNA.
DR RefSeq; XP_003686509.1; XM_003686461.1.
DR AlphaFoldDB; G8BVZ7; -.
DR STRING; 1071381.G8BVZ7; -.
DR GeneID; 11535799; -.
DR KEGG; tpf:TPHA_0G02400; -.
DR eggNOG; KOG2525; Eukaryota.
DR HOGENOM; CLU_015869_2_0_1; -.
DR OMA; NENYLVY; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000005666; Chromosome 7.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666}.
SQ SEQUENCE 435 AA; 48289 MW; 9EC402E25AD678F8 CRC64;
MSINLGLSRV NKLLQVIGNP HQRLKIIHVA GTNGKGSVCS YLASLLRHDS IPSRSPKIGK
FTTPHMVHIT DSICVNDKPI PINTYKSIRT LLEEKNMEYE IKCSEFELLT CAAIKFFEDS
SCNICVFEVG LGGRLDATNI IPGSNKLACG ITKIGLDHES ILGSTLAEIG REKAGIITDG
VNLVVVDSSN DHTVLNEIEK RCENTGSQLY KTELHSGGLT FKTDSWDIIK LDTLPLNGHY
QAFNFSVALK ILDKLQVQKK IYIEKEFITP KYLNDVKWPG RLQDLDFCYT MDETNSPKTV
PILLDGAHNG SAAIELEKYL REKYDDNQCI NFVIAVTDGK KLEPLLSPLI RPQDSVLVTQ
FENVDGMPWI KPYDPKVLAT FIQENYTKNV KVDSSLTSVV ANLGEMHSGN TTPIVICGSL
YLCGQLLNIN KTNNL
//
