ID I2H8M5_TETBL Unreviewed; 430 AA.
AC I2H8M5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Dihydrofolate synthetase {ECO:0000256|PIRNR:PIRNR001563};
DE EC=6.3.2.12 {ECO:0000256|PIRNR:PIRNR001563};
GN Name=TBLA0I00690 {ECO:0000313|EMBL:CCH62727.1};
GN ORFNames=TBLA_0I00690 {ECO:0000313|EMBL:CCH62727.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62727.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH62727.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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; HE806324; CCH62727.1; -; Genomic_DNA.
DR RefSeq; XP_004182246.1; XM_004182198.1.
DR AlphaFoldDB; I2H8M5; -.
DR STRING; 1071380.I2H8M5; -.
DR GeneID; 14497880; -.
DR KEGG; tbl:TBLA_0I00690; -.
DR eggNOG; KOG2525; Eukaryota.
DR HOGENOM; CLU_015869_1_1_1; -.
DR InParanoid; I2H8M5; -.
DR OMA; NENYLVY; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000002866; Chromosome 9.
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:UP000002866}.
FT DOMAIN 29..246
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 430 AA; 47394 MW; 7F1BD4EED1B2243F CRC64;
MSIILGLTRV TKLLSFIGNP ETHLQVIHIA GTNGKGSVCS YISSVLQQIP NAKIGKFTTP
HLIHVTDSIS VNEIPISDGT YRRLRKEVEN INKLNSLECT EFEIMTCTAL KYFHNIKCKW
CVIEVGLGGR LDATNVIPGV NKKACGITKI GLDHESFLGN TLQQIASEKA GIITKGVKFV
AIDGTNAKEV LKVVEDRCKE IKDCVLQITE ANGSNWIAET QSWGTVNLSH LPLNGQYQIF
NSRVAVSILD NLQQRSLLKI SIDQLLSGFS KVEWPGRLQE FIYKHDLEED SVSFLMDGAH
NGSAAIELSN FLKTKYGPSQ PLTFVLAVTN GKTLQPLLDP LLSAKDNVVV TEFESVDGMP
WIKAMDSTEL KSKIQEYTSS IYIDVSVPEA LKHASEISKL KNTPIVVCGS LYLCGQILRL
QNNQTAKSNF
//
