ID F9WUI9_TRYVY Unreviewed; 514 AA.
AC F9WUI9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=tetrahydrofolate synthase {ECO:0000256|ARBA:ARBA00013025};
DE EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE AltName: Full=Folylpoly-gamma-glutamate synthetase {ECO:0000256|ARBA:ARBA00030876};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN ORFNames=TvY486_0041450 {ECO:0000313|EMBL:CCD21238.1};
OS Trypanosoma vivax (strain Y486).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Duttonella.
OX NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCD21238.1, ECO:0000313|Proteomes:UP000009027};
RN [1] {ECO:0000313|EMBL:CCD21238.1, ECO:0000313|Proteomes:UP000009027}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y486 {ECO:0000313|EMBL:CCD21238.1,
RC ECO:0000313|Proteomes:UP000009027};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738,
CC Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005,
CC ChEBI:CHEBI:456216; EC=6.3.2.17;
CC Evidence={ECO:0000256|ARBA:ARBA00029332};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005150}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00008276}.
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DR EMBL; CAEX01007301; CCD21238.1; -; Genomic_DNA.
DR AlphaFoldDB; F9WUI9; -.
DR VEuPathDB; TriTrypDB:TvY486_0041450; -.
DR OMA; ATQWFLD; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000009027; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
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:SF5; FOLYLPOLYGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009027}.
SQ SEQUENCE 514 AA; 57285 MW; 83675FE3BD7C6EA6 CRC64;
MLSCTLWRSM RQSLVLASQQ VSERGTIFNE VGRTFEDVLR IMDKLACRKE KPSTDSVLTT
KQCNTNVELT RMLARHLGMN ECLEKLRFVH VTGTKGKGTT ATYIAALLKT YGLKVGLFTS
PHISDIRERI LVNSELLPRE VFAEYFFQVR DRFVKLAESE KQLFQELSCR TSFFRYIFLT
SLLVFIGENV DVAVMEVGIG GRHDTTNIIV PEVSVITALG IDHTKILGNT VEEIALDKAG
IMKPGVICYS ATQRDHPTTR QILRNYGNIV GAPLIFLEDA RLPEGNWPKL AIGGSHAIEN
SKLALLAARQ FAGVESSQPL SASERYELEY LTLAGRSQVT QVGDGKQITF YLDGAHTYES
LSTATRWFLS ESSSRTGEAD PRRVLLLYSS RDPRSILKAF TPFIACFSKA IIACVSAPKT
KRDLESIDSV ITEVNAIAEC WELLHPSVEC VTITKPFQSL EEVVDIASMK RNERGSRQKP
AQTFVTGSFF LVADIARLLN KHLCKGTQES VGPR
//
