FOLE_SCHPO
ID FOLE_SCHPO Reviewed; 505 AA.
AC O74742; P78906; Q9USF3;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable folylpolyglutamate synthase;
DE EC=6.3.2.17;
DE AltName: Full=Folylpoly-gamma-glutamate synthetase;
DE Short=FPGS;
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase;
DE Short=Tetrahydrofolate synthase;
GN Name=met7; ORFNames=SPBC1709.17;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 73-126, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-505.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes conversion of folates to polyglutamate derivatives
CC allowing concentration of folate compounds in the cell and the
CC intracellular retention of these cofactors, which are important
CC substrates for most of the folate-dependent enzymes that are involved
CC in one-carbon transfer reactions involved in purine, pyrimidine and
CC amino acid synthesis. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250};
CC Note=A monovalent cation. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC Mitochondrion matrix {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA21256.1; -; Genomic_DNA.
DR EMBL; AB027795; BAA87099.1; -; Genomic_DNA.
DR EMBL; D89257; BAA13918.1; -; mRNA.
DR PIR; T39645; T39645.
DR PIR; T43182; T43182.
DR RefSeq; NP_595450.1; NM_001021359.2.
DR AlphaFoldDB; O74742; -.
DR SMR; O74742; -.
DR STRING; 4896.SPBC1709.17.1; -.
DR MaxQB; O74742; -.
DR PaxDb; O74742; -.
DR PRIDE; O74742; -.
DR EnsemblFungi; SPBC1709.17.1; SPBC1709.17.1:pep; SPBC1709.17.
DR GeneID; 2540103; -.
DR KEGG; spo:SPBC1709.17; -.
DR PomBase; SPBC1709.17; met7.
DR VEuPathDB; FungiDB:SPBC1709.17; -.
DR eggNOG; KOG2525; Eukaryota.
DR HOGENOM; CLU_015869_0_1_1; -.
DR InParanoid; O74742; -.
DR OMA; EAPVMTF; -.
DR PhylomeDB; O74742; -.
DR Reactome; R-SPO-196757; Metabolism of folate and pterines.
DR UniPathway; UPA00850; -.
DR PRO; PR:O74742; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; ISS:PomBase.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0006536; P:glutamate metabolic process; NAS:PomBase.
DR GO; GO:0006730; P:one-carbon metabolic process; ISS:PomBase.
DR GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR023600; Folylpolyglutamate_synth_euk.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR PANTHER; PTHR11136; PTHR11136; 1.
DR PANTHER; PTHR11136:SF5; PTHR11136:SF5; 1.
DR PIRSF; PIRSF038895; FPGS; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01499; folC; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW One-carbon metabolism; Reference proteome.
FT CHAIN 1..505
FT /note="Probable folylpolyglutamate synthase"
FT /id="PRO_0000168311"
FT BINDING 89..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT CONFLICT 161..167
FT /note="DSEKPMY -> QPEIHVL (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="L -> F (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="E -> K (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="L -> P (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="L -> F (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="K -> E (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="K -> L (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="T -> A (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 458..460
FT /note="EAT -> VAA (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="T -> S (in Ref. 3; BAA13918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 56317 MW; BBA2997F937DB4BE CRC64;
MHTAKPVKRY FNLKSSRIGM NPQTKTFEGA INRLNSLQSN AKVLEVLRKR GKIPNDQSMV
EMRHWLRCIG YQPSDLNRLN VIHVAGTKGK GSTCAFTSSI LQQIQKSGER SIPKCIGMYT
SPHLRSVCER IQLNGKPISQ ELFTKYFFDV WERLENAVGS DSEKPMYFRF LTLMAWHVFI
SENVDAAIIE VGIGGEYDST NLIEKPYATA VTSLGLDHTS LLGNTIAEIA WQKAGIYKES
AIALTCEQAP EAMNVLKNRA AERNTSLKVV IPPAELTPDM IGLSGVHQLG NTSLAVSLVQ
EFYEKAGCPF DRDPYQDPAI LDGLKYVKWP GRCQIEEINN IKWCFDGAHT KESLEATGLW
LASKKNLYED ADARILLFNQ QSRDDPIALL RSFLKGLESS GTGISFTHVI FSTNVTWKDA
GYNPELLSIN TITDNKPVLH VQEDLCKWWK ESKGTTSEAT VAPTIQEAIE TVMSIKQKSR
NTFVCVTGSL HLTGGVFVVL DQAVF
