(data stored in SCRATCH zone)

SWISSPROT: Q6BM37_DEBHA

ID   Q6BM37_DEBHA            Unreviewed;       530 AA.
AC   Q6BM37;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Folylpolyglutamate synthase {ECO:0000256|PIRNR:PIRNR038895};
DE            EC=6.3.2.17 {ECO:0000256|PIRNR:PIRNR038895};
DE   AltName: Full=Folylpoly-gamma-glutamate synthetase {ECO:0000256|PIRNR:PIRNR038895};
DE   AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|PIRNR:PIRNR038895};
GN   OrderedLocusNames=DEHA2F08558g {ECO:0000313|EMBL:CAG89074.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 /
OS   IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89074.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89074.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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:0000256|PIRNR:PIRNR038895}.
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|PIRNR:PIRNR038895};
CC   -!- COFACTOR:
CC       Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038895};
CC       Note=A monovalent cation. {ECO:0000256|PIRNR:PIRNR038895};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC       biosynthesis. {ECO:0000256|PIRNR:PIRNR038895}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|PIRNR:PIRNR038895}.
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DR   EMBL; CR382138; CAG89074.2; -; Genomic_DNA.
DR   RefSeq; XP_460734.2; XM_460734.1.
DR   STRING; 4959.XP_460734.2; -.
DR   EnsemblFungi; CAG89074; CAG89074; DEHA2F08558g.
DR   GeneID; 2903356; -.
DR   KEGG; dha:DEHA2F08558g; -.
DR   HOGENOM; HOG000181278; -.
DR   InParanoid; Q6BM37; -.
DR   KO; K01930; -.
DR   OMA; HTFMLGN; -.
DR   OrthoDB; 840266at2759; -.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000000599; Chromosome F.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BM37.
DR   SWISS-2DPAGE; Q6BM37.
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR038895-1};
KW   Ligase {ECO:0000256|PIRNR:PIRNR038895};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR038895-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038895-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR038895-1};
KW   One-carbon metabolism {ECO:0000256|PIRNR:PIRNR038895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           124
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT   METAL           203
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT   METAL           230
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-2"
FT   BINDING         354
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
FT   BINDING         368
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038895-1"
SQ   SEQUENCE   530 AA;  59470 MW;  15FB2F9AF677D39B CRC64;
     MSESDNNKLT PTIINDMRVP TPSTASRTYK DAINALNTLQ SNFASIEAIK KLGPDVNKNE
     MSIREVYEYT RRLGYQPKDF NRMNLIHVTG TKGKGSTCAF AESILSQYRS TNSGPINKIG
     LFTSPHLKTV RERIRIDGSP INELKFTKYF FEVWDKLSTT ESSATEFPTL QPSNVVKPMY
     FKYLTILSFH VFMSEGVDTA IYEVGVGGQY DSTNIIDAPT VVGISSLGID HTFMLGNTID
     SITWNKTGIF KKGCPAVVSD QLEYPESLDV IKERATELGV SRLEIVDTNY LPPNVKLGLA
     GDFQRSNAAL AIKLATIHLQ KLGVPSNELP DFDNSNTLPD KFLKGLSDTQ WSGRCQLIEK
     EGINWYIDGA HTLESINVAS SWFKYTVNTK HQPNKGLKIL LFNQQNRENA NDLLRKLYGN
     VSSSEFKFDH VIFTTNITWS DGNYNSDLVS LNSSKEQVDK LIIQKELAEV WSKLDQKNGY
     NSRKHIFHDI ETSVNFIKSL THDSPVIDVF VCGSLHLVGG FLVVLDNERD
//

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