(data stored in SCRATCH zone)

SWISSPROT: FOLC_BACSU

ID   FOLC_BACSU              Reviewed;         430 AA.
AC   Q05865;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   11-DEC-2019, entry version 127.
DE   RecName: Full=Dihydrofolate synthase/folylpolyglutamate synthase;
DE            Short=DHFS / FPGS;
DE            EC=6.3.2.12;
DE            EC=6.3.2.17;
DE   AltName: Full=Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase;
DE   AltName: Full=Folylpolyglutamate synthetase;
DE   AltName: Full=Tetrahydrofolylpolyglutamate synthase;
GN   Name=folC; OrderedLocusNames=BSU28080;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PY79;
RX   PubMed=8419299; DOI=10.1128/jb.175.2.528-540.1993;
RA   Margolis P.S., Driks A., Losick R.;
RT   "Sporulation gene spoIIB from Bacillus subtilis.";
RL   J. Bacteriol. 175:528-540(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-429.
RX   PubMed=2553669; DOI=10.1128/jb.171.11.6043-6051.1989;
RA   Mohan S., Aghion J., Guillen N., Dubnau D.A.;
RT   "Molecular cloning and characterization of comC, a late competence gene of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 171:6043-6051(1989).
CC   -!- FUNCTION: Functions in two distinct reactions of the de novo folate
CC       biosynthetic pathway. Catalyzes the addition of a glutamate residue to
CC       dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate
CC       (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes
CC       successive additions of L-glutamate to tetrahydrofolate, leading to
CC       folylpolyglutamate derivatives. {ECO:0000250|UniProtKB:P08192}.
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:0000250|UniProtKB:P08192};
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:0000250|UniProtKB:P08192};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P08192};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P08192};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC       dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC       dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
CC       {ECO:0000250|UniProtKB:P08192}.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC       biosynthesis. {ECO:0000250|UniProtKB:P08192}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P08192}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA83364.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; L04520; AAB59021.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14768.1; -; Genomic_DNA.
DR   EMBL; M30805; AAA83364.1; ALT_INIT; Genomic_DNA.
DR   PIR; B40646; B40646.
DR   RefSeq; NP_390686.1; NC_000964.3.
DR   RefSeq; WP_003229640.1; NZ_JNCM01000036.1.
DR   SMR; Q05865; -.
DR   STRING; 224308.BSU28080; -.
DR   PaxDb; Q05865; -.
DR   PRIDE; Q05865; -.
DR   EnsemblBacteria; CAB14768; CAB14768; BSU28080.
DR   GeneID; 936327; -.
DR   KEGG; bsu:BSU28080; -.
DR   PATRIC; fig|224308.179.peg.3050; -.
DR   eggNOG; ENOG4105DPM; Bacteria.
DR   eggNOG; COG0285; LUCA.
DR   HOGENOM; HOG000019981; -.
DR   InParanoid; Q05865; -.
DR   KO; K11754; -.
DR   OMA; KCDYAVI; -.
DR   PhylomeDB; Q05865; -.
DR   BioCyc; BSUB:BSU28080-MONOMER; -.
DR   UniPathway; UPA00077; UER00157.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008841; F:dihydrofolate synthase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IBA:GO_Central.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   PANTHER; PTHR11136; PTHR11136; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PIRSF; PIRSF001563; Folylpolyglu_synth; 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   3: Inferred from homology;
DR   PRODOM; Q05865.
DR   SWISS-2DPAGE; Q05865.
KW   ATP-binding; Folate biosynthesis; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Reference proteome.
FT   CHAIN           1..430
FT                   /note="Dihydrofolate synthase/folylpolyglutamate synthase"
FT                   /id="PRO_0000168299"
FT   NP_BIND         51..54
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   REGION          114..117
FT                   /note="7,8-dihydropteroate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   REGION          152..154
FT                   /note="7,8-dihydropteroate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   METAL           75
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   METAL           145
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   METAL           172
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         263
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         302
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         315
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   CONFLICT        295
FT                   /note="V -> M (in Ref. 2; AAA83364)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   430 AA;  48165 MW;  8AD1DF9151D51160 CRC64;
     MFTAYQDARS WIHGRLKFGV KPGLGRMKQL MARLGHPEKK IRAFHVAGTN GKGSTVAFIR
     SMLQEAGYTV GTFTSPYIIT FNERISVNGI PISDEEWTAL VNQMKPHVEA LDQTEYGQPT
     EFEIMTACAF LYFAEFHKVD FVIFETGLGG RFDSTNVVEP LLTVITSIGH DHMNILGNTI
     EEIAGEKAGI IKEGIPIVTA VTQPEALQVI RHEAERHAAP FQSLHDACVI FNEEALPAGE
     QFSFKTEEKC YEDIRTSLIG THQRQNAALS ILAAEWLNKE NIAHISDEAL RSGLVKAAWP
     GRLELVQEHP PVYLDGAHNE EGVEKLAETM KQRFANSRIS VVFSALKDKP YQNMIKRLET
     IAHAIHFASF DFPRASLAKD LYDASEISNK SWSEDPDDVI KFIESKKGSN EIVLITGSLY
     FISDIRKRLK
//

If you have problems or comments...

PBIL Back to PBIL home page