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Database: UniProt/TrEMBL
Entry: A7GI29_CLOBL
LinkDB: A7GI29_CLOBL
Original site: A7GI29_CLOBL 
ID   A7GI29_CLOBL            Unreviewed;       429 AA.
AC   A7GI29;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   14-MAY-2014, entry version 51.
DE   SubName: Full=FolC bifunctional protein;
DE            EC=6.3.2.12;
DE            EC=6.3.2.17;
GN   Name=folC; OrderedLocusNames=CLI_3227;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L.,
RA   Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., White O.,
RA   Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
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DR   EMBL; CP000728; ABS39712.1; -; Genomic_DNA.
DR   RefSeq; YP_001392439.1; NC_009699.1.
DR   ProteinModelPortal; A7GI29; -.
DR   STRING; 441772.CLI_3227; -.
DR   EnsemblBacteria; ABS39712; ABS39712; CLI_3227.
DR   GeneID; 5403967; -.
DR   KEGG; cbf:CLI_3227; -.
DR   PATRIC; 19429403; VBICloBot15611_3135.
DR   eggNOG; COG0285; -.
DR   HOGENOM; HOG000019981; -.
DR   KO; K11754; -.
DR   OMA; WDATNVA; -.
DR   OrthoDB; EOG6ZPSW2; -.
DR   BioCyc; CBOT441772:GJIE-3193-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008841; F:dihydrofolate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
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; IPR004101; Mur_ligase_C.
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; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding.
SQ   SEQUENCE   429 AA;  48904 MW;  4FDAFC5897DD2767 CRC64;
     MDYKEAREYI QSKAKFGSNL GLERTEKLLE LLGNPHKRLR CIHIAGTNGK GSTTAMISAV
     LKESGYKVGM YTSPYIEEFE ERIQINGHNI TKEDLGYIIT KVANIVEKVE NMGYGNPTEF
     EIITVAMFYY FCLKEVDFAV IEVGLGGRLD STNVLEPILS IITSISYDHM NILGETLEEI
     TYEKAGIIKK APVIMYPQKK EVEKNIEKVC KEKNCDLIKV EDNLINIEIE IIEKNMGQQS
     FKLKTKEDTY NICLSLLGEH QIKNCITVIL ALEKLMKLGI KIEKIHIISA LKKVKWPARL
     EIVNKNPLTV IDGAHNIDGI ESLKNNVSKY FKYNKLILIL GILKDKQVED MIKTLVPLAD
     RVLTVAPHND RGESSKELMH IVLKHNESCE HLEDYKECYD KAKFYCEDGD MILICGSLYM
     VGDMRKLIR
//
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