(data stored in ACNUC30630 zone)

HOGENOM: BASUB1_1_PE2318

ID   BASUB1_1_PE2318                      STANDARD;      PRT;   515 AA.
AC   BASUB1_1_PE2318; P03963;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Anthranilate synthase component 1; EC=4.1.3 27;AltName:
DE   Full=Anthranilate synthase component I; (BASUB1_1.PE2318).
GN   Name=trpE; OrderedLocusNames=BSU22680;
OS   BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BASUB1_1.PE2318.
CC       Bacillus subtilis subsp. subtilis str. 168 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:TRPE_BACSU
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC       pyruvate + L-glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Tetramer of two components I and two components II (By
CC       similarity).
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=Ref.1; Type=Frameshift; Positions=343, 402;
CC       Sequence=Ref.2; Type=Frameshift; Positions=343, 402;
CC   -!- GENE_FAMILY: HOG000025142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P03963; -.
DR   EMBL; K01391; AAA22865.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; M80245; AAA20862.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14184.1; -; Genomic_DNA.
DR   EMBL; M27566; AAA22875.1; -; Genomic_DNA.
DR   PIR; A01119; NNBS1.
DR   RefSeq; NP_390149.1; NC_000964.3.
DR   ProteinModelPortal; P03963; -.
DR   SMR; P03963; 25-494.
DR   EnsemblBacteria; EBBACT00000001242; EBBACP00000001242; EBBACG00000001240.
DR   GeneID; 939008; -.
DR   GenomeReviews; AL009126_GR; BSU22680.
DR   KEGG; bsu:BSU22680; -.
DR   NMPDR; fig|224308.1.peg.2272; -.
DR   GenoList; BSU22680; -.
DR   GeneTree; EBGT00050000001425; -.
DR   OMA; PERLIHV; -.
DR   PhylomeDB; P03963; -.
DR   ProtClustDB; PRK13569; -.
DR   BioCyc; BSUB:BSU22680-MON; -.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR005256; Anth_synth_I_PabB.
DR   InterPro; IPR015890; Chorismate-bd_C.
DR   Gene3D; G3DSA:3.60.120.10; TRPE_1_chor_bd; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; TRPE_1_chor_bd; 1.
DR   TIGRFAMs; TIGR00564; TrpE_most; 1.
DR   HOGENOMDNA; BASUB1_1.PE2318; -.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Reference proteome; Tryptophan biosynthesis.
SQ   SEQUENCE   515 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNFQSNISAF LEDSLSHHTI PIVETFTVDT LTPIQMIEKL DREITYLLES KDDTSTWSRY
     SFIGLNPFLT IKEEQGRFSA ADQDSKSLYT GNELKEVLNW MNTTYKIKTP ELGIPFVGGA
     VGYLSYDMIP LIEPSVPSHT KETDMEKCML FVCRTLIAYD HETKNVHFIQ YARLTGEETK
     NEKMDVFHQN HLELQNLIEK MMDQKNIKEL FLSADSYKTP SFETVSSNYE KSAFMADVEK
     IKSYIKAGDI FQGVLSQKFE VPIKADAFEL YRVLRIVNPS PYMYYMKLLD REIVGSSPER
     LIHVQDGHLE IHPIAGTRKR GADKAEDERL KVELMKDEKE KAEHYMLVDL ARNDIGRVAE
     YGSVSVPEFT KIVSFSHVMH IISVVTGRLK KGVHPVDALM SAFPAGTLTG APKIRAMQLL
     QELEPTPRET YGGCIAYIGF DGNIDSCITI RTMSVKNGVA SIQAGAGIVA DSVPEAEYEE
     SCNKAGALLK TIHIAEDMFH SKEDKADEQI STIVR
//

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