(data stored in ACNUC30630 zone)

HOGENOM: NEIMF_1_PE921

ID   NEIMF_1_PE921                        STANDARD;      PRT;   491 AA.
AC   NEIMF_1_PE921; Q9S358; A1KTT8;
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; (NEIMF_1.PE921).
GN   Name=trpE; OrderedLocusNames=NMC1013;
OS   NEISSERIA MENINGITIDIS FAM18.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEIMF_1.PE921.
CC       Neisseria meningitidis FAM18, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:TRPE_NEIMF
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   -!- GENE_FAMILY: HOG000025142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q9S358; A1KTT8; -.
DR   EMBL; AJ242842; CAB44980.1; -; Genomic_DNA.
DR   EMBL; AM421808; CAM10278.1; -; Genomic_DNA.
DR   RefSeq; YP_975067.1; NC_008767.1.
DR   ProteinModelPortal; Q9S358; -.
DR   STRING; Q9S358; -.
DR   EnsemblBacteria; EBNEIT00000007651; EBNEIP00000007420; EBNEIG00000007651.
DR   GeneID; 4675564; -.
DR   GenomeReviews; AM421808_GR; NMC1013.
DR   KEGG; nmc:NMC1013; -.
DR   NMPDR; fig|487.2.peg.2042; -.
DR   eggNOG; COG0147; -.
DR   GeneTree; EBGT00050000020301; -.
DR   OMA; PSQRMSM; -.
DR   PhylomeDB; Q9S358; -.
DR   ProtClustDB; PRK13565; -.
DR   BioCyc; NMEN272831:NMC1013-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; NEIMF_1.PE921; -.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Tryptophan biosynthesis.
SQ   SEQUENCE   491 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MISKQEYQAQ AAQGYNRIPL VQELLADLDT PLSLYLKLAN RPYTYLLESV VGGERFGRYS
     FIGLPCSHYL KASGKHVDVY QNGEIVEQHD GNPLPFIEAF HNRFKTPEIP SLPRFTGGLV
     GYFGYETIYN FEHFAHRLKN TTKADPLGTP DILLMLSQEL AVVDNLSGKI YLIVYADPSQ
     PDGYERARER LEDIRTQLRQ SCAIPLSLGS KHTEAVSEFG EEPFKACVNK IKDYIFAGDC
     MQVVPSQRMS MEFTDSSLAL YRALRTLNPS PYLFYYDFGD FHIVGSSPEI LVRRERDDVI
     VRPIAGTRLR GKTPAEDLAN EQDLLSDAKE IAEHVMLIDL GRNDVGRISK TGEVKVTDKM
     VIEKYSHVMH IVSNVEGRLK DGMTNMDILA ATFPAGTLSG APKVRAMEII EEVEPSKRGI
     YGGAVGVWGF NNDMDLAIAI RTAVVKNNTL YVQSGAGVVA DSDPASEWQE TQNKARAVIH
     AAQMVQEGLD K
//

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