(data stored in ACNUC30630 zone)

HOGENOM: NEMEN1_1_PE983

ID   NEMEN1_1_PE983                       STANDARD;      PRT;   491 AA.
AC   NEMEN1_1_PE983; P56995;
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; (NEMEN1_1.PE983).
GN   Name=trpE; OrderedLocusNames=NMB1021;
OS   NEISSERIA MENINGITIDIS MC58.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEMEN1_1.PE983.
CC       Neisseria meningitidis MC58, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:TRPE_NEIMB
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; P56995; -.
DR   EMBL; AE002098; AAF41421.1; -; Genomic_DNA.
DR   PIR; E81132; E81132.
DR   RefSeq; NP_274055.1; NC_003112.2.
DR   ProteinModelPortal; P56995; -.
DR   EnsemblBacteria; EBNEIT00000009525; EBNEIP00000009145; EBNEIG00000009525.
DR   GeneID; 903159; -.
DR   GenomeReviews; AE002098_GR; NMB1021.
DR   KEGG; nme:NMB1021; -.
DR   NMPDR; fig|122586.1.peg.989; -.
DR   TIGR; NMB1021; -.
DR   GeneTree; EBGT00050000020301; -.
DR   OMA; PSQRMSM; -.
DR   ProtClustDB; PRK13565; -.
DR   BioCyc; NMEN122586:NMB_1021-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; NEMEN1_1.PE983; -.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Reference proteome; 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 AVIDNLSGKI HLVVYADPSQ
     PDGYERARER LEDIRTQLRQ SCAIPLSLGS KHTEAVSEFG EEPFKACVNK IKDYIFAGDC
     MQVVPSQRMS MEFTDSPLAL YRALRTLNPS PYLFYYDFGD FHIVGSSPEI LVRRERNDVI
     VRPIAGTRLR GKTPAEDLAN EQDLLSDAKE IAEHVMLIDL GRNDVGRISK TGEVKVTDKM
     VIEKYSHVMH IVSNVEGRLK DGMTNMDILA ATFPAGTLSG APKVRAMEII EEVEPSKRGI
     YGGAVGVWGF NNDMDLAIAI RTAVVKNNTL YVQSGAGVVA DSDPASEWQE TQNKARAVIH
     AAQMVQEGLD K
//

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