(data stored in ACNUC30630 zone)

HOGENOM: HAMAR1_7_PE297

ID   HAMAR1_7_PE297                       STANDARD;      PRT;   523 AA.
AC   HAMAR1_7_PE297; Q5V631;
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 3; EC=4.1.3 27;AltName:
DE   Full=Anthranilate synthase component I 3; (HAMAR1_7.PE297).
GN   Name=trpE3; OrderedLocusNames=pNG7327;
OS   HALOARCULA MARISMORTUI ATCC 43049.
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales; Halobacteriaceae;
OC   Haloarcula.
OX   NCBI_TaxID=272569;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HAMAR1_7.PE297.
CC       Haloarcula marismortui ATCC 43049 plasmid pNG700, complete sequence.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:TRPE3_HALMA
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=AAV45021.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000025142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5V631; -.
DR   EMBL; AY596296; AAV45021.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_134727.1; NC_006395.1.
DR   ProteinModelPortal; Q5V631; -.
DR   GeneID; 3127203; -.
DR   GenomeReviews; AY596296_GR; pNG7327.
DR   KEGG; hma:pNG7327; -.
DR   NMPDR; fig|272569.1.peg.3517; -.
DR   ProtClustDB; CLSK511064; -.
DR   BioCyc; HMAR272569:PNG7327-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; 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   HOGENOMDNA; HAMAR1_7.PE297; -.
KW   anthranilate synthase component I;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Plasmid; Tryptophan biosynthesis.
SQ   SEQUENCE   523 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLGLHNHTGR QGLSLRSNCT MTEIRFSTDK ESFIETARAA ADGTRVPVEA RVTVADPFEA
     YRRARDENTD GFYLETTGGQ SGWGYFGIEP IERVEVSAGA TPAQDGGSPS LEAIDDLLDR
     EHLERGDCTV PYPCGAFGWL SYDVARELED IPETTVSDGL PRLQFGVFDC IAAWEEPHDG
     NVEIHVTACP TVDGSPESAF ERGRTMAREL AQDAIHGEKH VQSQPTAASQ ATFESECGEA
     AFADRVRQIK QYVRDGDTFQ TNVSHRLTAP AAVHPVDTFD AVRRVNPAPY SALLEFPGVD
     LVSASPELLL DVDGDQLLTE PIAGTRPRGA TPSEDEDLEV DLCSDEKERA EHAMLVDLER
     NDLGKVSEYG SVDVAEYRRV DRYSEVMHLV SLIEGELRDA VSIADAVAAV FPGGTITGAP
     KPRTMEIIDE VERTRRGPYT GSIGMFGFDD RATLNITIRT LVHYDDEYRL RVGSGIVHDS
     VPEAEYRETL DKARALVTAV DEALGEQGSF AVESETEPME GMR
//

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