(data stored in ACNUC30630 zone)

HOGENOM: SYNY3_1_PE1643

ID   SYNY3_1_PE1643                       STANDARD;      PRT;   485 AA.
AC   SYNY3_1_PE1643; P74130;
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 I-like protein; EC=4.1.3
DE   27; (SYNY3_1.PE1643).
GN   Name=trpE2; OrderedLocusNames=slr1979;
OS   SYNECHOCYSTIS SP. PCC 6803.
OC   Bacteria; Cyanobacteria; Chroococcales; Synechocystis.
OX   NCBI_TaxID=1148;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SYNY3_1.PE1643.
CC       Synechocystis sp. PCC 6803 chromosome, complete genome.
CC       1..88329 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:TRE2_SYNY3
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   -!- CAUTION: This is a divergent form of trpE. It is not obvious if it
CC       is active in Trp biosynthesis.
CC   -!- GENE_FAMILY: HOG000025142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P74130; -.
DR   EMBL; BA000022; BAA18216.1; -; Genomic_DNA.
DR   PIR; S75655; S75655.
DR   RefSeq; NP_441536.1; NC_000911.1.
DR   ProteinModelPortal; P74130; -.
DR   STRING; P74130; -.
DR   GeneID; 951847; -.
DR   GenomeReviews; BA000022_GR; slr1979.
DR   KEGG; syn:slr1979; -.
DR   NMPDR; fig|1148.1.peg.1637; -.
DR   eggNOG; COG0147; -.
DR   OMA; DLAWEIE; -.
DR   PhylomeDB; P74130; -.
DR   ProtClustDB; PRK05940; -.
DR   BioCyc; SSP1148:SLR1979-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   InterPro; IPR010118; Para-NH2Bz/anthranilate_synth.
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; TIGR01824; PabB-clade2; 1.
DR   HOGENOMDNA; SYNY3_1.PE1643; -.
KW   anthranilate synthase component I-like-protein;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Reference proteome; Tryptophan biosynthesis.
SQ   SEQUENCE   485 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MASIAHCSGG LVGAGNFDFI LGGSDPVGRH GLMELQPWHW CCLPLEGRTG SEIFSQLFGH
     QGIATLLESP YPASPDHPHL GRYSLCAGQP RKGRLWTPKP EEIFSFLNQL CPCNHDVNLT
     KNIPEHLPFH GGWLGWLGYD TAWAIEKLPY SKADDLPFPV AYWYEPENFV ILDHQEQLLW
     LATTDQEKIK FFQTQLADKI NSVSSPQVPP LNLTYTTDQD QYETMVNQAK QYIKAGDIFQ
     ANLTLRFIAK TEQKLNSWQV YQHLQTINPS PFASYWRSPW GDVVSCSPER LVKLEGNVAQ
     TRPIAGTRAR GKNLAEDEQL LQELLVNTKE LAEHIMLVDL ERNDLGRVCT WGTVEVDELL
     AIERYSHVSH LVSNVKGILQ PDKTGVDLVK ALFPGGTITG CPKIRCLEII EELEPVRRSL
     FYGSCGYWDQ RGNLDLNILI RTLLFTSGQV TGQVGAGIVA DSDPAKEWLE SLQKAKALLA
     ALEGL
//

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