(data stored in ACNUC7421 zone)

SWISSPROT: C1ATY1_RHOOB

ID   C1ATY1_RHOOB            Unreviewed;       532 AA.
AC   C1ATY1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   05-JUL-2017, entry version 48.
DE   RecName: Full=Anthranilate synthase component 1 {ECO:0000256|RuleBase:RU364045};
DE            EC=4.1.3.27 {ECO:0000256|RuleBase:RU364045};
GN   Name=trpE {ECO:0000256|RuleBase:RU364045,
GN   ECO:0000313|EMBL:BAH48989.1};
GN   OrderedLocusNames=ROP_07420 {ECO:0000313|EMBL:BAH48989.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48989.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48989.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48989.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the
CC       two-step biosynthesis of anthranilate, an intermediate in the
CC       biosynthesis of L-tryptophan. In the first step, the glutamine-
CC       binding beta subunit (TrpG) of anthranilate synthase (AS) provides
CC       the glutamine amidotransferase activity which generates ammonia as
CC       a substrate that, along with chorismate, is used in the second
CC       step, catalyzed by the large alpha subunit of AS (TrpE) to produce
CC       anthranilate. In the absence of TrpG, TrpE can synthesize
CC       anthranilate directly from chorismate and high concentrations of
CC       ammonia. {ECO:0000256|RuleBase:RU364045}.
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC       pyruvate + L-glutamate. {ECO:0000256|RuleBase:RU364045}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364045};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC       {ECO:0000256|RuleBase:RU364045}.
CC   -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits:
CC       a beta subunit (TrpG) and a large alpha subunit (TrpE).
CC       {ECO:0000256|RuleBase:RU364045}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I
CC       family. {ECO:0000256|RuleBase:RU364045}.
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DR   EMBL; AP011115; BAH48989.1; -; Genomic_DNA.
DR   ProteinModelPortal; C1ATY1; -.
DR   STRING; 632772.ROP_07420; -.
DR   EnsemblBacteria; BAH48989; BAH48989; ROP_07420.
DR   KEGG; rop:ROP_07420; -.
DR   PATRIC; fig|632772.20.peg.805; -.
DR   eggNOG; ENOG4105CRQ; Bacteria.
DR   eggNOG; COG0147; LUCA.
DR   HOGENOM; HOG000025142; -.
DR   KO; K01657; -.
DR   OMA; IAGTFKR; -.
DR   OrthoDB; POG091H01VQ; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.120.10; -; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR005256; Anth_synth_I_PabB.
DR   InterPro; IPR015890; Chorismate_C.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   TIGRFAMs; TIGR00564; trpE_most; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ATY1.
DR   SWISS-2DPAGE; C1ATY1.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU364045};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU364045};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Lyase {ECO:0000256|RuleBase:RU364045, ECO:0000313|EMBL:BAH48989.1};
KW   Magnesium {ECO:0000256|RuleBase:RU364045};
KW   Metal-binding {ECO:0000256|RuleBase:RU364045};
KW   Tryptophan biosynthesis {ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN       54    195       Anth_synt_I_N. {ECO:0000259|Pfam:
FT                                PF04715}.
FT   DOMAIN      252    510       Chorismate_bind. {ECO:0000259|Pfam:
FT                                PF00425}.
SQ   SEQUENCE   532 AA;  56663 MW;  E0B798817618A4E6 CRC64;
     MMVGMHGEPT TIPAPESAAT PADGGSDSTT TREQFHALAA EHRVVPVTRK VLADAETPLS
     AYTKLAANRP GTFLLESAEN GRSWSRWSFI GAGSPAALTV VDGEAAWYGN VPAGAPSGGD
     PIAALGQTLE LLRSERLPDL PPLTGGMVGF LGYDAVRRIE RIGEHATDDL QIPEMVMLLA
     TDLAAVDHHE GAITLIANAV NWDGTDERVD EAYDSAVERL DRMTRALSAP ASSTVSTFAK
     PAPDYRRQRT TEGFGADVQK LVGDIEAGEA FQVVLSQRFE IDCTADPIDV YRMLRASNPS
     PYMYLLNVPD GDGETAFSIV GSSPEALVTV SEGVATTHPI AGTRWRGHTE EEDILLEKDL
     LADEKENAEH LMLVDLGRND LGRVCEPGTV KVHDYRHIER YSHVMHLVST VTGHLADGKQ
     ALDAVTACFP AGTLSGAPKV RAMQLIEELE PTRRGIYGGI IGYLDFAGDA DTAIAIRTAL
     IKDGIGYVQA GAGVVADSNP EYEDTEARNK AMAVLSAIAA AHTLKTLGGG TQ
//

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