(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBW7_SEGRD

ID   D6ZBW7_SEGRD            Unreviewed;       521 AA.
AC   D6ZBW7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 41.
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   OrderedLocusNames=Srot_0457 {ECO:0000313|EMBL:ADG96944.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96944.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96944.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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:
CC       Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-
CC         glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27;
CC         Evidence={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; CP001958; ADG96944.1; -; Genomic_DNA.
DR   RefSeq; WP_013137400.1; NC_014168.1.
DR   STRING; 640132.Srot_0457; -.
DR   EnsemblBacteria; ADG96944; ADG96944; Srot_0457.
DR   KEGG; srt:Srot_0457; -.
DR   eggNOG; ENOG4105CRQ; Bacteria.
DR   eggNOG; COG0147; LUCA.
DR   HOGENOM; HOG000025142; -.
DR   KO; K01657; -.
DR   OMA; IAGTFKR; -.
DR   OrthoDB; 1786019at2; -.
DR   BioCyc; SROT640132:G1GLH-457-MONOMER; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000002247; 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; D6ZBW7.
DR   SWISS-2DPAGE; D6ZBW7.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU364045};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU364045};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Lyase {ECO:0000256|RuleBase:RU364045, ECO:0000313|EMBL:ADG96944.1};
KW   Magnesium {ECO:0000256|RuleBase:RU364045};
KW   Metal-binding {ECO:0000256|RuleBase:RU364045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Tryptophan biosynthesis {ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN       39    180       Anth_synt_I_N. {ECO:0000259|Pfam:
FT                                PF04715}.
FT   DOMAIN      241    500       Chorismate_bind. {ECO:0000259|Pfam:
FT                                PF00425}.
SQ   SEQUENCE   521 AA;  55828 MW;  A904BF10B0BBDBA0 CRC64;
     MTVRALTGNA PSNTTTRAEF EALAQGRRVV PVARRLLADA ETPVSAFRKL AGERAGTFLL
     ESAEQGKMWS QWSFIGVRTG ATLTSAGERA VWRGTPPAGV PVEGSPLAVL DQTVRALATD
     PVPGLPPLTS GLVGYLGYDA VRWVEQLPER THDDLRLPTM TMLLVTDLAV FDHRANVITL
     IANAFLPASS ATAPDQAGLD ALYAEALARL DAMTADLAAH APSTVSVFDW PTPDFSSQLT
     EEEYGQNVRK VVAEIEAGEA FQVVPSQRYS MPVHADPLDV YRVLRVNNPS SHMYLMRVPA
     ETGETAFHIV GSSPEALLTA RGRTVTTRPI AGTQPRGRTN EDDVLFEKKL TDDPKEQAEH
     LMLVDLGRND LGRVCVPGSV RVAEFRVLER YSHVMHLVST VSGELAPGKT ALDAVLACFP
     AGTLSGAPKV RAMEIIEEVE ITRRGLYGGV VGYFDFAGEA DTAIAIRTAV VKDGVAYVQA
     GGGVVLDSDP SSEYRESRNK ANTVLSAIAA AQTMRSPNEA G
//

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