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Database: UniProt
Entry: A0A259TXZ4_9BACT
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ID   A0A259TXZ4_9BACT        Unreviewed;       516 AA.
AC   A0A259TXZ4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653, ECO:0000256|RuleBase:RU364045};
DE            EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266, ECO:0000256|RuleBase:RU364045};
GN   Name=trpE {ECO:0000256|RuleBase:RU364045};
GN   ORFNames=BSZ36_06315 {ECO:0000313|EMBL:OZC02622.1};
OS   Rubricoccus marinus.
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC   Rubricoccus.
OX   NCBI_TaxID=716817 {ECO:0000313|EMBL:OZC02622.1, ECO:0000313|Proteomes:UP000216446};
RN   [1] {ECO:0000313|EMBL:OZC02622.1, ECO:0000313|Proteomes:UP000216446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-29 {ECO:0000313|EMBL:OZC02622.1,
RC   ECO:0000313|Proteomes:UP000216446};
RA   Yoshizawa S., Kumagai Y., Kogure K.;
RT   "Study of marine rhodopsin-containing bacteria.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC       step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC       of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC       (TrpG) of anthranilate synthase (AS) provides the glutamine
CC       amidotransferase activity which generates ammonia as a substrate that,
CC       along with chorismate, is used in the second step, catalyzed by the
CC       large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC       absence of TrpG, TrpE can synthesize anthranilate directly from
CC       chorismate and high concentrations of ammonia.
CC       {ECO:0000256|RuleBase:RU364045}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC         pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359; EC=4.1.3.27;
CC         Evidence={ECO:0000256|ARBA:ARBA00000329,
CC         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. {ECO:0000256|ARBA:ARBA00004873,
CC       ECO:0000256|RuleBase:RU364045}.
CC   -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC       beta subunit (TrpG) and a large alpha subunit (TrpE).
CC       {ECO:0000256|ARBA:ARBA00011575, ECO:0000256|RuleBase:RU364045}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000256|ARBA:ARBA00009562, ECO:0000256|RuleBase:RU364045}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZC02622.1}.
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DR   EMBL; MQWB01000001; OZC02622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259TXZ4; -.
DR   InParanoid; A0A259TXZ4; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000216446; Unassembled WGS sequence.
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; Anthranilate synthase; 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   NCBIfam; TIGR00564; trpE_most; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF9; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU364045};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU364045};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU364045};
KW   Magnesium {ECO:0000256|RuleBase:RU364045};
KW   Metal-binding {ECO:0000256|RuleBase:RU364045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216446};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN          35..185
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          239..500
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
SQ   SEQUENCE   516 AA;  55376 MW;  DCA11F1D4D3A521B CRC64;
     MTFDAFQSFV SDHLPSAIAR GHRLAVPVWS RRSADLLTPV SAFLSLREPG TFGFLLESVE
     GGERLARYSF LGKRPYLVIE SRGGRSLIHR PPGAYTGDGA PHAVECVDES AFDALGAMLE
     GVDQPTVPGL PRFTGGAVGF VGYDAVRQVE AMGVGPPDLL GLPDGVWAFY DLVAAFDHVR
     HQLVLMATVF LDVETDLRSA WEEAQDRLLA LETDLTAPAA PGDPIRLLGE PSSSVERGAY
     EAAVRTAKDH ITEGDIFQVV LSQRFATPFE GDSFNLYRAL RQVNPSPYLF YVDVDGLEED
     GSQFTLVGSS PEVLARVDPR GTDRRAEVLP IAGTRPRGAT PEADQALADE LLADAKERAE
     HLMLVDLGRN DLGRVSDVGS VRLERYAQVE RYSHVMHLVS SVTGAVGERK ATDVLAACFP
     AGTVSGAPKV RAMEIIDELE PIRRGPYAGA VGYAGFDGAL DTCIAIRTFV VKDNTAYVQA
     GAGVVADSDP AAEFDETRHK AAALIQALQT ASGDLL
//
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