ID A0A1H9LHQ2_9BURK Unreviewed; 499 AA.
AC A0A1H9LHQ2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN02982919_01766 {ECO:0000313|EMBL:SER10956.1};
OS Giesbergeria anulus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Giesbergeria.
OX NCBI_TaxID=180197 {ECO:0000313|EMBL:SER10956.1, ECO:0000313|Proteomes:UP000199766};
RN [1] {ECO:0000313|EMBL:SER10956.1, ECO:0000313|Proteomes:UP000199766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35958 {ECO:0000313|EMBL:SER10956.1,
RC ECO:0000313|Proteomes:UP000199766};
RA de Groot N.N.;
RL Submitted (OCT-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|ARBA:ARBA00001946,
CC 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}.
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DR EMBL; FOGD01000004; SER10956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9LHQ2; -.
DR STRING; 180197.SAMN02982919_01766; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000199766; 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:SF48; ISOCHORISMATE SYNTHASE MENF; 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|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364045};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364045};
KW Reference proteome {ECO:0000313|Proteomes:UP000199766};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 27..175
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 226..483
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 499 AA; 54473 MW; C93A1C94F55CCC03 CRC64;
MITESEFHHL AQQGYNRIPL MAQAFADLET PLSLYFKLAH SQAGGQHSFL LESVVGGERF
GRYSFIGLPA HTLVRASGFG AAARTEVVTD GVVVETATGN PLDFIASYQQ RFKVALLPGL
PRFCGGLAGY FGYDAVRYIE KKLEATCPPD TLGCPDILLL QCEELAVIDN LSGKLSLIVY
ADPTQPEAYA QAQQRLRQLK ERLQAPVVAP VVQASTSHPA QRSFAKDDYL AAVAHAKELI
AAGDFMQVQV GQRIHKTYTE SPLSLYRALR SLNPSPYMYF YNFGDFQVVG SSPEILVRQE
QTPEGQKVTI RPLAGTRPRG ATPEQDKAAE LELINDPKER AEHVMLIDLA RNDIGRIAQI
GSVKVTEAFV VERYSHVMHI VSNVEGILNE GMTSMDVLKA TFPAGTLTGA PKVHAMELID
QLEPSKRGIY GGACGYLSYA GNMDLAIAIR TGLIKDGTLY VQAAAGVVAD SVPELEWKET
EHKARALLRA AELVEEGLE
//
