ID A0A290Q8B0_9LACT Unreviewed; 458 AA.
AC A0A290Q8B0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ECO:0000313|EMBL:QIW54165.1};
GN ORFNames=GU336_08440 {ECO:0000313|EMBL:QIW54165.1};
OS Lactococcus raffinolactis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1366 {ECO:0000313|EMBL:QIW54165.1, ECO:0000313|Proteomes:UP000501945};
RN [1] {ECO:0000313|EMBL:QIW54165.1, ECO:0000313|Proteomes:UP000501945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lr_19_5 {ECO:0000313|EMBL:QIW54165.1,
RC ECO:0000313|Proteomes:UP000501945};
RA Ybazeta G., Ross M., Brabant-Kirwan D., Saleh M., Dillon J.A., Splinter K.,
RA Nokhbeh R.;
RT "Whole genome sequences of Lactococcus raffinolactis strains isolated from
RT sewage.";
RL Submitted (DEC-2019) 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|ARBA:ARBA00025634, 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; CP047616; QIW54165.1; -; Genomic_DNA.
DR STRING; 1348633.GCA_001591765_00431; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000501945; 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; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
SQ SEQUENCE 458 AA; 51049 MW; 10A4B10080C684CF CRC64;
MTLKKTVNAD IITPILAYLR LELKHKLILE SIPREKENSR YSMIAYNPVH EIKFENGVLT
DNGQVKTGDP LDYLGELTVK NTEASSLPFT GGAIGFVSYD TISFYEYIGE IPEDVIGTPD
LHFFLYESYL IFDHKKEQIT IVESDIYSGR SELDQELAMA LVLSNLTRPH KNEFETVKLN
PLSFTSNTAK AEFMGMVEQA QTYIKNGDMF QIVLSQRLTS QITGNPFDYY RNLRLTNPSN
YLYFLDFGDY QIMGASPESL VSVKNGVVTT NPIAGTRPRG ADEAEDDALS KDLLGDQKEV
AEHRMLVDLG RNDIGKISKV GTVKVTKYME VEYFRYVMHL TSVVKGELLD SVSSLDALKS
TLPAGTVSGA PKIRAMQRIY ELEKTKRGIY AGAIGYLSSN SDMDFAIALR TMVLKDGKAH
AQAGAGIVFD SVPENEYQET LNKAKAMTKI GESNDFIS
//
