ID A0A1Y0G498_9PROT Unreviewed; 491 AA.
AC A0A1Y0G498;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CAP31_02065 {ECO:0000313|EMBL:ARU30582.1};
OS Sulfuriferula sp. AH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuriferula.
OX NCBI_TaxID=1985873 {ECO:0000313|EMBL:ARU30582.1, ECO:0000313|Proteomes:UP000195558};
RN [1] {ECO:0000313|EMBL:ARU30582.1, ECO:0000313|Proteomes:UP000195558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH1 {ECO:0000313|EMBL:ARU30582.1,
RC ECO:0000313|Proteomes:UP000195558};
RA Jones D.S., Hua A.A., Roepke E.W., Bailey J.V.;
RT "The complete genome sequence of Sulfuriferula sp. str. AH1, a sulfur-
RT oxidizing autotroph isolated from weathered sulfide-bearing rock from the
RT Duluth Complex.";
RL Submitted (MAY-2017) 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; CP021138; ARU30582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0G498; -.
DR KEGG; sulf:CAP31_02065; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000195558; 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 Reference proteome {ECO:0000313|Proteomes:UP000195558};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 26..169
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 219..471
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 491 AA; 53556 MW; E36AA4C0126B9037 CRC64;
MTEQQFFELA RQGYNRIPLT RELPADLDTP LAVYLKLANA PYSYLLESVV GGEQFGRYSF
IGLPAHTVLR VHGHVVTIET DGVKVEQHDS ADPLSFIESV LKRYRAADLP GLPRFDGGLA
GYFGYDTVRY IEKRLADTHK NDTLHTPDSL LLLTEELVVV DNLSSSLTLI VYVDPLEPDA
YSKGYVRLNQ LTAQLRAPLA APHTEAIAPA EVVSEFGEDA FKAAVSRAQE YILAGDIMQV
VLSQRMSRPF NASPLTLYRA LRSLNPSPYM FYYDMGGFHV VGASPEILVR LEDDTVTVRP
IAGTRPRGAS RESDAALATE LLADPKECAE HLQLLDLGRN DAGRVAITGS VKVTENMQIE
RYSHVMHIVS NVEGKLKPGL SAMDVLRATF PAGTVSGAPK VRAMEIIDEL EPSKRGIYAG
AVGYLSFNGA MDLAIAIRTA VIKDNMLYVQ AGAGIVADSI PENEWIETQN KARAVIRAAE
LAQAGLEGAG E
//
