ID A0A1G9QWM4_9ACTN Unreviewed; 644 AA.
AC A0A1G9QWM4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN ORFNames=SAMN05444921_104330 {ECO:0000313|EMBL:SDM15409.1};
OS Streptomyces wuyuanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1196353 {ECO:0000313|EMBL:SDM15409.1, ECO:0000313|Proteomes:UP000199063};
RN [1] {ECO:0000313|Proteomes:UP000199063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7042 {ECO:0000313|Proteomes:UP000199063};
RA Varghese N., Submissions S.;
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|ARBA:ARBA00025634}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873}.
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}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000256|ARBA:ARBA00009562}.
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DR EMBL; FNHI01000004; SDM15409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9QWM4; -.
DR STRING; 1196353.SAMN05444921_104330; -.
DR OrthoDB; 8594609at2; -.
DR Proteomes; UP000199063; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF46; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF56322; ADC synthase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000199063}.
FT DOMAIN 113..391
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 451..632
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 534
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 618
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 644 AA; 68910 MW; 93778E89AD364165 CRC64;
MHILDRLLNP GAPPFALLRR RTPGRDHDTV EVLTGPVREV ERLADIPVGE RPSLALVPFR
QIRERGFDVR DDGTPLSVLV AEETFELPLD EVLGRLPAHG VDVEDGGFDV GDEEYAEIVR
RVVEDEIGRG EGANFVIRRT FTGRVPDFGR ADALALFRRL LTTERGAYWT YVVHTGDGRP
SSEVRDGGTG GRTLVGASPE VHVRMSGGTV VMNPISGTYR YPAGGPTVDG LLDFLSDRKE
TDELSMVVDE ELKMMCTVGD MGGVVVGPRL KEMSHLAHTE YELRGRSSLD VREVLRETMF
AATVTGSPVQ NACRVIERHE PAGRDGGGGR GYYAGALALL GVDAGGAQLL DSPILIRTAD
ISASGEVRVP VGATLVRHSD PESEVAETHA KAAGVLAALG VRPGPAREET TRPRLADDPR
VRAALDARRA DLAPFWLRMQ SLPERVTGHA LVVDGEDTFT AMLAHLLRGA GLEVTVRRYD
EPGVREAALS HAGPVVLGPG PGDPSDAADP KMRFLRSLTG ELLRGHRGGL LGVCLGHELI
AAELGLGIAR KETPFQGAQL RIGLFGAEET VGFYNSFTAV CDDGAAAELS LHGVEVGRAP
SGEVHALRGP GFAGIQFHPE SVLTLRGPEI VRGLLSSVVR ETSV
//
