ID A0A1I5V608_9PSEU Unreviewed; 692 AA.
AC A0A1I5V608;
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=SAMN05421810_104243 {ECO:0000313|EMBL:SFQ02822.1};
OS Amycolatopsis arida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=587909 {ECO:0000313|EMBL:SFQ02822.1, ECO:0000313|Proteomes:UP000198727};
RN [1] {ECO:0000313|Proteomes:UP000198727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5579 {ECO:0000313|Proteomes:UP000198727};
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; FOWW01000004; SFQ02822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5V608; -.
DR STRING; 587909.SAMN05421810_104243; -.
DR OrthoDB; 8594609at2; -.
DR Proteomes; UP000198727; 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:UP000198727}.
FT DOMAIN 140..398
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 501..679
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 408..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 581
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 665
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 692 AA; 72967 MW; 6FD3BAEB04146626 CRC64;
MTISTVRDTA TVEARELMAD LLAPDPPAFA LLCRSTGAAP AAGESTMEES TVELVAGEAV
ELTALADLPL PAAGTAAGEV LAVVPFRQIT ERGYACHDDG APILALTADR RAGLPVPDAL
ELLPDVEVSV SGGGFDLPDD EYARVVRRIV DGEIRAGEGS NFVIRRTFTA TLDGYRPAVA
MTIFRRLLTA ESNAYWTFLV HTGDRTFVGA SPEQHVRSSG GVVRMNPISG TYRYPPSGAD
PRGVLDFLAD QKEIDELYMV VDEELKMLAG VCRGGARVRG PYLREMARLA HTEYVLEGPC
ARDAREVLRE TMFAPTVVGS PLENACRVIA RHEAGGRGYY AGALALLGRD ASGSSTVDSA
ILIRTAEIHR DGALRIDVGA TLVRDSRPAA EVAETWAKVD ALLAATGVRA PNGPAGRRRT
GPDGSGSTRA PLGGRADVAA ALRRRNAGLS AFWLASPDPP EPDPAVPGSA VPGSAVPDVA
VPDVAVPDRP ASNRPVPGRV LIVDAEDMFT RMLGHQVRAL GAEVALRPWS AVAPDDVAAA
DCVLLGPGPG DPRAGGDPRI AALRGFVERL LDARVPFVAE CLSHQVLCAV LGLPLVARNR
PNQGTRHRID LFGTPELVGF YNSYAARHDA DRLTAAPGSV EVCRDTRTGE VHAVRGPGFA
SAQFHLESVL TERGAEILAG LVAWAAGTGE ER
//
