ID A0A1N7ETH2_9ACTN Unreviewed; 635 AA.
AC A0A1N7ETH2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN ORFNames=SAMN05444858_12720 {ECO:0000313|EMBL:SIR91366.1};
OS Micromonospora avicenniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1198245 {ECO:0000313|EMBL:SIR91366.1, ECO:0000313|Proteomes:UP000186004};
RN [1] {ECO:0000313|EMBL:SIR91366.1, ECO:0000313|Proteomes:UP000186004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45758 {ECO:0000313|EMBL:SIR91366.1,
RC ECO:0000313|Proteomes:UP000186004};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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|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; FTNF01000027; SIR91366.1; -; Genomic_DNA.
DR RefSeq; WP_076473629.1; NZ_FTNF01000027.1.
DR AlphaFoldDB; A0A1N7ETH2; -.
DR STRING; 1198245.SAMN05444858_12720; -.
DR OrthoDB; 8594609at2; -.
DR Proteomes; UP000186004; 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; PR00099; CPSGATASE.
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:UP000186004}.
FT DOMAIN 117..376
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 442..619
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 520
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 604
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 606
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 635 AA; 67315 MW; CA3A02BD881D3156 CRC64;
MIHLNDLLTT VSAGADPGPF ALVRRADADQ LELFTGPVRT VDRLADIPLP EGASGPRTLA
LVPFRQITER GFACVDDGMP LECLLVTRHE RIGLAEALAA LPDQPVRASD AAFDVTDEEY
AAAVDRVLAE EIGRGEGANF VIHRTLTATV QDPPLVAALA ALRRLLLGER GAYWTFVVYT
GDRVLVGASP ERHVSVDDGL VMMNPISGTF RHAGAEPDRA ALLRFLADQK EVEELYMVLD
EELKMMATVA EDGGQVVGPY LKEMSHLAHT EYLLAGRGTR DVRDVLRETM FAPTVTGSPM
ENACRVIARH ERTGRRYYAG VLALLGHDDA GRQTLDAPIL IRTAEISPDG ALRVSVGATL
VRHSTAAGEV AETHAKAAGV LAALGLGPQA ARAGREAPPR LADDPDVRAA LAARNAPLAR
FWLDQRAPGV GALPALAGRS ALVVDAEDTF TGMLTHQLRA LGLAVTVRPW HAPGPFDGYD
LVVVGPGPGD PGSTTEPKMR ALRGLLAGLL AAGHPTLAVC LGHQLLAGLL GLPLHQRDAP
YQGLQREIDV FGTPRRVGFY ATFTARAGAD ALDTSYGRVE LARDAADGAV HALRGPAFAG
VQFHPESVLS PDGIAVLADL LPAVLSTADR FEPTA
//
