ID J1RJM7_9ACTN Unreviewed; 656 AA.
AC J1RJM7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN ORFNames=SU9_008485 {ECO:0000313|EMBL:QTZ91511.1}, SU9_23025
GN {ECO:0000313|EMBL:EJJ04589.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ04589.1};
RN [1] {ECO:0000313|EMBL:EJJ04589.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ04589.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ91511.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ91511.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) 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; AJGV01000139; EJJ04589.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ91511.1; -; Genomic_DNA.
DR RefSeq; WP_006606118.1; NZ_CP072931.1.
DR AlphaFoldDB; J1RJM7; -.
DR STRING; 1160718.SU9_23025; -.
DR KEGG; sauh:SU9_008485; -.
DR PATRIC; fig|1160718.3.peg.4655; -.
DR eggNOG; COG0147; Bacteria.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_028026_0_0_11; -.
DR OrthoDB; 8594609at2; -.
DR Proteomes; UP000009036; Chromosome.
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:UP000009036}.
FT DOMAIN 131..402
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 466..649
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 549
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 634
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 636
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 656 AA; 70036 MW; E922EDF00880C86C CRC64;
MHREPPAATD AAALVGRLLD PACPPFALLR RRSPGRDGTL VEVLTGEVTE VDRLADIPLG
EGVPDAPVTD ALALIPFRQI HERGFRAHDD GTPLAVLRPR ESAEVPLDEL MAALPTHDVR
VTNGAFDVDD DAYAEIVGRV VRDEIGTGEG ANFVIRRTFQ GEIADFSAAD ALALFRRLLA
GERGAYWTYV VHRPGVHTLV GASPEVHVRM SGGTVVMNPI SGTYRYPPGG PTAESLLAFL
DDRKEAEELS MVVDEELKMM CTVGDKGGVV VGPRLKEMAH LAHTEYELRG RSTLDVREVL
KETMFAATVT GSPVQNACRV IERHEPVDPD GRGRGYYAGA LALIGRAPGG GPEEGGCTRT
LDSPILIRTA DISAAGRLRV PVGATLVRAS DPYSEVAETH AKAAGVLSAL GVRPAPVRPA
DGSRPPRLAD DPRVRAALDA RRAGLAPFWL RMQTTAPVAE LSGQALVIDA EDTFTAMLAH
LLRTSGLGVT VRRFDEPGLR EAARAHRGPV VLGPGPGDPS DAADPKMRFL RSLTAELVAG
HRHGLLGVCL GHELLAAELG LEIVRKEVPF QGAQERIDFF GRQETVGFYN TFTARCDDTT
AAELAMHRVE LSRDTGTGEV HALRGPGFAG VQFHPESVLT LDGAAVTAQL LAAVLV
//
