ID A0A097H0X2_9ACTN Unreviewed; 671 AA.
AC A0A097H0X2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=anthranilate synthase {ECO:0000256|ARBA:ARBA00012266};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN Name=cnq728 {ECO:0000313|EMBL:AIT42118.1};
GN ORFNames=AA958_30775 {ECO:0000313|EMBL:AKH85871.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AIT42118.1};
RN [1] {ECO:0000313|EMBL:AIT42118.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AIT42118.1};
RX PubMed=25224759;
RA Zeyhle P., Bauer J.S., Steimle M., Leipoldt F., Rosch M., Kalinowski J.,
RA Gross H., Heide L.;
RT "A Membrane-Bound Prenyltransferase Catalyzes the O-Prenylation of 1,6-
RT Dihydroxyphenazine in the Marine Bacterium Streptomyces sp. CNQ-509.";
RL ChemBioChem 15:2385-2392(2014).
RN [2] {ECO:0000313|EMBL:AKH85871.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH85871.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KJ451627; AIT42118.1; -; Genomic_DNA.
DR EMBL; CP011492; AKH85871.1; -; Genomic_DNA.
DR RefSeq; WP_047019099.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A097H0X2; -.
DR STRING; 444103.AA958_30775; -.
DR KEGG; strc:AA958_30775; -.
DR PATRIC; fig|444103.5.peg.6505; -.
DR OrthoDB; 8594609at2; -.
DR Proteomes; UP000034283; Chromosome.
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:SF49; 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 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283}.
FT DOMAIN 136..395
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 485..665
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 408..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 563
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 648
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 650
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 671 AA; 70780 MW; A3E5704C2E54AB1F CRC64;
MTTAPGSRRS AAAGAALLDR LLAGPLPPAY ALLHRPESGT PGTVDVLLGD VTHPATLAGL
PLPDQGAEPP AATAHRTLLV VPYRQLTERG FAAPDDGAPL IAMNVTEQAA VPLDDTLARL
PDTPAALTGH RFDLSDEEYA DVVRRVVTGE IGTGEGANFV IKRTLLADVG DDPARAALTV
FRRLIALEPS AYWTFAIHAD GRTFVGATPE RHLSVHEGRA VMNPISGTYR YPAGGPTLDG
LTAFLRDRKE TDELYMVLDE ELKMMSRICP AGGRVTGPAL KEMARLAHTE YFIEGHTTRD
IRDVLRETLF APTVTGSPLE SAARVIARHE PHGRGYYSGI AALVSDEPTG SRNLDSAILI
RTADIADDGR LALSVGATLV RHSSPEGEAA ETRAKAAALL DALGADGTAD TAADPARTPA
TAAADAAPAA EPGAAGTAPR PPGFADHPAV RDVLRGRNTG IADFWLAATA ARPLTVPALE
GMKVLVVDAE DTFTAMMVQQ LEALGPTAEV RRFDEPYAVD GFDLVVMGPG PGDPRATADP
KIAALDTAVA GLLRDRTPFL AVCLSHQVLS LRLGLDLVRR DRPNQGVQRA IDLFGRREHV
GYYNTFAAVS PADALDVPGV GRVRVSRDPA TGQIDALRGP HFASYQFHAE SVLTVEGPRL
IGDALLGAIG R
//