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Database: UniProt
Entry: A0A097H0X2_9ACTN
LinkDB: A0A097H0X2_9ACTN
Original site: A0A097H0X2_9ACTN 
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
//
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