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Database: UniProt
Entry: A0A429G4B5_9ACTN
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Original site: A0A429G4B5_9ACTN 
ID   A0A429G4B5_9ACTN        Unreviewed;       720 AA.
AC   A0A429G4B5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE            EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN   ORFNames=DMH08_10235 {ECO:0000313|EMBL:RSN68691.1};
OS   Actinomadura sp. WAC 06369.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2203193 {ECO:0000313|EMBL:RSN68691.1, ECO:0000313|Proteomes:UP000288610};
RN   [1] {ECO:0000313|EMBL:RSN68691.1, ECO:0000313|Proteomes:UP000288610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 06369 {ECO:0000313|EMBL:RSN68691.1,
RC   ECO:0000313|Proteomes:UP000288610};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) 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|PIRNR:PIRNR036934};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5. {ECO:0000256|PIRNR:PIRNR036934}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RSN68691.1}.
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DR   EMBL; QHJN01000027; RSN68691.1; -; Genomic_DNA.
DR   RefSeq; WP_026406189.1; NZ_QHJN01000027.1.
DR   AlphaFoldDB; A0A429G4B5; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000288610; Unassembled WGS sequence.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic 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; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010112; TrpE-G_bact.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR01815; TrpE-clade3; 1.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF9; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PIRSF; PIRSF036934; TrpE-G; 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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036934};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036934};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Lyase {ECO:0000256|PIRNR:PIRNR036934, ECO:0000313|EMBL:RSN68691.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288610};
KW   Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT   DOMAIN          39..203
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          246..496
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   DOMAIN          534..706
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          218..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        609
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        696
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        698
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   720 AA;  78601 MW;  6193FD66DD0CAE3B CRC64;
     METVSQQPTT GEFVTAGGVR VTRTAAPVDP ERKSDVLNAL VAAVGERRGG VLSSGMEYPG
     RYSRWHMAYV DPCLEIVARG RTVAARALNG RGRVVLPAVA EVLRGTGEVR ADGPGECAVF
     VPPTEEFFPE EERSRQPTVF TALRAVVDLF RCDDPHLGLY GAFGYDLSLQ FEPLRPRLER
     PDDQRDLVLH LADEMVVVDR KRETSHRISY DFEVGGTATA GLPRDTEPTP PVVPAELPPQ
     PVPGVYAQMV RDAKERFVRG DLFEVTPGHA MHGRCDSPAA FFERLRETNP APYEFLFNLG
     DGEYLVGASP EMFVRVTGDR VETCPIAGTI KRGGDALQDA EQIRTILASA KDESELTMCT
     DVDRNDKSRV CVPGSVRVLG RRQIEMYSRL IHTVDHIEGR LRPEFDALDA FLTHMWAVTV
     TGAPKTWAMQ FIEDHEDSPR RWYGGAVGFV GFDGSMNTGL TLRTAQIRDG VATVRAGATL
     LYDSDPDEEE RETHLKASAL LGALAATARD GAEPEADREP EPAPERPGDG LKVLLVDHED
     SFVNTLADYF RQHGAGVVTL RHGFPARLLD EHAPDLVVLS PGPGRPDDFA TRDLLDALDA
     RGLPVFGVCL GLQAMVEHAG GSLDLLPEPS HGKPGQVKVT GGGLFEGLPD EFTAARYHSL
     HATPDRVRGF QVTATTGDVV MAIENAERRR WAVQFHPESI LTAAGGAGHR IVANVLRLCR
//
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