ID A0A1T4KBK3_9ACTN Unreviewed; 728 AA.
AC A0A1T4KBK3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN ORFNames=SAMN02745673_00292 {ECO:0000313|EMBL:SJZ39757.1};
OS Marinactinospora thermotolerans DSM 45154.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Marinactinospora.
OX NCBI_TaxID=1122192 {ECO:0000313|EMBL:SJZ39757.1, ECO:0000313|Proteomes:UP000190637};
RN [1] {ECO:0000313|EMBL:SJZ39757.1, ECO:0000313|Proteomes:UP000190637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45154 {ECO:0000313|EMBL:SJZ39757.1,
RC ECO:0000313|Proteomes:UP000190637};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUWS01000001; SJZ39757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4KBK3; -.
DR STRING; 1122192.SAMN02745673_00292; -.
DR OrthoDB; 3518032at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000190637; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000190637};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT DOMAIN 40..199
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 245..501
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 535..712
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 211..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 610
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 704
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 706
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 728 AA; 80126 MW; F82B94B3CD10A9C5 CRC64;
MDDSSTSYHT AGGIAVRRTV RPCAPEALSE LVRSVEHRRG GVLSSGMEYP GRYSRWHLGY
VDPCLELAAR GRAVTVTALN ERGRVLLPVV AEALRAHGET VEQSPDTFGI VIPEPDVEVF
LPEEQRSRRP GVFSALREIV ALFAAEDDPH LGLYGAFGYD LAFQFEPIEQ LLHRDAADRD
LVLQLPDEII VRDRKRETCL RFSYDFTVPA GPGRDEASTD TLPRATEPTP EVVTAQTPPQ
PEPGSYARVV AEAKKRFVRG DLFEVVPSHR TYGSCSSPAR FYERLRERNP APYEFFFNLG
EGEYLVGASP EMFVRVSGRP GRGQRVETCP ISGTIRRGDD ALGDAANILE LLGSAKEESE
LTMCTDVDRN DKSRVCEPGS VRVIGRRQIE LYSRLIHTVD HIEGTLRPEF DALDAFVTHM
WAVTVTGAPK TWAMRFIEAH ESTPRRWYGG AVGVVNFDGS MNTGLTLRTA HIRDGVAAVR
VGATLLYDSD PEAEERETFL KARALLETLA EEGEDASPAT EASAPPKAGE GMRVLLVDHE
DSFVNTLADY VRRHGAQVTT LRHGFDPLLL DRLAPDLVVL SPGPGLPADF AMSALLDELY
ARDLPTFGVC LGLQGMVEHA GGELLTLAEP VHGKPSRIRV TGGRLLEGVA DPDMTFTAGR
YHSTYTTPDR VKTFEVTAVV DDGAEPVVMA IEAPESRRWA VQFHPESILT AKVGERIVEN
VLRMARRP
//
