ID A0A1H7T963_9ACTN Unreviewed; 709 AA.
AC A0A1H7T963;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN ORFNames=SAMN05660976_03397 {ECO:0000313|EMBL:SEL81283.1};
OS Nonomuraea pusilla.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=46177 {ECO:0000313|EMBL:SEL81283.1, ECO:0000313|Proteomes:UP000198953};
RN [1] {ECO:0000313|EMBL:SEL81283.1, ECO:0000313|Proteomes:UP000198953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43357 {ECO:0000313|EMBL:SEL81283.1,
RC ECO:0000313|Proteomes:UP000198953};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOBF01000007; SEL81283.1; -; Genomic_DNA.
DR RefSeq; WP_055502512.1; NZ_FOBF01000007.1.
DR AlphaFoldDB; A0A1H7T963; -.
DR STRING; 46177.SAMN05660976_03397; -.
DR OrthoDB; 3518032at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000198953; 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 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:UP000198953};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT DOMAIN 103..194
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 236..487
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 520..694
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 595
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 684
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 686
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 709 AA; 77657 MW; B9303142C18F8C28 CRC64;
METSGYTTAG GIKVEREARD VPEAALEEIV TALGERRGGA FSSGMDYPGR YSRWAFGYVD
PCLELVAKGR VIAATALNER GRVLLPAVAS CLLAAGKPVS PPTAERVEVY VPEPGDDHLP
EEMRSRRPTV FTAIREVIAA FRGDDPHLGL YGAFGYDLAF QFEPIRQELV RPDDQRDLVL
HLPDRLVVID RQRETSVEYR YEFTVDGATT RGLERTGSSV PQVTPTDIPE NPVRGEYAKV
VAAAKERFKR GDLFEVVPGQ VFHAVCTDPS AFYRGLRHSN PAPYEFIISL GEGEHLVGAS
PEMYVRVTGD RVETCPISGT IARGSNPVED AEAIRTLLTS VKEESELTMC TDVDRNDKSR
ICVPGSVRVI GRRQIELYSR LIHTVDHIEG RLRPEFDALD AFLTHMWAVT VTGAPKTWAM
QFIEDHEATT RRWYGGAIGF IGFDGSMNTG LTLRTAQIKN GVAAVRAGAT LLFDSDPEAE
ERETELKASA LLGALAAVNQ PQERPVAEVR PQAGVGMKVL LVDHEDSFVN TLADYFRQEG
AEVVTLRHGF PVHLIDEIAP DLVVLSPGPG WPSDFGMSAL IDEVYARDLP VFGVCLGLQA
MVEHAGGTLE LLGYPEHGKR GQVSRLGESA LLDGLPEQFT AARYHSLHAK RPGVVGFTAT
ALTPDGNVMA IEDPERRRFA VQFHPESILT QEGGAGARII ANVLRLCRR
//
