ID A0A0C5WQE6_9GAMM Unreviewed; 527 AA.
AC A0A0C5WQE6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|PIRNR:PIRNR001373};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001373};
GN ORFNames=H744_2c2712 {ECO:0000313|EMBL:AJR09368.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR09368.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR09368.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR09368.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) 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,
CC ECO:0000256|PIRNR:PIRNR001373};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR001373-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR001373-2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|PIRNR:PIRNR001373}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000256|ARBA:ARBA00009562, ECO:0000256|PIRNR:PIRNR001373}.
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DR EMBL; CP005974; AJR09368.1; -; Genomic_DNA.
DR RefSeq; WP_044623867.1; NZ_CP005974.1.
DR AlphaFoldDB; A0A0C5WQE6; -.
DR STRING; 658445.H744_2c2712; -.
DR KEGG; pgb:H744_2c2712; -.
DR PATRIC; fig|658445.3.peg.4747; -.
DR HOGENOM; CLU_006493_9_4_6; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000032303; Chromosome 2.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR005257; Anth_synth_I_TrpE.
DR InterPro; IPR015890; Chorismate_C.
DR NCBIfam; TIGR00565; trpE_proteo; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF49; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PIRSF; PIRSF001373; TrpE; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; ADC synthase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW ECO:0000256|PIRSR:PIRSR001373-1};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001373};
KW Lyase {ECO:0000256|PIRNR:PIRNR001373};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001373-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001373-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000032303};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW ECO:0000256|PIRSR:PIRSR001373-1}.
FT DOMAIN 22..193
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 247..507
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT BINDING 43
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 296..298
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 333..334
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
FT BINDING 454
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 474
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 488..490
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
SQ SEQUENCE 527 AA; 58461 MW; 063992C83B0FE294 CRC64;
MNTNPLGVGE LELLSLDVPY VADPTELYYS VCGDRPYNLL LESAEIDSKQ DLKSLMLIDA
AVRIVCRGKV VTLEALTDNG LNVLQTLEGK MPADITAERQ GRQLALRFPS AERALDEDSR
LRQTSSFDAL RMIQHAFNIA GHPREALFIG GLFAYDVVDG FEPLPGVKQD NRCPDYLFYI
AETLLVIDHQ RRKGKLQATL FGGDEYTSSY FELSRRLQHI KEACLEPMPL PAAQLLDECE
PVASVSDEDF CQQVLDLKQH VINGDVFQVV PSRQFTLPCP SPLNAYKELK IGNPSPYMFY
LQDADFTLFG ASPESALKYC TESNQIEIYP IAGTRRRGKN PDGSINLDLD GRIELELRCD
MKENAEHMML VDLARNDVAR ISEPGSRYVA DLLAVDRYSH VMHLVSRVVG QLRGDLDALH
AYQACMNMGT LTGAPKIRAM QLIREVEQRR RGSYGGAVGY LTGHGDMDTC IVIRSAYVED
DVASVQAGAG VVYDSVPQAE ADETRGKAQA VITAIRKAHS APDRQSH
//
