ID A0A151JL00_9VIBR Unreviewed; 520 AA.
AC A0A151JL00;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|PIRNR:PIRNR001373};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001373};
GN ORFNames=AUQ44_14775 {ECO:0000313|EMBL:KYN26332.1};
OS Vibrio cidicii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1763883 {ECO:0000313|EMBL:KYN26332.1, ECO:0000313|Proteomes:UP000075349};
RN [1] {ECO:0000313|Proteomes:UP000075349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2756-81 {ECO:0000313|Proteomes:UP000075349};
RA Tarr C.L., Gladney L.M.;
RL Submitted (DEC-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,
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}.
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:KYN26332.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LOMK01000001; KYN26332.1; -; Genomic_DNA.
DR RefSeq; WP_061900066.1; NZ_LOBP01000146.1.
DR AlphaFoldDB; A0A151JL00; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000075349; Unassembled WGS sequence.
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 Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW ECO:0000256|PIRSR:PIRSR001373-1}.
FT DOMAIN 25..198
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 246..506
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT BINDING 45
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 295..297
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 332..333
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
FT BINDING 453
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 473
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 487..489
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 502
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
SQ SEQUENCE 520 AA; 57362 MW; 7F82C104F1118CFB CRC64;
MNKAIKIKTL GKLDVITASV PYTQDPTRLF HTLCESKTDS LLLESAEIDS KQDLKSLLIV
DSALRIVCYG QTVTCNALTD NGRHLLAHVQ GNIQPEIKQQ FDGQTLTLTF SESDDTLDED
SRLREASSFD ALRLIQHSFD LGGHDKHALF IGGLFAYDLV ANFEPLGPAS ATNQCPDYVF
YVAETLLVVD HQTESCHLQA TLFANSEQKS VLETRIEQIS TLCADPKTLP QAVKLAQVDA
TPSVSDEAFC QIVRDLKQYV VKGDIFQVVP SRRFTLPCPS PLAAYKELKL SNPSPYMFYM
QDELFTLFGA SPESALKYET DTNQVEIYPI AGTRRRGKRA NGEIDFDLDS RIELELRTDK
KENAEHMMLV DLARNDVARI SQAGTRHVAD LLKVDRYSHV MHLVSRVVGQ LRADLDALHA
YQACMNMGTL TGAPKIRAMQ LIRDVEGARR GSYGGAVGYL TGEGTLDTCI VIRSAYVENG
IAQVQAGAGV VFDSDPQAEA DETRGKAQAV ISAIQKAHKE
//
