ID A0A1V3TJX3_9PAST Unreviewed; 516 AA.
AC A0A1V3TJX3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|PIRNR:PIRNR001373};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001373};
GN ORFNames=BMT54_10840 {ECO:0000313|EMBL:OOH86415.1};
OS Pasteurellaceae bacterium 15-036681.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae.
OX NCBI_TaxID=1924934 {ECO:0000313|EMBL:OOH86415.1, ECO:0000313|Proteomes:UP000188845};
RN [1] {ECO:0000313|EMBL:OOH86415.1, ECO:0000313|Proteomes:UP000188845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15-036681 {ECO:0000313|EMBL:OOH86415.1,
RC ECO:0000313|Proteomes:UP000188845};
RA Stuber T.P., Hicks J.A., Robbe-Austerman S., Lantz K.;
RT "Draft genome sequence of a Pasteurellaceae bacterium isolated from a pygmy
RT hippo (Hexaprotodon liberiensis).";
RL Submitted (NOV-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|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:OOH86415.1}.
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DR EMBL; MQVI01000055; OOH86415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3TJX3; -.
DR STRING; 1924934.BMT54_10840; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000188845; 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 Reference proteome {ECO:0000313|Proteomes:UP000188845};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW ECO:0000256|PIRSR:PIRSR001373-1}.
FT DOMAIN 20..193
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 243..502
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT BINDING 35
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 291..293
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
FT BINDING 449
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 469
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 483..485
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
SQ SEQUENCE 516 AA; 57607 MW; 85F687CE576245AD CRC64;
MAVKIEQTQL PYYQDTAAVF YHLCGDKPHT LLLDSAEIQS KNSLKSLLFA KSAVHIACEG
QTVTFEALTA NGKAVLPLIH SALSKLNPAP ICKTFAESDR LQAEFPTLNE ALDEDSKLKT
TTIFDGLRCV SQLFADSQSP VYLGGLFSYD LVAQFIPMEN ITLNDDGLRC PDFSFYLAEQ
LIFIDHQAET ATLHSFCFDP SQQDIIQQQA VKFAEKLAEN ADKSLDLAIK KASDKVNVNL
EDEPFKLIVR DLKHHINIGD VFQIVPSRRF SLECPNTLAS YRQLKINNPS PYMFFMQGEN
FTLFGASPES ALKYSEDNRQ LEIYPIAGSR PRGFDEQGNI DLELDSRLEL ELRLDQKELA
EHLMLVDLAR NDVARVAVSG SRRVADLMQI DRYSHIMHLV SRVIGTLRPD LDALHAYQAC
MNMGTLTGAP KIKAMQLIYQ FEQQKRHSYG GAVGYLTSEG NLDTCIVIRS AFVQDGIAYV
QAGCGEVLDS DPQLEADETR HKARAVLKAI TQVNSI
//
