ID Q12LE6_SHEDO Unreviewed; 546 AA.
AC Q12LE6;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|PIRNR:PIRNR001373};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001373};
GN OrderedLocusNames=Sden_2450 {ECO:0000313|EMBL:ABE55730.1};
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE55730.1, ECO:0000313|Proteomes:UP000001982};
RN [1] {ECO:0000313|EMBL:ABE55730.1, ECO:0000313|Proteomes:UP000001982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC {ECO:0000313|Proteomes:UP000001982};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) 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; CP000302; ABE55730.1; -; Genomic_DNA.
DR RefSeq; WP_011496881.1; NC_007954.1.
DR AlphaFoldDB; Q12LE6; -.
DR STRING; 318161.Sden_2450; -.
DR KEGG; sdn:Sden_2450; -.
DR eggNOG; COG0147; Bacteria.
DR HOGENOM; CLU_006493_9_4_6; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000001982; Chromosome.
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, ECO:0000313|EMBL:ABE55730.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001373-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001373-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001982};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW ECO:0000256|PIRSR:PIRSR001373-1}.
FT DOMAIN 29..201
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 272..532
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT BINDING 50
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 321..323
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 358..359
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
FT BINDING 479
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 499
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 513..515
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
SQ SEQUENCE 546 AA; 60011 MW; ABFE4BC555649685 CRC64;
MTAPTSTQRA STASIAKVST QKRRLTYHAD PLSLYHSITQ DLPHTLLLES AEVTSKQNLK
SIIMTHAAMM IRCDAYQITF SALTPNGASL LAPIAAFFSH AKPTQDEQHL VVQLCKSAEL
QDEDARLKAT SPLDGLRLLV NAIKTDKAPE FEDLFLGGVL AYDLIDTVEP LPPVPNASND
CPDYLFYLAE TLILADHQTE QSELITHLFN PNLIDADNDA SRDENNDKAI DNSSYMRVLS
ERAAMLTQAC QQPLMTPALK PLDAQERVNI SDEQFKKTVV DLKEHIVAGD IFQVVPSRSF
SLPCPNTLGA YRALRLTNPS PYMFYFRGPD FTLFGASPES ALKYQASNNQ VEVYPIAGTR
KRGKNALGEI DFDLDSRIEL ELRLDKKELS EHLMLVDLAR NDIARISQSG SRKVPELLKV
DRYSHVMHLV SRVTGQLRTD LDALHAYQAC MNMGTLVGAP KVRASQLVRE AEKARRGSYG
GAVGYLNALG DMDTCIVIRS AFVKDGVAHI QAGAGVVFDS DPQAEADETR QKAQAVISAI
KLGGAL
//