ID A0A068ZBC6_9GAMM Unreviewed; 520 AA.
AC A0A068ZBC6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653, ECO:0000256|PIRNR:PIRNR001373};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266, ECO:0000256|PIRNR:PIRNR001373};
GN ORFNames=GPZ83_00640 {ECO:0000313|EMBL:MXR53289.1}, GPZ83_011260
GN {ECO:0000313|EMBL:NYV30464.1}, SYMBAF_05570
GN {ECO:0000313|EMBL:QLH62515.1};
OS Serratia symbiotica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=138074 {ECO:0000313|EMBL:MXR53289.1};
RN [1] {ECO:0000313|EMBL:QLH62515.1, ECO:0000313|Proteomes:UP000042738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWBI-2.3 {ECO:0000313|EMBL:QLH62515.1};
RX PubMed=25146134;
RA Foray V., Grigorescu A.S., Sabri A., Haubruge E., Lognay G., Francis F.,
RA Fauconnier M.L., Hance T., Thonart P.;
RT "Whole-Genome Sequence of Serratia symbiotica Strain CWBI-2.3T, a Free-
RT Living Symbiont of the Black Bean Aphid Aphis fabae.";
RL Genome Announc. 2:e00767-e00714(2014).
RN [2] {ECO:0000313|EMBL:QLH62515.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CWBI-2.3 {ECO:0000313|EMBL:QLH62515.1};
RA Foray V.V.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MXR53289.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24.1 {ECO:0000313|EMBL:MXR53289.1};
RA Renoz F., Ambroise J., Gala J.-L., Hance T.;
RT "Draft genome sequence of Serratia symbiotica strain 24.1.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:NYV30464.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=24.1 {ECO:0000313|EMBL:NYV30464.1}, and CWBI-2.3
RC {ECO:0000313|EMBL:QLH62515.1};
RA Renoz F., Foray V., Ambroise J., Baa-Puyoulet P., Bearzatto B.,
RA Mendez G.L., Vanderpoorten A., Mahillon J., Gala J.-L., Calevro F.,
RA Hance T.;
RT "Genomic Insight into Nascent Stage of Mutualistic Insect Bacterial
RT Symbioses through the Bacterial Symbiont Serratia symbiotica.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC (TrpG) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia.
CC {ECO:0000256|ARBA:ARBA00025634}.
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|ARBA:ARBA00004873,
CC 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; WSPN01000001; MXR53289.1; -; Genomic_DNA.
DR EMBL; WSPN02000002; NYV30464.1; -; Genomic_DNA.
DR EMBL; CP050855; QLH62515.1; -; Genomic_DNA.
DR STRING; 138074.SYMBAF_50488; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000042738; 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:MXR53289.1};
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 19..190
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 242..502
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT BINDING 40
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 328..329
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
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 520 AA; 57233 MW; 913A21323BD672F4 CRC64;
MINQKPQLKL LKVQASYRDD PTTVFHQLCG ARPATLLLES AEITSKQNLQ SLLVIDSALR
ITAQGRTVTV QTLTANGAAL LPLLDEALPS EVHIQVCPNG RALTFPQIDT VQDEDARLRS
LSVFDALRTL LTLVDSPADE REAVMLGGLF AYDLVAGFED LPELRQDQRC PDFCFYLVET
LLVMDHQHTS AHLQASVFTA DHAEAQRLQQ RLEQLQAQLT HAAQPIPHQR LESIRLGCSQ
TDEEYCALVS GLQEAIRQGE IFQVVPSRRF SLPCPAPLAA YKTLKDNNPS PYMFFMQDDE
FTLFGASPES ALKYSASTRQ LEIYPIAGTR PRGYRADGSL DLDLDSRIEL EMRTDDKELA
EHLMLVDLAR NDLARICQVG SRYVADLTKV DRYSFVMHLV SRVVGTLRSD LDALHAYQAC
MNMGTLSGAP KVRAMQLIAA SEGSRRGSYG GAVGYFTATG DLDTCIVIRS AYVEDGIATV
QAGAGVVLAS VPQAEADETR NKARAVLRAI ASAHHAREVF
//
