ID TRPG_AZOBR Reviewed; 196 AA.
AC P26922;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 13-SEP-2023, entry version 97.
DE RecName: Full=Anthranilate synthase component 2;
DE Short=AS;
DE Short=ASII;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase, GATase component;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
GN Name=trpG;
OS Azospirillum brasilense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN INDOLE-3-ACETIC ACID.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=1896020; DOI=10.1007/bf00264211;
RA Zimmer W., Aparicio C., Elmerich C.;
RT "Relationship between tryptophan biosynthesis and indole-3-acetic acid
RT production in Azospirillum: identification and sequencing of a trpGDC
RT cluster.";
RL Mol. Gen. Genet. 229:41-51(1991).
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 (By similarity).
CC Participates in the tryptophan-dependent indole-3-acetic acid
CC production, which is a phytohormone released by A.brasilense.
CC {ECO:0000250, ECO:0000269|PubMed:1896020}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
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DR EMBL; X57853; CAA40984.1; -; Genomic_DNA.
DR PIR; S17703; S17703.
DR AlphaFoldDB; P26922; -.
DR SMR; P26922; -.
DR MEROPS; C26.955; -.
DR UniPathway; UPA00035; UER00040.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glutamine amidotransferase; Lyase; Tryptophan biosynthesis.
FT CHAIN 1..196
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000056871"
FT DOMAIN 1..195
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 80
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 169
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 52..54
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 84
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 130..131
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
SQ SEQUENCE 196 AA; 21405 MW; BBE41EEB84CC0EAA CRC64;
MLLLIDNYDS FTYNLVHYLG ELGAELDVRR NDSLTVEEAM ALRPEGIVLS PGPCDPDKAG
ICLPLIDAAA KAAVPLMGVC LGHQAIGQPF GGTVVRAPVP MHGKVDRMFH QGRGVLKDLP
SPFRATRYHS LIVERATLPA CLEVTGETED GLIMALSHRE LPIHGVQFHP ESIESEHGHK
ILENFLNTTR RLETAA
//
