TRPG_SERMA
ID TRPG_SERMA Reviewed; 193 AA.
AC P00900;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
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 Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7007652; DOI=10.1016/0022-2836(80)90260-0;
RA Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C.;
RT "Nucleotide sequences of the trpG regions of Escherichia coli, Shigella
RT dysenteriae, Salmonella typhimurium and Serratia marcescens.";
RL J. Mol. Biol. 142:503-517(1980).
RN [2]
RP PROTEIN SEQUENCE OF 2-193.
RX PubMed=6986371; DOI=10.1016/s0021-9258(19)86051-9;
RA Tso J.Y., Hermodson M.A., Zalkin H.;
RT "Primary structure of Serratia marcescens anthranilate synthase component
RT II.";
RL J. Biol. Chem. 255:1451-1457(1980).
RN [3]
RP PROTEIN SEQUENCE OF 2-62.
RX PubMed=4598537; DOI=10.1021/bi00705a028;
RA Li S.-L., Hanlon J., Yanofsky C.;
RT "Separation of anthranilate synthetase components I and II of Escherichia
RT coli, Salmonella typhimurium, and Serratia marcescens and determination of
RT their amino-terminal sequences by automatic Edman degradation.";
RL Biochemistry 13:1736-1744(1974).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, FUNCTION,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=11371633; DOI=10.1073/pnas.111150298;
RA Spraggon G., Kim C., Nguyen-Huu X., Yee M.-C., Yanofsky C., Mills S.E.;
RT "The structures of anthranilate synthase of Serratia marcescens
RT crystallized in the presence of (i) its substrates, chorismate and
RT glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-
RT tryptophan.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6021-6026(2001).
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 (Probable).
CC {ECO:0000305|PubMed:11371633}.
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).
CC {ECO:0000269|PubMed:11371633}.
CC -!- INTERACTION:
CC P00900; P00897: trpE; NbExp=2; IntAct=EBI-1031352, EBI-1031345;
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; AY027546; AAK37409.1; -; Genomic_DNA.
DR PIR; D92860; NNSE2.
DR PDB; 1I7Q; X-ray; 1.95 A; B/D=1-193.
DR PDB; 1I7S; X-ray; 2.40 A; B/D=1-193.
DR PDBsum; 1I7Q; -.
DR PDBsum; 1I7S; -.
DR AlphaFoldDB; P00900; -.
DR SMR; P00900; -.
DR IntAct; P00900; 1.
DR STRING; 273526.SMDB11_1934; -.
DR MEROPS; C26.960; -.
DR UniPathway; UPA00035; UER00040.
DR EvolutionaryTrace; P00900; -.
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 Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Glutamine amidotransferase; Lyase;
KW Tryptophan biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4598537,
FT ECO:0000269|PubMed:6986371"
FT CHAIN 2..193
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000056898"
FT DOMAIN 3..193
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 84
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000269|PubMed:11371633"
FT ACT_SITE 170
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 172
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 57..59
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000305|PubMed:11371633"
FT BINDING 88
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000305|PubMed:11371633"
FT BINDING 134..135
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000305|PubMed:11371633"
FT CONFLICT 36
FT /note="G -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="E -> Q (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="H -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="E -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..62
FT /note="TPS -> ASV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Q -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="S -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1I7Q"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1I7S"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 97..114
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 125..139
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:1I7Q"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:1I7Q"
SQ SEQUENCE 193 AA; 20868 MW; 8F53EBFEC7F4524A CRC64;
MADILLLDNV DSFTYNLVDQ LRASGHQVVI YRNQIGAEVI IERLQHMEQP VLMLSPGPGT
PSEAGCMPEL LQRLRGQLPI IGICLGHQAI VEAYGGQVGQ AGEILHGKAS AIAHDGEGMF
AGMANPLPVA RYHSLVGSNI PADLTVNARS GEMVMAVRDD RRRVCGFQFH PESILTTHGA
RLLEQTLAWA LAK
