TRPE_SERMA
ID TRPE_SERMA Reviewed; 519 AA.
AC P00897;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS)
RP IN COMPLEX WITH SUBSTRATES AND MAGNESIUM ION, FUNCTION, COFACTOR, AND
RP 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).
RN [2]
RP PROTEIN SEQUENCE OF 1-25.
RC STRAIN=SM6;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=366432; DOI=10.1038/276684a0;
RA Miozzari G.F., Yanofsky C.;
RT "The regulatory region of the trp operon of Serratia marcescens.";
RL Nature 276:684-689(1978).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 494-519.
RC STRAIN=SM6;
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).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11371633};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:11371633};
CC -!- ACTIVITY REGULATION: Feedback inhibited by tryptophan. {ECO:0000250}.
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 P00897; P00900: trpG; NbExp=2; IntAct=EBI-1031345, EBI-1031352;
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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; AAA57308.2; -; Genomic_DNA.
DR PIR; A01117; A01117.
DR PDB; 1I7Q; X-ray; 1.95 A; A/C=1-519.
DR PDB; 1I7S; X-ray; 2.40 A; A/C=1-519.
DR PDBsum; 1I7Q; -.
DR PDBsum; 1I7S; -.
DR AlphaFoldDB; P00897; -.
DR SMR; P00897; -.
DR IntAct; P00897; 1.
DR STRING; 273526.SMDB11_1933; -.
DR BRENDA; 4.1.3.27; 5690.
DR UniPathway; UPA00035; UER00040.
DR EvolutionaryTrace; P00897; -.
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; -; 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 PANTHER; PTHR11236; PTHR11236; 1.
DR PANTHER; PTHR11236:SF22; PTHR11236:SF22; 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; SSF56322; 1.
DR TIGRFAMs; TIGR00565; trpE_proteo; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Lyase; Magnesium; Metal-binding;
KW Tryptophan biosynthesis.
FT CHAIN 1..519
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154111"
FT BINDING 39
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|PubMed:11371633,
FT ECO:0007744|PDB:1I7S"
FT BINDING 290..292
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|PubMed:11371633,
FT ECO:0007744|PDB:1I7S"
FT BINDING 327..328
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000305|PubMed:11371633"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11371633"
FT BINDING 448
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000305|PubMed:11371633"
FT BINDING 468
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000305|PubMed:11371633"
FT BINDING 482..484
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000305|PubMed:11371633"
FT BINDING 484
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000305|PubMed:11371633"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11371633"
FT CONFLICT 502..504
FT /note="ARA -> PVP (in Ref. 4; AAA57308)"
FT /evidence="ECO:0000305"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1I7Q"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 47..63
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 171..184
FT /evidence="ECO:0007829|PDB:1I7Q"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:1I7Q"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 355..375
FT /evidence="ECO:0007829|PDB:1I7Q"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 382..391
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 396..406
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 412..419
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:1I7Q"
FT TURN 446..449
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:1I7Q"
FT STRAND 476..482
FT /evidence="ECO:0007829|PDB:1I7Q"
FT HELIX 491..512
FT /evidence="ECO:0007829|PDB:1I7Q"
SQ SEQUENCE 519 AA; 57658 MW; D3B59D47619FB0C1 CRC64;
MNTKPQLTLL KVQASYRGDP TTLFHQLCGA RPATLLLESA EINDKQNLQS LLVIDSALPI
TALGHTVSVQ ALTANGPALL PVLDEALPPE VRNQARPNGR ELTFPAIDAV QDEDARLRSL
SVFDALRTLL TLVDSPADER EAVMLGGLFA YDLVAGFENL PAVRQDQRCP DFCFYLAETL
LVLDHQRGSA RLQASVFSEQ ASEAQRLQHR LEQLQAELQQ PPQPIPHQKL ENMQLSCNQS
DEEYGAVVSE LQEAIRQGEI FQVVPSRRFS LPCPAPLGPY QTLKDNNPSP YMFFMQDDDF
TLFGASPESA LKYDAGNRQI EIYPIAGTRP RGRRADGSLD LDLDSRIELE MRTDHKELAE
HLMLVDLARN DLARICQAGS RYVADLTKVD RYSFVMHLVS RVVGTLRADL DVLHAYQACM
NMGTLSGAPK VRAMQLIAAL RSTRRGSYGG RVGYFTAHRH LDTCIVIRSA YVEDGHRTVQ
AGAGVVQDSI RRREADETRN KARAVLRAIA TAHHAKEVF
