TRPE_SACS2
ID TRPE_SACS2 Reviewed; 421 AA.
AC Q06128;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=SSO0893;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=8416906; DOI=10.1128/jb.175.1.299-302.1993;
RA Tutino M.L., Scarano G., Marino G., Sannia G., Cubellis M.V.;
RT "Tryptophan biosynthesis genes trpEGC in the thermoacidophilic
RT archaebacterium Sulfolobus solfataricus.";
RL J. Bacteriol. 175:299-302(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=9016772; DOI=10.1006/bbrc.1996.5951;
RA Tutino M.L., Tosco A., Marino G., Sannia G.;
RT "Expression of Sulfolobus solfataricus trpE and trpG genes in E. coli.";
RL Biochem. Biophys. Res. Commun. 230:306-310(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, ACTIVITY REGULATION, AND
RP SUBUNIT.
RX PubMed=10449718; DOI=10.1073/pnas.96.17.9479;
RA Knoechel T., Ivens A., Hester G., Gonzalez A., Bauerle R., Wilmanns M.,
RA Kirschner K., Jansonius J.N.;
RT "The crystal structure of anthranilate synthase from Sulfolobus
RT solfataricus: functional implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9479-9484(1999).
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:0000269|PubMed:10449718}.
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:0000250|UniProtKB:P00897};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
CC -!- ACTIVITY REGULATION: Cooperatively feedback inhibited by tryptophan.
CC {ECO:0000269|PubMed:10449718}.
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:10449718}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; M98048; AAA73379.1; -; Genomic_DNA.
DR EMBL; Z50014; CAA90311.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41175.1; -; Genomic_DNA.
DR PIR; H90239; H90239.
DR PIR; JC5323; JC5323.
DR RefSeq; WP_009992309.1; NC_002754.1.
DR PDB; 1QDL; X-ray; 2.50 A; A=1-421.
DR PDBsum; 1QDL; -.
DR AlphaFoldDB; Q06128; -.
DR SMR; Q06128; -.
DR DIP; DIP-6202N; -.
DR IntAct; Q06128; 1.
DR MINT; Q06128; -.
DR STRING; 273057.SSO0893; -.
DR EnsemblBacteria; AAK41175; AAK41175; SSO0893.
DR GeneID; 44129823; -.
DR KEGG; sso:SSO0893; -.
DR PATRIC; fig|273057.12.peg.896; -.
DR eggNOG; arCOG02014; Archaea.
DR HOGENOM; CLU_006493_9_3_2; -.
DR InParanoid; Q06128; -.
DR OMA; NMDFNIA; -.
DR PhylomeDB; Q06128; -.
DR BioCyc; MetaCyc:MON-3603; -.
DR BRENDA; 4.1.3.27; 6163.
DR UniPathway; UPA00035; UER00040.
DR EvolutionaryTrace; Q06128; -.
DR Proteomes; UP000001974; 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; IBA:GO_Central.
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; IPR010116; Anthranilate_synth_I_arc_typ.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR01820; TrpE-arch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Lyase; Magnesium; Metal-binding;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..421
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154132"
FT BINDING 31
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 207..209
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 242..243
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 357
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 377
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 391..393
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 393
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 406
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 337
FT /note="A -> R (in Ref. 1; AAA73379 and 2; CAA90311)"
FT /evidence="ECO:0000305"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1QDL"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 157..173
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 177..191
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 264..282
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 302..315
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:1QDL"
FT TURN 355..358
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 385..394
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 400..417
FT /evidence="ECO:0007829|PDB:1QDL"
SQ SEQUENCE 421 AA; 47652 MW; BD49BD7771ECC6EE CRC64;
MEVHPISEFA SPFEVFKCIE RDFKVAGLLE SIGGPQYKAR YSVIAWSTNG YLKIHDDPVN
ILNGYLKDLK LADIPGLFKG GMIGYISYDA VRFWEKIRDL KPAAEDWPYA EFFTPDNIII
YDHNEGKVYV NADLSSVGGC GDIGEFKVSF YDESLNKNSY ERIVSESLEY IRSGYIFQVV
LSRFYRYIFS GDPLRIYYNL RRINPSPYMF YLKFDEKYLI GSSPELLFRV QDNIVETYPI
AGTRPRGADQ EEDLKLELEL MNSEKDKAEH LMLVDLARND LGKVCVPGTV KVPELMYVEK
YSHVQHIVSK VIGTLKKKYN ALNVLSATFP AGTVSGAPKP MAMNIIETLE EYKRGPYAGA
VGFISADGNA EFAIAIRTAF LNKELLRIHA GAGIVYDSNP ESEYFETEHK LKALKTAIGV
R
