TRPG_SACS2
ID TRPG_SACS2 Reviewed; 195 AA.
AC Q06129;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
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; OrderedLocusNames=SSO0894;
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 [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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, AND 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 (Probable).
CC {ECO:0000305|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 -!- 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}.
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DR EMBL; M98048; AAA73380.1; -; Genomic_DNA.
DR EMBL; Z50014; CAA90312.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41176.1; -; Genomic_DNA.
DR PIR; A99240; A99240.
DR PIR; B40635; B40635.
DR RefSeq; WP_009992310.1; NC_002754.1.
DR PDB; 1QDL; X-ray; 2.50 A; B=1-195.
DR PDBsum; 1QDL; -.
DR AlphaFoldDB; Q06129; -.
DR SMR; Q06129; -.
DR DIP; DIP-6203N; -.
DR IntAct; Q06129; 1.
DR MINT; Q06129; -.
DR STRING; 273057.SSO0894; -.
DR EnsemblBacteria; AAK41176; AAK41176; SSO0894.
DR GeneID; 44129824; -.
DR KEGG; sso:SSO0894; -.
DR PATRIC; fig|273057.12.peg.897; -.
DR eggNOG; arCOG00086; Archaea.
DR HOGENOM; CLU_014340_1_3_2; -.
DR InParanoid; Q06129; -.
DR OMA; TEHGHAM; -.
DR PhylomeDB; Q06129; -.
DR BioCyc; MetaCyc:MON-3604; -.
DR BRENDA; 4.1.3.27; 6163.
DR UniPathway; UPA00035; UER00040.
DR EvolutionaryTrace; Q06129; -.
DR Proteomes; UP000001974; Chromosome.
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; IBA:GO_Central.
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 Glutamine amidotransferase; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..195
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000056900"
FT DOMAIN 3..195
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:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 175
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 177
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 54..56
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 88
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 137..138
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT CONFLICT 49
FT /note="I -> L (in Ref. 1; AAA73380/CAA90312)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1QDL"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1QDL"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 97..114
FT /evidence="ECO:0007829|PDB:1QDL"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 128..141
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:1QDL"
FT STRAND 159..175
FT /evidence="ECO:0007829|PDB:1QDL"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1QDL"
SQ SEQUENCE 195 AA; 21909 MW; 155B62933E9CD33E CRC64;
MDLTLIIDNY DSFVYNIAQI VGELGSYPIV IRNDEISIKG IERIDPDRII ISPGPGTPEK
REDIGVSLDV IKYLGKRTPI LGVCLGHQAI GYAFGAKIRR ARKVFHGKIS NIILVNNSPL
SLYYGIAKEF KATRYHSLVV DEVHRPLIVD AISAEDNEIM AIHHEEYPIY GVQFHPESVG
TSLGYKILYN FLNRV
