TRPG_HALVD
ID TRPG_HALVD Reviewed; 204 AA.
AC P33974; D4GT35;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=HVO_2453;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS2 / DSM 5716 / WFD11;
RX PubMed=1537810; DOI=10.1128/jb.174.5.1694-1697.1992;
RA Lam W.L., Logan S.M., Doolittle W.F.;
RT "Genes for tryptophan biosynthesis in the halophilic archaebacterium
RT Haloferax volcanii: the trpDFEG cluster.";
RL J. Bacteriol. 174:1694-1697(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
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 {ECO:0000250}.
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; M83788; AAA73178.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE03081.1; -; Genomic_DNA.
DR PIR; B42301; B42301.
DR RefSeq; WP_004042365.1; NZ_AOHU01000044.1.
DR AlphaFoldDB; P33974; -.
DR SMR; P33974; -.
DR STRING; 309800.C498_07565; -.
DR MEROPS; C26.959; -.
DR EnsemblBacteria; ADE03081; ADE03081; HVO_2453.
DR GeneID; 8926019; -.
DR KEGG; hvo:HVO_2453; -.
DR eggNOG; arCOG00086; Archaea.
DR HOGENOM; CLU_014340_1_2_2; -.
DR OMA; HQVVIYR; -.
DR OrthoDB; 100703at2157; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000008243; 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; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glutamine amidotransferase; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..204
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000056883"
FT DOMAIN 3..204
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 88
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 178
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 180
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 58..60
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 138..139
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT CONFLICT 38
FT /note="N -> T (in Ref. 1; AAA73178)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..108
FT /note="EP -> DA (in Ref. 1; AAA73178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 21849 MW; 6FC8FCE64599C444 CRC64;
MIRLVVVDNF DSFTYNLVEY FSEQTVEGEP LDIEVRKNTA SLDEIRDLDP DAIVISPGPG
HPKNDRDVGV TNDVLTELST EIPTLGVCLG LEAAVYAYGG TIGHAPEPIH GKAFPVDHDG
AGVFAGLEDG FPAGRYHSLV ATDVPDCFDV SATTDHDGEA LVMGVRHRDY PIECVQFHPE
SVLTGSGHGV VRNFLTAVAG FDVA
