TRPGD_THEMA
ID TRPGD_THEMA Reviewed; 589 AA.
AC Q08654;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Bifunctional protein TrpGD;
DE Includes:
DE RecName: Full=Anthranilate synthase component 2;
DE Short=AS;
DE Short=ASII;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
DE Includes:
DE RecName: Full=Anthranilate phosphoribosyltransferase;
DE EC=2.4.2.18;
GN Name=trpGD; Synonyms=trpD; OrderedLocusNames=TM_0141;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7685830; DOI=10.1006/jmbi.1993.1345;
RA Kim C.W., Markiewicz P.G., Lee J.J., Schierle C.F., Miller J.H.;
RT "Studies of the hyperthermophile Thermotoga maritima by random sequencing
RT of cDNA and genomic libraries. Identification and sequencing of the trpEG
RT (D) operon.";
RL J. Mol. Biol. 231:960-981(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 494-589.
RX PubMed=7556082; DOI=10.1002/j.1460-2075.1995.tb00118.x;
RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.;
RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the
RT hyperthermophile Thermotoga maritima.";
RL EMBO J. 14:4395-4402(1995).
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. In addition to
CC synthesizing anthranilate, it also catalyzes the second step of the
CC pathway, the transfer of the phosphoribosyl group of 5-
CC phosphorylribose-1-pyrophosphate (PRPP) to anthranilate (By
CC similarity). {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 -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + anthranilate;
CC Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 2/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC phosphoribosyltransferase family. {ECO:0000305}.
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DR EMBL; X74075; CAA52203.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35234.1; -; Genomic_DNA.
DR EMBL; X92729; CAA63388.1; -; Genomic_DNA.
DR PIR; C72414; C72414.
DR RefSeq; NP_227956.1; NC_000853.1.
DR AlphaFoldDB; Q08654; -.
DR SMR; Q08654; -.
DR STRING; 243274.THEMA_04100; -.
DR EnsemblBacteria; AAD35234; AAD35234; TM_0141.
DR KEGG; tma:TM0141; -.
DR PATRIC; fig|243274.5.peg.140; -.
DR eggNOG; COG0512; Bacteria.
DR eggNOG; COG0547; Bacteria.
DR InParanoid; Q08654; -.
DR OMA; VIYRNHV; -.
DR BioCyc; MetaCyc:MON-282; -.
DR UniPathway; UPA00035; UER00040.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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; 3.40.1030.10; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00211; TrpD; 1.
DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR SUPFAM; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR TIGRFAMs; TIGR01245; trpD; 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; Glycosyltransferase; Lyase;
KW Multifunctional enzyme; Reference proteome; Transferase;
KW Tryptophan biosynthesis.
FT CHAIN 1..589
FT /note="Bifunctional protein TrpGD"
FT /id="PRO_0000056901"
FT DOMAIN 46..241
FT /note="Glutamine amidotransferase type-1"
FT REGION 253..589
FT /note="Anthranilate phosphoribosyltransferase"
FT ACT_SITE 126
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT ACT_SITE 215
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 217
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 99..101
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 130
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 176..177
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT CONFLICT 384
FT /note="E -> G (in Ref. 1; CAA52203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 64269 MW; 8DF80E6DA0C68610 CRC64;
MAPGRSGYRL RFRSGARISG DSEQTQGFVQ EPGSCAEDPG GIVLKRVIVI DNYDSFVYNI
VQYIGEVEPD CEIEVFRNDE ITIEEIERKN PTHIVISPGP GRPEEAGISV DVVRHFSGKV
PILGVCLGHQ VIGYAFGGKI VHAKRILHGK TSKIVHNGKG VFSGVKNPLV ATRYHSLVVE
EASLPEVLEI TAKSDDGEIM GLQHKEHPTF GVQFHPESVL TEEGKRIIKN FLNIQDIQVK
KVSEETEIDI VSALKKLVEF EDLTFEESRQ VMNFIMSGNA TDAQIAGFLV ALRMKEETGD
ELGGMASVMR EKSIHIKAPS PRTVDTCGTG GDGFGTFNIS TTTAFVVAAA GIPVAKHGNR
SVSSKVGSAD VLEAGGYKLE KTPEEMEREL KETGFSFLFA PLLHPAMKHV MPARRQLKIR
TAFNLLGPIT NPARVKYQVV GVFDLSFASK LATALQRLGT ERSAVVNGGF TDELTTCGKN
NLLLVTQEEI VPMVLDPEEL GLKSGDPEEL KGPSDPKEAY RMMESVLKGE ASRTQVETVA
LNAGVVFWLV GECDTIKDGV GKALDLIRTG EAYKKLREVM DYQKTLGNS
