TRPG_METTM
ID TRPG_METTM Reviewed; 196 AA.
AC P26923; D9PUE6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=MTBMA_c02350;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=1860817; DOI=10.1128/jb.173.16.5017-5023.1991;
RA Meile L., Stettler R., Banholzer R., Kotik M., Leisinger T.;
RT "Tryptophan gene cluster of Methanobacterium thermoautotrophicum Marburg:
RT molecular cloning and nucleotide sequence of a putative trpEGCFBAD
RT operon.";
RL J. Bacteriol. 173:5017-5023(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADL57844.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; M65060; AAA73029.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL57844.1; ALT_INIT; Genomic_DNA.
DR PIR; G40362; G40362.
DR AlphaFoldDB; P26923; -.
DR SMR; P26923; -.
DR STRING; 79929.MTBMA_c02350; -.
DR MEROPS; C26.A25; -.
DR EnsemblBacteria; ADL57844; ADL57844; MTBMA_c02350.
DR KEGG; mmg:MTBMA_c02350; -.
DR PATRIC; fig|79929.8.peg.231; -.
DR HOGENOM; CLU_014340_1_2_2; -.
DR OMA; TEHGHAM; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000345; 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; Tryptophan biosynthesis.
FT CHAIN 1..196
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000056890"
FT DOMAIN 4..196
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 89
FT /note="Nucleophile; 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 ACT_SITE 179
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 60..62
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 93
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"
SQ SEQUENCE 196 AA; 21954 MW; 71A8D7D180D8D203 CRC64;
MNKLILIIDN YDSFTHNLYQ MAGEIMMEMD SADIMVVRND EVDIDYVRGL DPERIIISPG
PGNPIKREDF GICSEVIGEF TDRPILGVCL GHQGIFHYFG GVVGYGEPVH GKISEVFHDG
SELFRGVPNP FRATRYHSLR CECSGVPEDI LVSASAPDGT IMAIRHRQYP VYGLQFHPES
AGTPHGRDIL ENFLRM
