位置:首页 > 蛋白库 > TRPG_CYACA
TRPG_CYACA
ID   TRPG_CYACA              Reviewed;         195 AA.
AC   O19914;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Anthranilate synthase component 2;
DE            Short=AS;
DE            EC=4.1.3.27;
DE   AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
GN   Name=trpG;
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
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: Tetramer of two components I and two components II.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
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; AF022186; AAB82675.1; -; Genomic_DNA.
DR   PIR; T11982; T11982.
DR   RefSeq; NP_045086.1; NC_001840.1.
DR   AlphaFoldDB; O19914; -.
DR   SMR; O19914; -.
DR   MEROPS; C26.955; -.
DR   GeneID; 800224; -.
DR   UniPathway; UPA00035; UER00040.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW   Glutamine amidotransferase; Lyase; Plastid; Tryptophan biosynthesis.
FT   CHAIN           1..195
FT                   /note="Anthranilate synthase component 2"
FT                   /id="PRO_0000056893"
FT   DOMAIN          1..195
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        79
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         52..54
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         83
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         129..130
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
SQ   SEQUENCE   195 AA;  21985 MW;  51C53AE010352AD0 CRC64;
     MILIIDNYDS FSYNLVQSVG EINSDLIVLR SDEIDVSKLQ NLNIKHIIIS PGPGHPDEYT
     ICKQVVKFFA PYTPILGICL GHQIIATCYN ASIKKSSPVF HGRASKIYCL KDKLFLGIHA
     PFTAARYHSL VVDQDKRGLD LTTCLKTIAI TREGVIMACK HRYYHFTYGI QFHPESMLTI
     QGTKLLKNFL SLSYG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025