位置:首页 > 蛋白库 > TRPD_THETH
TRPD_THETH
ID   TRPD_THETH              Reviewed;         329 AA.
AC   P83827;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00211};
DE            EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211};
GN   Name=trpD {ECO:0000255|HAMAP-Rule:MF_00211};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of anthranilate phosphoribosyltransferase (TRPD) from
RT   Thermus thermophilus HB8.";
RL   Submitted (JAN-2004) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-
CC       phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-
CC       phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP-Rule:MF_00211}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00211};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00211};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_00211};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00211}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211,
CC       ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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   RefSeq; WP_011173866.1; NC_006461.1.
DR   PDB; 1V8G; X-ray; 2.10 A; A/B=1-329.
DR   PDBsum; 1V8G; -.
DR   AlphaFoldDB; P83827; -.
DR   SMR; P83827; -.
DR   PRIDE; P83827; -.
DR   GeneID; 3169363; -.
DR   UniPathway; UPA00035; UER00041.
DR   EvolutionaryTrace; P83827; -.
DR   GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1030.10; -; 1.
DR   HAMAP; MF_00211; TrpD; 1.
DR   InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
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   PANTHER; PTHR43285; PTHR43285; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   TIGRFAMs; TIGR01245; trpD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glycosyltransferase; Magnesium; Metal-binding; Transferase;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..329
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_0000154496"
FT   BINDING         78
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         78
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         81..82
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         88..91
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         106..114
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         109
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         118
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         164
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   HELIX           3..8
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           32..45
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           49..61
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          71..78
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           89..99
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           118..124
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           133..143
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           155..159
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           161..167
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           172..176
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          187..191
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           198..207
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          211..217
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          228..232
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          236..240
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           243..245
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           260..271
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           278..293
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   STRAND          296..299
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           300..312
FT                   /evidence="ECO:0007829|PDB:1V8G"
FT   HELIX           315..328
FT                   /evidence="ECO:0007829|PDB:1V8G"
SQ   SEQUENCE   329 AA;  34275 MW;  C18C6A8C40C513A6 CRC64;
     MDAVKKAILG EVLEEEEAYE VMRALMAGEV SPVRAAGLLV ALSLRGERPH EIAAMARAMR
     EAARPLRVHR RPLLDIVGTG GDGKGLMNLS TLAALVAAAG GVAVAKHGNR AASSRAGSAD
     LLEALGVDLE APPERVGEAI EELGFGFLFA RVFHPAMRHV APVRAELGVR TVFNLLGPLT
     NPAGADAYVL GVFSPEWLAP MAEALERLGA RGLVVHGEGA DELVLGENRV VEVGKGAYAL
     TPEEVGLKRA PLEALKGGGP EENAALARRL LKGEEKGPLA DAVALAAGAG FYAAGKTPSL
     KEGVALAREV LASGEAYLLL ERYVAFLRA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024