TRPD2_NOSS1
ID TRPD2_NOSS1 Reviewed; 362 AA.
AC Q8YXQ9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Anthranilate phosphoribosyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00211};
DE EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211};
GN Name=trpD2 {ECO:0000255|HAMAP-Rule:MF_00211}; OrderedLocusNames=alr1153;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of anthranilate phosphoribosyltransferase 2 (17130499)
RT from Nostoc sp. at 1.85 A resolution.";
RL Submitted (JUL-2011) 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.2}.
CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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DR EMBL; BA000019; BAB73110.1; -; Genomic_DNA.
DR PIR; AF1950; AF1950.
DR RefSeq; WP_010995326.1; NZ_RSCN01000008.1.
DR PDB; 1VQU; X-ray; 1.85 A; A/B=1-362.
DR PDBsum; 1VQU; -.
DR AlphaFoldDB; Q8YXQ9; -.
DR SMR; Q8YXQ9; -.
DR STRING; 103690.17130499; -.
DR EnsemblBacteria; BAB73110; BAB73110; BAB73110.
DR KEGG; ana:alr1153; -.
DR eggNOG; COG0547; Bacteria.
DR OMA; GPMTNPA; -.
DR OrthoDB; 1238435at2; -.
DR UniPathway; UPA00035; UER00041.
DR EvolutionaryTrace; Q8YXQ9; -.
DR Proteomes; UP000002483; Chromosome.
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; Reference proteome;
KW Transferase; Tryptophan biosynthesis.
FT CHAIN 1..362
FT /note="Anthranilate phosphoribosyltransferase 2"
FT /id="PRO_0000154420"
FT BINDING 103
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 103
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 106..107
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 111
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 113..116
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 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 131..139
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 134
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 143
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 189
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:1VQU"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1VQU"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 291..302
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 308..324
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:1VQU"
FT HELIX 348..361
FT /evidence="ECO:0007829|PDB:1VQU"
SQ SEQUENCE 362 AA; 37598 MW; C392D1446391AC13 CRC64;
MTSSPTSTQE SSTSWYLLLQ QLIDGESLSR SQAAELMQGW LSEAVPPELS GAILTALNFK
GVSADELTGM AEVLQSQSKM GTGENYSQLP ITNSPFSIID TCGTGGDGSS TFNISTAVAF
VAAAYGVPVA KHGNRSASSL TGSADVLEAL GVNLGASPEK VQAALQEVGI TFLFAPGWHP
ALKAVATLRR TLRIRTVFNL LGPLVNPLRP TGQVVGLFTP KLLTTVAQAL DNLGKQKAIV
LHGRERLDEA GLGDLTDLAV LSDGELQLTT INPQEVGVTP APIGALRGGD VQENAEILKA
VLQGKGTQAQ QDAVALNAAL ALQVAGAVPL LDHAQGVSVA KEILQTGTAW AKLAQLVYFL
GN
