TRPD_MYCTA
ID TRPD_MYCTA Reviewed; 370 AA.
AC A5U4M0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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}; OrderedLocusNames=MRA_2208;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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 -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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DR EMBL; CP000611; ABQ73970.1; -; Genomic_DNA.
DR RefSeq; WP_003411387.1; NZ_CP016972.1.
DR PDB; 4ZOF; X-ray; 1.80 A; A/B=2-370.
DR PDB; 4ZOJ; X-ray; 1.96 A; A/B=2-370.
DR PDB; 4ZOK; X-ray; 2.34 A; A/B=2-370.
DR PDB; 4ZTV; X-ray; 2.01 A; A/B=1-370.
DR PDB; 5BO2; X-ray; 2.00 A; A/B=2-370.
DR PDB; 5BO3; X-ray; 1.75 A; A/B=2-370.
DR PDBsum; 4ZOF; -.
DR PDBsum; 4ZOJ; -.
DR PDBsum; 4ZOK; -.
DR PDBsum; 4ZTV; -.
DR PDBsum; 5BO2; -.
DR PDBsum; 5BO3; -.
DR AlphaFoldDB; A5U4M0; -.
DR SMR; A5U4M0; -.
DR STRING; 419947.MRA_2208; -.
DR EnsemblBacteria; ABQ73970; ABQ73970; MRA_2208.
DR KEGG; mra:MRA_2208; -.
DR eggNOG; COG0547; Bacteria.
DR HOGENOM; CLU_034315_4_1_11; -.
DR OMA; GPMTNPA; -.
DR BRENDA; 2.4.2.18; 3445.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000001988; 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; Transferase;
KW Tryptophan biosynthesis.
FT CHAIN 1..370
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_1000043036"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 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 107
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 110..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 115
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 117..120
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 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 135..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 138
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 147
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 193
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4ZOF"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:5BO3"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 336..352
FT /evidence="ECO:0007829|PDB:5BO3"
FT HELIX 355..368
FT /evidence="ECO:0007829|PDB:5BO3"
SQ SEQUENCE 370 AA; 37740 MW; 23C8B67D6C33E18D CRC64;
MALSAEGSSG GSRGGSPKAE AASVPSWPQI LGRLTDNRDL ARGQAAWAMD QIMTGNARPA
QIAAFAVAMT MKAPTADEVG ELAGVMLSHA HPLPADTVPD DAVDVVGTGG DGVNTVNLST
MAAIVVAAAG VPVVKHGNRA ASSLSGGADT LEALGVRIDL GPDLVARSLA EVGIGFCFAP
RFHPSYRHAA AVRREIGVPT VFNLLGPLTN PARPRAGLIG CAFADLAEVM AGVFAARRSS
VLVVHGDDGL DELTTTTTST IWRVAAGSVD KLTFDPAGFG FARAQLDQLA GGDAQANAAA
VRAVLGGARG PVRDAVVLNA AGAIVAHAGL SSRAEWLPAW EEGLRRASAA IDTGAAEQLL
ARWVRFGRQI
