TRPD_MYCTU
ID TRPD_MYCTU Reviewed; 370 AA.
AC P9WFX5; L0T8W2; P66992; Q10382;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=Rv2192c;
GN ORFNames=MTCY190.03c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-370 IN COMPLEX WITH
RP PHOSPHORIBOSYLPYROPHOSPHATE AND MAGNESIUM IONS, COFACTOR, AND SUBUNIT.
RX PubMed=16337227; DOI=10.1016/j.jmb.2005.11.016;
RA Lee C.E., Goodfellow C., Javid-Majd F., Baker E.N., Shaun Lott J.;
RT "The crystal structure of TrpD, a metabolic enzyme essential for lung
RT colonization by Mycobacterium tuberculosis, in complex with its substrate
RT phosphoribosylpyrophosphate.";
RL J. Mol. Biol. 355:784-797(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 2-370 IN COMPLEX WITH
RP PHOSPHORIBOSYLPYROPHOSPHATE AND MAGNESIUM IONS, COFACTOR, AND SUBUNIT.
RA Castell A., Short L.F., Evans G., Bulloch E.M., Cookson T., Parker E.,
RA Lee C., Baker E.N., Lott J.S.;
RT "Inhibition of Mycobacterium tuberculosis anthranilate
RT phosphoribosyltransferase by blocking of an active site entrance tunnel.";
RL Submitted (FEB-2011) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 2-370 IN COMPLEX WITH
RP PHOSPHORIBOSYLPYROPHOSPHATE, ANTHRANILATE ANALOGS AND MAGNESIUM IONS,
RP COFACTOR, AND SUBUNIT.
RA Evans G.L., Gamage S.A., Denny W.A., Baker E.N., Lott J.S.;
RT "Improved inhibitors against Mycobacterium tuberculosis anthranilate
RT phosphoribosyltransferase.";
RL Submitted (AUG-2012) to the PDB data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 2-370 IN COMPLEX WITH
RP PHOSPHORIBOSYLPYROPHOSPHATE, ANTHRANILATE ANALOGS AND MAGNESIUM IONS,
RP COFACTOR, AND SUBUNIT.
RX PubMed=23363292; DOI=10.1021/bi301387m;
RA Castell A., Short F.L., Evans G.L., Cookson T.V., Bulloch E.M.,
RA Joseph D.D., Lee C.E., Parker E.J., Baker E.N., Lott J.S.;
RT "The substrate capture mechanism of Mycobacterium tuberculosis anthranilate
RT phosphoribosyltransferase provides a dode for inhibition.";
RL Biochemistry 52:1776-1787(2013).
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).
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 ECO:0000269|PubMed:16337227, ECO:0000269|PubMed:23363292,
CC ECO:0000269|Ref.4, ECO:0000269|Ref.5};
CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_00211, ECO:0000269|PubMed:16337227,
CC ECO:0000269|PubMed:23363292, ECO:0000269|Ref.4, ECO:0000269|Ref.5};
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|PubMed:16337227, ECO:0000269|PubMed:23363292,
CC ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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DR EMBL; AL123456; CCP44969.1; -; Genomic_DNA.
DR PIR; A70784; A70784.
DR RefSeq; NP_216708.1; NC_000962.3.
DR RefSeq; WP_003411387.1; NC_000962.3.
DR PDB; 1ZVW; X-ray; 2.30 A; A/B=1-370.
DR PDB; 2BPQ; X-ray; 1.90 A; A/B=2-370.
DR PDB; 3QQS; X-ray; 1.97 A; A/B/C/D=2-370.
DR PDB; 3QR9; X-ray; 1.87 A; A/B=2-370.
DR PDB; 3QS8; X-ray; 2.00 A; A/B/C/D=2-370.
DR PDB; 3QSA; X-ray; 2.18 A; A/B=2-370.
DR PDB; 3R6C; X-ray; 1.83 A; A/B=2-370.
DR PDB; 3R88; X-ray; 1.73 A; A/B=2-370.
DR PDB; 3TWP; X-ray; 1.83 A; A/B/C/D=2-370.
DR PDB; 3UU1; X-ray; 1.82 A; A/B/C/D=2-370.
DR PDB; 4GIU; X-ray; 1.67 A; A/B=1-370.
DR PDB; 4GKM; X-ray; 1.67 A; A/B=2-370.
DR PDB; 4IJ1; X-ray; 1.79 A; A/B=2-370.
DR PDB; 4M0R; X-ray; 1.96 A; A/B=2-370.
DR PDB; 4N5V; X-ray; 1.90 A; A/B=1-370.
DR PDB; 4N8Q; X-ray; 2.08 A; A/B=1-370.
DR PDB; 4N93; X-ray; 2.03 A; A/B=1-370.
DR PDB; 4OWM; X-ray; 1.99 A; A/B=1-370.
DR PDB; 4OWN; X-ray; 2.11 A; A/B=1-370.
DR PDB; 4OWO; X-ray; 1.99 A; A/B=1-370.
DR PDB; 4OWQ; X-ray; 1.89 A; A/B=1-370.
DR PDB; 4OWS; X-ray; 2.43 A; A/B=1-370.
DR PDB; 4OWU; X-ray; 1.89 A; A/B=1-370.
DR PDB; 4OWV; X-ray; 1.90 A; A/B=1-370.
DR PDB; 4X58; X-ray; 1.75 A; A/B=1-370.
DR PDB; 4X59; X-ray; 1.80 A; A/B=1-370.
DR PDB; 4X5A; X-ray; 1.93 A; A/B=1-370.
DR PDB; 4X5B; X-ray; 2.47 A; A/B=1-370.
DR PDB; 4X5C; X-ray; 2.33 A; A/B=1-370.
DR PDB; 4X5D; X-ray; 2.30 A; A/B=1-370.
DR PDB; 4X5E; X-ray; 1.77 A; A/B=1-370.
DR PDB; 5BNE; X-ray; 2.15 A; A/B/C/D=2-370.
DR PDB; 5BYT; X-ray; 2.00 A; A/B=2-370.
DR PDB; 5C1R; X-ray; 1.80 A; A/B=2-370.
DR PDB; 5C2L; X-ray; 2.01 A; A/B=2-370.
DR PDB; 5C7S; X-ray; 2.10 A; A/B=2-370.
DR PDBsum; 1ZVW; -.
DR PDBsum; 2BPQ; -.
DR PDBsum; 3QQS; -.
DR PDBsum; 3QR9; -.
DR PDBsum; 3QS8; -.
DR PDBsum; 3QSA; -.
DR PDBsum; 3R6C; -.
DR PDBsum; 3R88; -.
DR PDBsum; 3TWP; -.
DR PDBsum; 3UU1; -.
DR PDBsum; 4GIU; -.
DR PDBsum; 4GKM; -.
DR PDBsum; 4IJ1; -.
DR PDBsum; 4M0R; -.
DR PDBsum; 4N5V; -.
DR PDBsum; 4N8Q; -.
DR PDBsum; 4N93; -.
DR PDBsum; 4OWM; -.
DR PDBsum; 4OWN; -.
DR PDBsum; 4OWO; -.
DR PDBsum; 4OWQ; -.
DR PDBsum; 4OWS; -.
DR PDBsum; 4OWU; -.
DR PDBsum; 4OWV; -.
DR PDBsum; 4X58; -.
DR PDBsum; 4X59; -.
DR PDBsum; 4X5A; -.
DR PDBsum; 4X5B; -.
DR PDBsum; 4X5C; -.
DR PDBsum; 4X5D; -.
DR PDBsum; 4X5E; -.
DR PDBsum; 5BNE; -.
DR PDBsum; 5BYT; -.
DR PDBsum; 5C1R; -.
DR PDBsum; 5C2L; -.
DR PDBsum; 5C7S; -.
DR AlphaFoldDB; P9WFX5; -.
DR SMR; P9WFX5; -.
DR STRING; 83332.Rv2192c; -.
DR iPTMnet; P9WFX5; -.
DR PaxDb; P9WFX5; -.
DR DNASU; 887681; -.
DR GeneID; 887681; -.
DR KEGG; mtu:Rv2192c; -.
DR PATRIC; fig|83332.111.peg.2439; -.
DR TubercuList; Rv2192c; -.
DR eggNOG; COG0547; Bacteria.
DR OMA; GPMTNPA; -.
DR PhylomeDB; P9WFX5; -.
DR BRENDA; 2.4.2.18; 3445.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; IBA:GO_Central.
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; Acetylation; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Glycosyltransferase; Magnesium;
KW Metal-binding; Reference proteome; Transferase; Tryptophan biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..370
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000154461"
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 ECO:0000269|PubMed:16337227, ECO:0000269|PubMed:23363292,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.5"
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 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 ECO:0000269|PubMed:16337227, ECO:0000269|PubMed:23363292,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT BINDING 117..120
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 135..143
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 138
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
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 ECO:0000269|PubMed:16337227, ECO:0000269|PubMed:23363292,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT BINDING 193
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4X5D"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:4GIU"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:3QR9"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3QR9"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:4GIU"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:4GIU"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:4IJ1"
FT HELIX 336..352
FT /evidence="ECO:0007829|PDB:4GIU"
FT HELIX 355..368
FT /evidence="ECO:0007829|PDB:4GIU"
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
