TRPD_XANCP
ID TRPD_XANCP Reviewed; 345 AA.
AC Q8PD71;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=XCC0469;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, AND
RP SUBUNIT.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of an anthranilate phosphoribosyltransferase (target ID
RT NYSGRC-016600) from Xanthomonas campestris.";
RL Submitted (OCT-2012) 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; AE008922; AAM39787.1; -; Genomic_DNA.
DR RefSeq; NP_635863.1; NC_003902.1.
DR RefSeq; WP_011035722.1; NC_003902.1.
DR PDB; 4HKM; X-ray; 1.95 A; A/B=1-345.
DR PDBsum; 4HKM; -.
DR AlphaFoldDB; Q8PD71; -.
DR SMR; Q8PD71; -.
DR STRING; 340.xcc-b100_0499; -.
DR DNASU; 998756; -.
DR EnsemblBacteria; AAM39787; AAM39787; XCC0469.
DR KEGG; xcc:XCC0469; -.
DR PATRIC; fig|190485.4.peg.516; -.
DR eggNOG; COG0547; Bacteria.
DR HOGENOM; CLU_034315_2_1_6; -.
DR OMA; GPMTNPA; -.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW Transferase; Tryptophan biosynthesis.
FT CHAIN 1..345
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000154503"
FT BINDING 84
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 84
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 87..88
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 92
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 94..97
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 112..120
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 115
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 124
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 170
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:4HKM"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:4HKM"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 289..304
FT /evidence="ECO:0007829|PDB:4HKM"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:4HKM"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:4HKM"
SQ SEQUENCE 345 AA; 36477 MW; 2352F6B2241B6A0F CRC64;
MPITPQQALQ RTIEHREIFH DEMVDLMRQI MRGEVSDAMV SAILTGLRVK KETIGEIAGA
ATVMREFSRR VEVTDRRHMV DIVGTGGDGS HTFNISTCAM FVAAAGGAKV AKHGNRSVSS
KSGSADALEA LGAVIELQPE QVAASLAQTG IGFMYAPVHH PAMKVVAPVR REMGVRTIFN
ILGPLTNPAG SPNILMGVFH PDLVGIQARV LQELGAERAL VVWGRDGMDE LSLGAGTLVG
ELRDGQVHEY EVHPEDFGIA MSASRNLKVA DAAESRAMLL QVLDNVPGPA LDIVALNAGA
ALYVAGVADS IADGIVRARQ VLADGSARAC LDAYVAFTQQ ATAQG
