TRPD_ACIAD
ID TRPD_ACIAD Reviewed; 349 AA.
AC P00500; Q6F9N2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 151.
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=ACIAD2462;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6599977; DOI=10.1093/oxfordjournals.molbev.a040331;
RA Kaplan J.B., Goncharoff P., Seibold A.M., Nichols B.P.;
RT "Nucleotide sequence of the Acinetobacter calcoaceticus trpGDC gene
RT cluster.";
RL Mol. Biol. Evol. 1:456-472(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).
RA Ponniah K., Nigon L.V., Anderson B.F., Norris G.E., Patrick W.M.;
RT "Structure of anthranilate phosphoribosyl transferase from Acinetobacter
RT baylyi.";
RL Submitted (AUG-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 -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00211}.
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DR EMBL; M36636; AAA21904.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG69232.1; -; Genomic_DNA.
DR PIR; A00585; NPKEDC.
DR RefSeq; WP_004928448.1; NC_005966.1.
DR PDB; 4GTN; X-ray; 2.03 A; A=2-349.
DR PDB; 4YI7; X-ray; 1.85 A; A=2-349.
DR PDBsum; 4GTN; -.
DR PDBsum; 4YI7; -.
DR AlphaFoldDB; P00500; -.
DR SMR; P00500; -.
DR STRING; 62977.ACIAD2462; -.
DR EnsemblBacteria; CAG69232; CAG69232; ACIAD2462.
DR GeneID; 45234767; -.
DR KEGG; aci:ACIAD2462; -.
DR eggNOG; COG0547; Bacteria.
DR HOGENOM; CLU_034315_2_1_6; -.
DR OMA; GPMTNPA; -.
DR OrthoDB; 1238435at2; -.
DR BioCyc; ASP62977:ACIAD_RS11250-MON; -.
DR BRENDA; 4.1.3.27; 5690.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000000430; 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..349
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000154417"
FT BINDING 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 82
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 85..86
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..95
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
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 110..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 113
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 122
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 168
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT HELIX 2..11
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4YI7"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:4YI7"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 287..306
FT /evidence="ECO:0007829|PDB:4YI7"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:4YI7"
FT HELIX 328..343
FT /evidence="ECO:0007829|PDB:4YI7"
SQ SEQUENCE 349 AA; 37556 MW; AF53E46A63564A89 CRC64;
MNIQQALNHI TKNIHLTQAQ MEDVMRSIMQ GEATEAQIGA LMMGLRMKGE SIDEITAAAR
VMRELAIKID VSDIQYLVDI VGTGGDGQNL FNVSTASSFV IAAAGATIAK HGNRGVSSKS
GSSDLLEQAG INLDLDMQQT ERCIREMGVG FLFAPNHHKA MKYAVGPRRE LGIRSIFNLL
GPLTNPAGVK RFVIGVFSDE LCRPIAEVMK QLGAEHVMVV HSKDGLDEIS LASQTYIAEL
KNGEVTEWVL NPEDVNIPSQ TLSGLIVEDS NASLKLIKDA LGRKKSDIGE KAANMIALNA
GAGIYVSGLA TSYKQGVALA HDIIYGGQAL EKMSILSEFT KALKEYANN