(data stored in ACNUC7421 zone)

SWISSPROT: TRPD_RHILO

ID   TRPD_RHILO              Reviewed;         336 AA.
AC   Q98ME4;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 102.
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=mlr0614;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
DR   EMBL; BA000012; BAB48169.1; -; Genomic_DNA.
DR   RefSeq; WP_010909524.1; NC_002678.2.
DR   SMR; Q98ME4; -.
DR   STRING; 266835.14021557; -.
DR   EnsemblBacteria; BAB48169; BAB48169; BAB48169.
DR   KEGG; mlo:mlr0614; -.
DR   PATRIC; fig|266835.9.peg.491; -.
DR   eggNOG; ENOG4107QYG; Bacteria.
DR   eggNOG; COG0547; LUCA.
DR   HOGENOM; HOG000230451; -.
DR   KO; K00766; -.
DR   OMA; HHSAMKH; -.
DR   OrthoDB; 1238435at2; -.
DR   BioCyc; MLOT266835:G1G20-505-MONOMER; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000000552; 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; 1.20.970.10; -; 1.
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   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   3: Inferred from homology;
DR   PRODOM; Q98ME4.
DR   SWISS-2DPAGE; Q98ME4.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glycosyltransferase; Magnesium; Metal-binding; Transferase;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..336
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_0000154474"
FT   REGION          84..85
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   REGION          91..94
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   REGION          109..117
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           93
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           225
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           226
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           226
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         81
FT                   /note="Anthranilate 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         81
FT                   /note="Phosphoribosylpyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         89
FT                   /note="Phosphoribosylpyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         112
FT                   /note="Anthranilate 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         121
FT                   /note="Phosphoribosylpyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         167
FT                   /note="Anthranilate 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
SQ   SEQUENCE   336 AA;  34609 MW;  B7ABE46F0971DB62 CRC64;
     MSALKTHIAK VAAGTALSFE EAREAFDIIM SGDATPGQIG GFLMALRVRG ETVSEISGAV
     ATMRAKMLRV EAPAGAIDIV GTGGDNSHSV NISTGSAFVI AAAGVPVAKH GNRGLSSLTG
     AADVLIALGV KIDIPPDAIG RCIHEAGVGF MFAPAHHPAM KHVGPTRVEL GTRTIFNLLG
     PLSNPAGVVR QMVGVFLPEW ILPVAETLKA LGTEHAWVVH GDGYDEITTT GETQVAELIG
     GEIRSFTLTP EEVGLKRHTK DELRGGDAAY NANALRDMLD GAAGAYRDTV LMNAGAGLVI
     AGKATTLGDG IALAAQAIDS GRALQVLDRL VEISNG
//

If you have problems or comments...

PBIL Back to PBIL home page