(data stored in SCRATCH zone)

SWISSPROT: TRPD_LACP3

ID   TRPD_LACP3              Reviewed;         341 AA.
AC   Q03CY0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   11-DEC-2019, 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=LSEI_0078;
OS   Lactobacillus paracasei (strain ATCC 334 / BCRC 17002 / CIP 107868 / KCTC
OS   3260 / NRRL B-441).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CIP 107868 / KCTC 3260 / NRRL B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000423; ABJ68942.1; -; Genomic_DNA.
DR   RefSeq; WP_011673966.1; NC_008526.1.
DR   RefSeq; YP_805384.1; NC_008526.1.
DR   SMR; Q03CY0; -.
DR   EnsemblBacteria; ABJ68942; ABJ68942; LSEI_0078.
DR   GeneID; 4418984; -.
DR   KEGG; lca:LSEI_0078; -.
DR   PATRIC; fig|321967.11.peg.103; -.
DR   HOGENOM; HOG000230451; -.
DR   KO; K00766; -.
DR   OMA; HHSAMKH; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000001651; 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; Q03CY0.
DR   SWISS-2DPAGE; Q03CY0.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW   Transferase; Tryptophan biosynthesis.
FT   CHAIN           1..341
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_1000043018"
FT   REGION          82..83
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   REGION          89..92
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   REGION          107..115
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           91
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           224
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           225
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   BINDING         79
FT                   /note="Anthranilate 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         79
FT                   /note="Phosphoribosylpyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         87
FT                   /note="Phosphoribosylpyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         110
FT                   /note="Anthranilate 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         119
FT                   /note="Phosphoribosylpyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         165
FT                   /note="Anthranilate 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
SQ   SEQUENCE   341 AA;  36515 MW;  1BC1016228062E43 CRC64;
     MIKQAIEKVV NHENLTFEES EAVLDEIMNG EASEVQTASL LTALTAKNPT IDEIAGAAAS
     MRSHALAFPE TKDVLEIVGT GGDHANTFNI STTSAIVVAA TGTQVAKHGN RAASSKSGAA
     DVLEALGLDI NETPAVSYES LQENNLAFLF AQEYHKSMKY VATVRKQLGF RTIFNILGPL
     ANPAHPTHQL LGVYDETLLE PLANVLKKLG VTNAMVVHGR DGLDEMTTAD ETAVVELQDD
     HLTKYTVTPE QFGLKRRQRA DLVGGTPEAN ADITRRILAG DHGPQRDIVL LNAGAALHVA
     HPALSIQAGI DLAAKTIDDG KAFEELNRLL AFSDKRKDVV A
//

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