(data stored in ACNUC7421 zone)

SWISSPROT: TRPD_ANADF

ID   TRPD_ANADF              Reviewed;         337 AA.
AC   A7H793;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   11-DEC-2019, entry version 72.
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};
GN   OrderedLocusNames=Anae109_0374;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RX   PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
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; CP000769; ABS24589.1; -; Genomic_DNA.
DR   RefSeq; WP_011984695.1; NC_009675.1.
DR   SMR; A7H793; -.
DR   STRING; 404589.Anae109_0374; -.
DR   EnsemblBacteria; ABS24589; ABS24589; Anae109_0374.
DR   KEGG; afw:Anae109_0374; -.
DR   eggNOG; ENOG4108I0Q; Bacteria.
DR   eggNOG; COG0547; LUCA.
DR   HOGENOM; HOG000230451; -.
DR   KO; K00766; -.
DR   OMA; HHSAMKH; -.
DR   OrthoDB; 1238435at2; -.
DR   BioCyc; ASP404589:G1G9J-383-MONOMER; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000006382; 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; A7H793.
DR   SWISS-2DPAGE; A7H793.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW   Transferase; Tryptophan biosynthesis.
FT   CHAIN           1..337
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_1000042988"
FT   REGION          83..84
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   REGION          90..93
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   REGION          108..116
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           92
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         80
FT                   /note="Anthranilate 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         80
FT                   /note="Phosphoribosylpyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         88
FT                   /note="Phosphoribosylpyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         111
FT                   /note="Anthranilate 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         120
FT                   /note="Phosphoribosylpyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         166
FT                   /note="Anthranilate 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
SQ   SEQUENCE   337 AA;  34767 MW;  6815C780A4EFF5A3 CRC64;
     MIQQALTRLL DRHDLARAEM SAVMDEIADG GATPAQVGAF LAALRLKGET VEEIAGAAEV
     MRARVDPIRV DRDVFVDTCG TGGDGRHTFN ISTTAAFIVA GAGVTVAKHG NRAVSSRSGS
     ADVLAALGVD VDAAKDVVER AIEEVGIGFL FAPRLHPAFK AVAGIRRELG VRTVFNLLGP
     LANPAGARYQ VLGVYEPRWV PILGGVLAAL GAAHAFVVHG EGLDEIAVTG MTHVCEVRAG
     ECERYAMVPE DLGLRRHEEA EIAGGDADRN ARILADVLAG QQGGPRDAAL ANAAAALVAA
     GAAADLREGV RLGAEAVDRG AASDKLARLV AVTRGGA
//

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