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Database: UniProt
Entry: B9XJL1_PEDPL
LinkDB: B9XJL1_PEDPL
Original site: B9XJL1_PEDPL 
ID   B9XJL1_PEDPL            Unreviewed;       347 AA.
AC   B9XJL1;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00211};
DE            EC=2.4.2.18 {ECO:0000256|HAMAP-Rule:MF_00211};
GN   Name=trpD {ECO:0000256|HAMAP-Rule:MF_00211};
GN   ORFNames=Cflav_PD2691 {ECO:0000313|EMBL:EEF59887.1};
OS   Pedosphaera parvula (strain Ellin514).
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX   NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF59887.1, ECO:0000313|Proteomes:UP000003688};
RN   [1] {ECO:0000313|EMBL:EEF59887.1, ECO:0000313|Proteomes:UP000003688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin514 {ECO:0000313|EMBL:EEF59887.1,
RC   ECO:0000313|Proteomes:UP000003688};
RX   PubMed=21460084; DOI=10.1128/JB.00299-11;
RA   Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA   Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA   Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT   "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT   Verrucomicrobial isolate from pasture soil.";
RL   J. Bacteriol. 193:2900-2901(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_00211};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00211};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00211};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00211}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00211}.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00211}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00211}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEF59887.1}.
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DR   EMBL; ABOX02000022; EEF59887.1; -; Genomic_DNA.
DR   RefSeq; WP_007416004.1; NZ_ABOX02000022.1.
DR   AlphaFoldDB; B9XJL1; -.
DR   STRING; 320771.Cflav_PD2691; -.
DR   OMA; GPMTNPA; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000003688; Unassembled WGS sequence.
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; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 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   NCBIfam; TIGR01245; trpD; 1.
DR   PANTHER; PTHR43285; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43285:SF2; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00211}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00211};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003688};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00211}; Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211}.
FT   DOMAIN          6..64
FT                   /note="Glycosyl transferase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02885"
FT   DOMAIN          78..335
FT                   /note="Glycosyl transferase family 3"
FT                   /evidence="ECO:0000259|Pfam:PF00591"
FT   BINDING         84
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         84
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         94..97
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         112..120
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         115
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         170
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
SQ   SEQUENCE   347 AA;  37360 MW;  7F1FB8314722808B CRC64;
     MLKSLNQQLA QAVHLTDEQV RIAVGQLLDE SIPADLKADF LCHLAAKIET PEEIAAFARE
     LRAKSIQPPI DAETRSREIL DVCGTGGDRL NTFNISTTVA IICAAAGVAV AKHGNRAITS
     QSGSADVLEA LGIRVELTPA EAAQSLREHN FAFFFAPNYH PAFKHISAAR KLCAQRGQRT
     IFNFVGPLLN PARPSAQLIG VSRPELCETL AHVLQSLGVR RGMVVSGQVG TAWLDELSTL
     GENIIAEFYQ DRGFTTSSIS PNHFPLQPAT LADLAGSDRQ ANAEIVRRLL RNEDRGPKRD
     AILLNAGASL FVANRTKSLL EGWELADNLI TSGQAFAKLQ ALAATGN
//
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