ID A0A1B9NFI3_9MICO Unreviewed; 354 AA.
AC A0A1B9NFI3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ECO:0000313|EMBL:QBR74365.1};
GN ORFNames=A7J15_02820 {ECO:0000313|EMBL:OCG75340.1}, E3O41_08065
GN {ECO:0000313|EMBL:QBR74365.1};
OS Microbacterium sediminis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=904291 {ECO:0000313|EMBL:OCG75340.1, ECO:0000313|Proteomes:UP000093355};
RN [1] {ECO:0000313|EMBL:OCG75340.1, ECO:0000313|Proteomes:UP000093355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-01 {ECO:0000313|EMBL:OCG75340.1,
RC ECO:0000313|Proteomes:UP000093355};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBR74365.1, ECO:0000313|Proteomes:UP000295661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-01 {ECO:0000313|EMBL:QBR74365.1,
RC ECO:0000313|Proteomes:UP000295661};
RA Yu L.;
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QBR74365.1, ECO:0000313|Proteomes:UP000295661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-01 {ECO:0000313|EMBL:QBR74365.1,
RC ECO:0000313|Proteomes:UP000295661};
RA Xu X.;
RT "Genomic analysis of Microbacterium sediminis YLB-01 reveals backgrounds
RT related to its deep sea enviroment adaptation.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LXMD01000013; OCG75340.1; -; Genomic_DNA.
DR EMBL; CP038256; QBR74365.1; -; Genomic_DNA.
DR RefSeq; WP_067023984.1; NZ_KV744781.1.
DR AlphaFoldDB; A0A1B9NFI3; -.
DR STRING; 904291.A7J15_02820; -.
DR KEGG; msed:E3O41_08065; -.
DR OrthoDB; 9806430at2; -.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000093355; Unassembled WGS sequence.
DR Proteomes; UP000295661; 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; 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:UP000093355};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00211}; Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211}.
FT DOMAIN 10..70
FT /note="Glycosyl transferase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02885"
FT DOMAIN 77..337
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 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
SQ SEQUENCE 354 AA; 36870 MW; CEE61EC2C100A1B3 CRC64;
MPESLSWPAV LTTVLEGRDL SVSEATWAMT QVMTGAATPA QLAGFLTALR AKGESVEEVI
GFRDAILDAA VPLPVDPNVL DIVGTGGDRI GTVNVSTTAS IVIAATGIPV VKHGNRAVSS
KTGSSDVLGE LGIDLGLSPE AVASVLDRAG ITFAWAAAFH PGFKHAAAVR GELGVPTVFN
FLGPLVNPAR AEANAVGVAN PDVVPLIAGV FRTRGATALV FRGEDGLDEL TTTGYSRIWQ
ISNGDQHEFD IHPRDLDMPT ATLADITGGD PAHNAGVLRR TLAGEQGAVR DIVLLNAAAG
IVAYRLSQDP GQAQRNLIQR LVEARDEAAA AIDDGRAEAK LEAWVRASRE AQTD
//
