ID D4DST4_NEIEG Unreviewed; 341 AA.
AC D4DST4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
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:EFE49118.1};
GN ORFNames=NEIELOOT_02130 {ECO:0000313|EMBL:EFE49118.1}, NELON_08830
GN {ECO:0000313|EMBL:AJE18986.1};
OS Neisseria elongata subsp. glycolytica ATCC 29315.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546263 {ECO:0000313|EMBL:EFE49118.1, ECO:0000313|Proteomes:UP000005536};
RN [1] {ECO:0000313|EMBL:EFE49118.1, ECO:0000313|Proteomes:UP000005536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|EMBL:EFE49118.1,
RC ECO:0000313|Proteomes:UP000005536};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000031392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|Proteomes:UP000031392};
RA Veyrier F.J., Taha M.-K.;
RT "Complete Genome sequence of Neisseria elongata subsp. glycolytica.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AJE18986.1, ECO:0000313|Proteomes:UP000031392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|EMBL:AJE18986.1,
RC ECO:0000313|Proteomes:UP000031392};
RX PubMed=26162030;
RA Veyrier F.J., Biais N., Morales P., Belkacem N., Guilhen C., Ranjeva S.,
RA Sismeiro O., Pehau-Arnaudet G., Rocha E.P., Werts C., Taha M.K.,
RA Boneca I.G.;
RT "Common Cell Shape Evolution of Two Nasopharyngeal Pathogens.";
RL PLoS Genet. 11:E1005338-E1005338(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: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; CP007726; AJE18986.1; -; Genomic_DNA.
DR EMBL; ADBF01000227; EFE49118.1; -; Genomic_DNA.
DR RefSeq; WP_003773656.1; NZ_CP007726.1.
DR AlphaFoldDB; D4DST4; -.
DR STRING; 546263.NELON_08830; -.
DR KEGG; nel:NELON_08830; -.
DR PATRIC; fig|546263.7.peg.1899; -.
DR HOGENOM; CLU_034315_2_1_4; -.
DR UniPathway; UPA00035; UER00041.
DR Proteomes; UP000005536; Unassembled WGS sequence.
DR Proteomes; UP000031392; 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:UP000031392};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00211};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00211}.
FT DOMAIN 5..67
FT /note="Glycosyl transferase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02885"
FT DOMAIN 77..327
FT /note="Glycosyl transferase family 3"
FT /evidence="ECO:0000259|Pfam:PF00591"
FT BINDING 83
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 83
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 86..87
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 91
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 93..96
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 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT BINDING 111..119
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 123
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 169
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 341 AA; 36043 MW; 0BAF1792F4E1CE07 CRC64;
MITPQQAIER LISNNELFYD EMTDLMRQIM SGQVPPEQIA AILTGLRIKV ETVSEITAAA
AVMREFATPV PVVDKNGLVD IVGTGGDGAK TFNISTTAMF VAAAAGAKVA KHGGRSVSSS
SGAADVVEQM GAKTDLSPEQ VARTIEETGI GFMFAPNHHS AMRYVAPVRR SLGFRSIFNI
LGPLTNPAGA PNQLLGVFHK DLCGILSRVL QQLGSQHVLV VCGSDGLDEI TLTGETYVAE
LKDGTIREYT ISPEQFGLPL RRNLDEIKVA DSRESLSMMN AVLAGEAGAA RDIVLLNAAA
ALYAGNVVSS LTEGMAAARE AIDSGRAKVK QEEFIAATLK G
//
