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Database: UniProt
Entry: K9UDA9_CHAP6
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Original site: K9UDA9_CHAP6 
ID   K9UDA9_CHAP6            Unreviewed;       346 AA.
AC   K9UDA9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
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=Cha6605_1472 {ECO:0000313|EMBL:AFY92638.1};
OS   Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC   Chamaesiphon.
OX   NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY92638.1, ECO:0000313|Proteomes:UP000010366};
RN   [1] {ECO:0000313|EMBL:AFY92638.1, ECO:0000313|Proteomes:UP000010366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Chamaesiphon sp. PCC 6605.";
RL   Submitted (MAY-2012) 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; CP003600; AFY92638.1; -; Genomic_DNA.
DR   RefSeq; WP_015158818.1; NC_019697.1.
DR   AlphaFoldDB; K9UDA9; -.
DR   STRING; 1173020.Cha6605_1472; -.
DR   KEGG; cmp:Cha6605_1472; -.
DR   PATRIC; fig|1173020.3.peg.1699; -.
DR   eggNOG; COG0547; Bacteria.
DR   HOGENOM; CLU_034315_2_1_3; -.
DR   OMA; KCFNTLQ; -.
DR   OrthoDB; 9806430at2; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000010366; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00211};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   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:UP000010366};
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          12..71
FT                   /note="Glycosyl transferase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02885"
FT   DOMAIN          79..331
FT                   /note="Glycosyl transferase family 3"
FT                   /evidence="ECO:0000259|Pfam:PF00591"
FT   BINDING         85
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         85
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         88..89
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
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..98
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         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         113..121
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         116
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         125
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         171
FT                   /ligand="anthranilate"
FT                   /ligand_id="ChEBI:CHEBI:16567"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00211"
SQ   SEQUENCE   346 AA;  35235 MW;  6C49A7A5CCCB8C45 CRC64;
     MLTLTESATW SQLLQQLLEK QSLSQAQSKI LMQGWLDGEI PPGLSGAILA ALEAKQITAP
     ELAGMAQALQ APAIAPFTPA IDTCGTGGDG ASTFNISTAV AFVAAAAGAK VAKHGNRSAS
     SRVGSADVLE ALGVKLTAPA ERVAAALDAV GITFLFAPGW HPAMKAVASL RQELKIRTVF
     NLLGPLVNPL RPTGQIIGVF TPHLLEIIAE AAGILGTHQA IVLHGREGLD EAGLGDATDL
     AILTNGEVKL TSIDPVELGI IPAPITALAG GDVAENAAIL TAVLQGKGTP AQRDVVAVNA
     GLALQVANLV PMGAHQQGIE LATAVLNSGV AWDKLTELVD FLGAVD
//
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