ID   TRPD_PECCA              Reviewed;          39 AA.
AC   P12320;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Anthranilate phosphoribosyltransferase;
DE            EC=2.4.2.18;
DE   Flags: Fragment;
GN   Name=trpD;
OS   Pectobacterium carotovorum (Erwinia carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=554;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=TRP9;
RX   PubMed=338606; DOI=10.1016/s0021-9258(17)38224-8;
RA   Largen M., Mills S.E., Rowe J., Yanofsky C.;
RT   "Purification and properties of a third form of anthranilate-5-
RT   phosphoribosylpyrophosphate phosphoribosyltransferase from the
RT   Enterobacteriaceae.";
RL   J. Biol. Chem. 253:409-412(1978).
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:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   PIR; A05003; A05003.
DR   PRIDE; P12320; -.
DR   UniPathway; UPA00035; UER00041.
DR   GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Direct protein sequencing; Glycosyltransferase; Magnesium; Metal-binding;
KW   Transferase; Tryptophan biosynthesis.
FT   CHAIN           1..>39
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_0000154447"
FT   NON_TER         39
SQ   SEQUENCE   39 AA;  4460 MW;  EEA59A03A0CA650F CRC64;
     MQATLIKPTI FTHQPILEKL FKSQSMTQEE SXQLFAAIV