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TRPD_SERMA
ID   TRPD_SERMA              Reviewed;          38 AA.
AC   P12321;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Anthranilate phosphoribosyltransferase;
DE            EC=2.4.2.18;
DE   Flags: Fragment;
GN   Name=trpD;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=TRPE7;
RX   PubMed=786623; DOI=10.1111/j.1432-1033.1976.tb10628.x;
RA   Largen M., Mills S.E., Rowe J., Yanofsky C.;
RT   "Purification, subunit structure and partial amino-acid sequence of
RT   anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase from
RT   the enteric bacterium Serratia marcescens.";
RL   Eur. J. Biochem. 67:31-36(1976).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   PIR; A05222; A05222.
DR   AlphaFoldDB; P12321; -.
DR   SMR; P12321; -.
DR   STRING; 273526.SMDB11_1935; -.
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.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
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..>38
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_0000154477"
FT   NON_TER         38
SQ   SEQUENCE   38 AA;  4308 MW;  55ECA01364E969CC CRC64;
     MQPILEKLYR AESMSQQESQ QLFSAIVRGE LEPSQLAA
 
 
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