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