(data stored in ACNUC7421 zone)

SWISSPROT: TRPF_RHOPS

ID   TRPF_RHOPS              Reviewed;         218 AA.
AC   Q13EQ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_00135};
DE            Short=PRAI {ECO:0000255|HAMAP-Rule:MF_00135};
DE            EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_00135};
GN   Name=trpF {ECO:0000255|HAMAP-Rule:MF_00135};
GN   OrderedLocusNames=RPD_0196;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC         carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC         EC=5.3.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00135};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00135}.
CC   -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00135}.
DR   EMBL; CP000283; ABE37436.1; -; Genomic_DNA.
DR   RefSeq; WP_011500628.1; NC_007958.1.
DR   SMR; Q13EQ3; -.
DR   STRING; 316057.RPD_0196; -.
DR   PRIDE; Q13EQ3; -.
DR   EnsemblBacteria; ABE37436; ABE37436; RPD_0196.
DR   KEGG; rpd:RPD_0196; -.
DR   eggNOG; ENOG4108ZGB; Bacteria.
DR   eggNOG; COG0135; LUCA.
DR   HOGENOM; HOG000161598; -.
DR   KO; K01817; -.
DR   OMA; FYAKSPR; -.
DR   OrthoDB; 1854712at2; -.
DR   BioCyc; RPAL316057:RPD_RS00995-MONOMER; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00405; PRAI; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001240; PRAI.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13EQ3.
DR   SWISS-2DPAGE; Q13EQ3.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Isomerase; Tryptophan biosynthesis.
FT   CHAIN         1    218       N-(5'-phosphoribosyl)anthranilate
FT                                isomerase.
FT                                /FTId=PRO_1000018635.
SQ   SEQUENCE   218 AA;  22810 MW;  3D0F834F6D9E8F07 CRC64;
     MSVVVKICGL STCDTLEAAV AAGADMVGFV FFPASPRHVG LDVARELSDQ VGSRAAKVAL
     TVDASDALIR DIVEILKPDL LQLHGSESPE RVRALKQAFG LPVMKAIAVA TAADLAMLPA
     YAETADRILF DARPPKDATR PGGLGMTFDW ELLRDLDLSL PFMVSGGVNP GNVAAALRVT
     GAGGVDVSSG VERAPGAKDP ELIRSFIRAA RASEELMT
//

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