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Database: UniProt/SWISS-PROT
Entry: TRPF_THEP1
LinkDB: TRPF_THEP1
Original site: TRPF_THEP1 
ID   TRPF_THEP1              Reviewed;         205 AA.
AC   A5IKT2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   01-OCT-2014, entry version 44.
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=Tpet_0786;
OS   Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKU-1 / ATCC BAA-488 / DSM 13995;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P.,
RA   Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-
CC       (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
CC       {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}.
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DR   EMBL; CP000702; ABQ46805.1; -; Genomic_DNA.
DR   RefSeq; YP_001244381.1; NC_009486.1.
DR   ProteinModelPortal; A5IKT2; -.
DR   SMR; A5IKT2; 1-205.
DR   STRING; 390874.Tpet_0786; -.
DR   EnsemblBacteria; ABQ46805; ABQ46805; Tpet_0786.
DR   GeneID; 5170504; -.
DR   KEGG; tpt:Tpet_0786; -.
DR   PATRIC; 23944364; VBIThePet65348_0795.
DR   eggNOG; COG0135; -.
DR   HOGENOM; HOG000161598; -.
DR   KO; K01817; -.
DR   OMA; DILQLHG; -.
DR   OrthoDB; EOG6N94DF; -.
DR   BioCyc; TPET390874:GHJI-816-MONOMER; -.
DR   UniPathway; UPA00035; UER00042.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001240; PRAI_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Isomerase; Tryptophan biosynthesis.
FT   CHAIN         1    205       N-(5'-phosphoribosyl)anthranilate
FT                                isomerase.
FT                                /FTId=PRO_1000018645.
SQ   SEQUENCE   205 AA;  22982 MW;  FB7B22114F7A28DF CRC64;
     MVRVKICGIT NLEDALFSVE SGADAVGFVF YPKSKRYISP EDARRISVEL PPFVFRVGVF
     VNEEPEKILD VASYVQLNAV QLHGEEPIEL CRKIAERILV IKAVGISNER DIERALNYRE
     FPVLLDTKTP EYGGSGKTFD WSLILPYRDQ FRYLVLSGGL NPDNVRSAID MVRPFAVDVS
     SGVEAFPGKK DHDSIKTFIK NAKGL
//
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