TRPF_THEMA
ID TRPF_THEMA Reviewed; 205 AA.
AC Q56320;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE Short=PRAI;
DE EC=5.3.1.24;
GN Name=trpF; OrderedLocusNames=TM_0139;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7556082; DOI=10.1002/j.1460-2075.1995.tb00118.x;
RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.;
RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the
RT hyperthermophile Thermotoga maritima.";
RL EMBO J. 14:4395-4402(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9166771; DOI=10.1021/bi962718q;
RA Hennig M., Sterner R., Kirschner K., Jansonius J.N.;
RT "Crystal structure at 2.0-A resolution of phosphoribosyl anthranilate
RT isomerase from the hyperthermophile Thermotoga maritima: possible
RT determinants of protein stability.";
RL Biochemistry 36:6009-6016(1997).
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;
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000305}.
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DR EMBL; X92729; CAA63390.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35232.1; -; Genomic_DNA.
DR PIR; S59048; S59048.
DR RefSeq; NP_227954.1; NC_000853.1.
DR RefSeq; WP_004082737.1; NZ_CP011107.1.
DR PDB; 1DL3; X-ray; 2.70 A; A/B=1-205.
DR PDB; 1LBM; X-ray; 2.80 A; A=1-205.
DR PDB; 1NSJ; X-ray; 2.00 A; A=1-205.
DR PDBsum; 1DL3; -.
DR PDBsum; 1LBM; -.
DR PDBsum; 1NSJ; -.
DR AlphaFoldDB; Q56320; -.
DR SMR; Q56320; -.
DR STRING; 243274.THEMA_04110; -.
DR DrugBank; DB03543; 1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate.
DR PRIDE; Q56320; -.
DR EnsemblBacteria; AAD35232; AAD35232; TM_0139.
DR KEGG; tma:TM0139; -.
DR eggNOG; COG0135; Bacteria.
DR InParanoid; Q56320; -.
DR OMA; FYAKSPR; -.
DR OrthoDB; 1854712at2; -.
DR BioCyc; MetaCyc:MON-301; -.
DR BRENDA; 5.3.1.24; 6331.
DR SABIO-RK; Q56320; -.
DR UniPathway; UPA00035; UER00042.
DR EvolutionaryTrace; Q56320; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR044643; TrpF_fam.
DR PANTHER; PTHR42894; PTHR42894; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Isomerase; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..205
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_0000154390"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1NSJ"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1NSJ"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1NSJ"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:1NSJ"
SQ SEQUENCE 205 AA; 23041 MW; 9E1D76948C7EAE5E CRC64;
MVRVKICGIT NLEDALFSVE SGADAVGFVF YPKSKRYISP EDARRISVEL PPFVFRVGVF
VNEEPEKILD VASYVQLNAV QLHGEEPIEL CRKIAERILV IKAVGVSNER DMERALNYRE
FPILLDTKTP EYGGSGKTFD WSLILPYRDR FRYLVLSGGL NPENVRSAID VVRPFAVDVS
SGVEAFPGKK DHDSIKMFIK NAKGL
