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Q56320 (TRPF_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-(5'-phosphoribosyl)anthranilate isomerase

Short name=PRAI
EC=5.3.1.24
Gene names
Name:trpF
Ordered Locus Names:TM_0139
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00135

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00135

Subunit structure

Homodimer.

Sequence similarities

Belongs to the TrpF family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135
PRO_0000154390

Secondary structure

........................................ 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56320 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9E1D76948C7EAE5E

FASTA20523,041
        10         20         30         40         50         60 
MVRVKICGIT NLEDALFSVE SGADAVGFVF YPKSKRYISP EDARRISVEL PPFVFRVGVF 

        70         80         90        100        110        120 
VNEEPEKILD VASYVQLNAV QLHGEEPIEL CRKIAERILV IKAVGVSNER DMERALNYRE 

       130        140        150        160        170        180 
FPILLDTKTP EYGGSGKTFD WSLILPYRDR FRYLVLSGGL NPENVRSAID VVRPFAVDVS 

       190        200 
SGVEAFPGKK DHDSIKMFIK NAKGL 

« Hide

References

« Hide 'large scale' references
[1]"(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima."
Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.
EMBO J. 14:4395-4402(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Crystal structure at 2.0-A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability."
Hennig M., Sterner R., Kirschner K., Jansonius J.N.
Biochemistry 36:6009-6016(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92729 Genomic DNA. Translation: CAA63390.1.
AE000512 Genomic DNA. Translation: AAD35232.1.
PIRS59048.
RefSeqNP_227954.1. NC_000853.1.
YP_007976488.1. NC_021214.1.
YP_008990885.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DL3X-ray2.70A/B1-205[»]
1LBMX-ray2.80A1-205[»]
1NSJX-ray2.00A1-205[»]
ProteinModelPortalQ56320.
SMRQ56320. Positions 1-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0139.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35232; AAD35232; TM_0139.
GeneID896969.
KEGGtma:TM0139.
tmi:THEMA_04110.
tmm:Tmari_0137.
PATRIC23935120. VBITheMar51294_0138.

Phylogenomic databases

eggNOGCOG0135.
KOK01817.
OMADILQLHG.
OrthoDBEOG6N94DF.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-301.
UniPathwayUPA00035; UER00042.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ56320.

Entry information

Entry nameTRPF_THEMA
AccessionPrimary (citable) accession number: Q56320
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways