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Q5F9X5 (TRPF_NEIG1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:NGO0261
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090) [Reference proteome] [HAMAP]
Taxonomic identifier242231 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Sequence similarities

Belongs to the TrpF family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135
PRO_1000018613

Sequences

Sequence LengthMass (Da)Tools
Q5F9X5 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 99DF5E512DE00664

FASTA20822,531
        10         20         30         40         50         60 
MRKIRTKICG ITTPEDALYA AHAGADALGL VFYPQSPRAI DIIKAQKIAA ALPPFVSVVA 

        70         80         90        100        110        120 
LFVNESAQNI RRILAEVPIH IIQFHGDEDD AFCRQFDRPY IKAIRVQTAS DIRNAATRFP 

       130        140        150        160        170        180 
NAQALLFDAY HPSEYGGTGH RFDWTLLAEY SGKPWVLAGG LTPENVGEAV RITGAEAVDV 

       190        200 
SGGVEASKGK KDPAKVAAFI ATANRLSR 

« Hide

References

[1]"The complete genome sequence of Neisseria gonorrhoeae."
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. expand/collapse author list , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004969 Genomic DNA. Translation: AAW89012.1.
RefSeqYP_207424.1. NC_002946.2.

3D structure databases

ProteinModelPortalQ5F9X5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242231.NGO0261.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW89012; AAW89012; NGO0261.
GeneID3281084.
KEGGngo:NGO0261.
PATRIC20333489. VBINeiGon24812_0325.

Phylogenomic databases

eggNOGCOG0135.
HOGENOMHOG000161598.
KOK01817.
OMAFVNASRC.
OrthoDBEOG6N94DF.
ProtClustDBPRK01222.

Enzyme and pathway databases

BioCycNGON242231:GI2G-244-MONOMER.
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...

Entry information

Entry nameTRPF_NEIG1
AccessionPrimary (citable) accession number: Q5F9X5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 54 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

PATHWAY comments

Index of metabolic and biosynthesis pathways