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Q42527 (PAI2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-(5'-phosphoribosyl)anthranilate isomerase 2, chloroplastic

EC=5.3.1.24
Gene names
Name:PAI2
Ordered Locus Names:At5g05590
ORF Names:MOP10.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Subcellular location

Plastidchloroplast Ref.7.

Tissue specificity

Expressed in roots and shoots. Ref.8

Induction

By silver nitrate and UV irradiation. Ref.8

Sequence similarities

Belongs to the TrpF family.

Sequence caution

The sequence BAB11548.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BX829410 differs from that shown. Reason: Sequencing errors.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Tryptophan biosynthesis
   Cellular componentChloroplast
Plastid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtryptophan biosynthetic process

Inferred from mutant phenotype Ref.1. Source: TAIR

   Cellular_componentchloroplast

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionphosphoribosylanthranilate isomerase activity

Inferred from sequence or structural similarity Ref.1. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q42527-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q42527-2)

The sequence of this isoform differs from the canonical sequence as follows:
     146-146: Q → QVLYILIDFDFALTKVIFSTLLTVDSYGFLQ
     201-225: SGHGFNWAQFKLPSVRSRNGWLLAG → RYQEQLFNFFRIVMYSLEEKFKQSL
     226-275: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Chloroplast Potential
Chain33 – 275243N-(5'-phosphoribosyl)anthranilate isomerase 2, chloroplastic HAMAP-Rule MF_00135
PRO_0000417454

Natural variations

Alternative sequence1461Q → QVLYILIDFDFALTKVIFST LLTVDSYGFLQ in isoform 2.
VSP_043742
Alternative sequence201 – 22525SGHGF…WLLAG → RYQEQLFNFFRIVMYSLEEK FKQSL in isoform 2.
VSP_043743
Alternative sequence226 – 27550Missing in isoform 2.
VSP_043744

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FF55DC899925F2C7

FASTA27529,619
        10         20         30         40         50         60 
MSTGISTDLH VHFGALNFSK TYKSGLSNRT VSFSRVGYAQ NRKLSCSVSN TENVAPKDDE 

        70         80         90        100        110        120 
RGKDRPLVKM CGITSARDAA MAVEAGADFI GMIIWPHSKR SISLSVAKDI SKVAREGGAK 

       130        140        150        160        170        180 
PVGVFVEDDD NTILRAADSS DLELVQLHGN GSRAAFSRLV RKRRVIYVLN ANQDGKLLNE 

       190        200        210        220        230        240 
VPEEDCHLAD WILVDSATGG SGHGFNWAQF KLPSVRSRNG WLLAGGINPT NVSEALSILQ 

       250        260        270 
PDGIDVSSGI CGTDGIQKDK SKISSFITAV RSVHY 

« Hide

Isoform 2 [UniParc].

Checksum: FF8F1A55B2944244
Show »

FASTA25528,314

References

« Hide 'large scale' references
[1]"Arabidopsis phosphoribosylanthranilate isomerase: molecular genetic analysis of triplicate tryptophan pathway genes."
Li J., Zhao J., Rose A.B., Schmidt R., Last R.L.
Plant Cell 7:447-461(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[6]"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM2).
Strain: cv. Columbia.
[7]"Immunological characterization and chloroplast localization of the tryptophan biosynthetic enzymes of the flowering plant Arabidopsis thaliana."
Zhao J., Last R.L.
J. Biol. Chem. 270:6081-6087(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Differential expression of triplicate phosphoribosylanthranilate isomerase isogenes in the tryptophan biosynthetic pathway of Arabidopsis thaliana (L.) Heynh."
He Y., Li J.
Planta 212:641-647(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18968 Genomic DNA. Translation: AAC49003.1.
AB005241 Genomic DNA. Translation: BAB11548.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED90894.1.
CP002688 Genomic DNA. Translation: AED90895.1.
BT003070 mRNA. Translation: AAO23635.1.
AK227265 mRNA. Translation: BAE99293.1.
BX829410 mRNA. No translation available.
RefSeqNP_196178.2. NM_120641.4.
NP_974734.1. NM_203005.2.
UniGeneAt.273.
At.48165.
At.48988.

3D structure databases

ProteinModelPortalQ42527.
SMRQ42527. Positions 6-273.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ42527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G05590.1; AT5G05590.1; AT5G05590. [Q42527-1]
GeneID830442.
KEGGath:AT5G05590.

Organism-specific databases

TAIRAT5G05590.

Phylogenomic databases

HOGENOMHOG000161598.
InParanoidQ42527.
KOK01817.
OMAFERQAID.
PhylomeDBQ42527.
ProtClustDBPLN02363.

Enzyme and pathway databases

BioCycARA:AT5G05590-MONOMER.
UniPathwayUPA00035; UER00042.

Gene expression databases

GenevestigatorQ42527.

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 namePAI2_ARATH
AccessionPrimary (citable) accession number: Q42527
Secondary accession number(s): F4K0R4, Q9FFF7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names