Q42527 (PAI2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
Subcellular location	Plastid › chloroplast 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 process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Cellular component	Chloroplast Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tryptophan biosynthetic process Inferred from mutant phenotype Ref.1. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	phosphoribosylanthranilate 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 32	32	Chloroplast Potential
	Chain	33 – 275	243	N-(5'-phosphoribosyl)anthranilate isomerase 2, chloroplastic		PRO_0000417454
Natural variations
	Alternative sequence	146	1	Q → QVLYILIDFDFALTKVIFST LLTVDSYGFLQ in isoform 2.		VSP_043742
	Alternative sequence	201 – 225	25	SGHGF…WLLAG → RYQEQLFNFFRIVMYSLEEK FKQSL in isoform 2.		VSP_043743
	Alternative sequence	226 – 275	50	Missing in isoform 2.		VSP_043744

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: FF55DC899925F2C7	FASTA	275	29,619
	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
	Isoform 2 [UniParc]. Checksum: FF8F1A55B2944244	FASTA	255	28,314
	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 DLELVQVLYI LIDFDFALTK VIFSTLLTVD SYGFLQLHGN 190 200 210 220 230 240 GSRAAFSRLV RKRRVIYVLN ANQDGKLLNE VPEEDCHLAD WILVDSATGG RYQEQLFNFF 250 RIVMYSLEEK FKQSL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
+	Additional computationally mapped references.

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.
IPI	IPI00539464.
RefSeq	NP_196178.2. NM_120641.4. NP_974734.1. NM_203005.2.
UniGene	At.273. At.48165. At.48988.
3D structure databases
ProteinModelPortal	Q42527.
SMR	Q42527. Positions 68-273.
ModBase	Search...
Proteomic databases
PRIDE	Q42527.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G05590.1; AT5G05590.1; AT5G05590.
GeneID	830442.
KEGG	ath:AT5G05590.
Organism-specific databases
TAIR	At5g05590.
Phylogenomic databases
HOGENOM	HOG000161598.
InParanoid	Q42527.
KO	K01817.
OMA	ISALHCE.
PhylomeDB	Q42527.
ProtClustDB	PLN02363.
Enzyme and pathway databases
UniPathway	UPA00035; UER00042.
Gene expression databases
ArrayExpress	Q42527.
Genevestigator	Q42527.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR001240. PRAI_dom. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Pfam	PF00697. PRAI. 1 hit. [Graphical view]
SUPFAM	SSF51366. RibP_bind_barrel. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PAI2_ARATH

Accession

Primary (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:	May 29, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program