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Q42563 (APT2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 82. Feed History...

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

Names and origin

Protein namesRecommended name:
Adenine phosphoribosyltransferase 2
Short name=APRT 2
EC=2.4.2.7
Gene names
Name:APT2
Ordered Locus Names:At1g80050
ORF Names:F18B13.14
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.

Catalytic activity

AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate.

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processadenine salvage

Traceable author statement. Source: TAIR

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: TAIR

   Molecular functionadenine phosphoribosyltransferase activity

Inferred from direct assay Ref.1. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192Adenine phosphoribosyltransferase 2
PRO_0000149515

Experimental info

Sequence conflict401L → M in CAA65610. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q42563 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 29D648EE59BBB026

FASTA19221,009
        10         20         30         40         50         60 
MFAVENGLQG DPRLKAISDA IRVIPHFPKT GIMFQDITTL LLDPVAFKHV VDIFVDRYKH 

        70         80         90        100        110        120 
MNISLVAGVE ARGFIFGPPI ALAIGAKFVP LRKPGKLPGR VISEEYELEY GRDCLEMSVE 

       130        140        150        160        170        180 
AVKSEERALI IDDLVATGGT LSASINLLER AGAEVVECAC VVGLPKFKGQ CKLKGKPLYV 

       190 
LVEPNQFDEL TL

« Hide

References

« Hide 'large scale' references
[1]"A second form of adenine phosphoribosyltransferase in Arabidopsis thaliana with relative specificity towards cytokinins."
Schnorr K.M., Gaillard C., Biget E., Nygaard P., Laloue M.
Plant J. 9:891-898(1996) [PubMed: 8696367] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X96866 mRNA. Translation: CAA65609.1.
X96867 Genomic DNA. Translation: CAA65610.1.
AC009322 Genomic DNA. Translation: AAD55485.1.
CP002684 Genomic DNA. Translation: AEE36351.1.
AY072021 mRNA. Translation: AAL57714.1.
BT001122 mRNA. Translation: AAN64513.1.
IPIIPI00518989.
PIRS71272.
RefSeqNP_178122.1. NM_106654.2.
UniGeneAt.130.

3D structure databases

ProteinModelPortalQ42563.
SMRQ42563. Positions 11-185.
ModBaseSearch...

Protein-protein interaction databases

IntActQ42563. 2 interactions.
STRINGQ42563.

Proteomic databases

PRIDEQ42563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G80050.1; AT1G80050.1; AT1G80050.
GeneID844345.
GenomeReviewsGene locus AT1G80050 in contig CT485782_GR.
KEGGath:AT1G80050.
NMPDRfig|3702.1.peg.7590.

Organism-specific databases

TAIRAt1g80050.

Phylogenomic databases

eggNOGKOG1712.
GeneTreeEPGT00050000006146.
HOGENOMHBG703830.
InParanoidQ42563.
OMAISEEYEL.
PhylomeDBQ42563.
ProtClustDBPLN02293.

Enzyme and pathway databases

BRENDA2.4.2.7. 399.

Gene expression databases

ArrayExpressQ42563.
GenevestigatorQ42563.
GermOnlineAT1G80050. Arabidopsis thaliana.

Family and domain databases

InterProIPR005764. Ade_phspho_trans.
IPR000836. PRibTrfase.
[Graphical view]
KOK00759.
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR01090. Apt. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPT2_ARATH
AccessionPrimary (citable) accession number: Q42563
Secondary accession number(s): Q39004
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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