Q9SU38 (Q9SU38_ARATH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Adenine phosphoribosyl transferase 4 EMBL AEE83133.1

Submitted name:
Putative adenine phosphoribosyltransferase EMBL CAB41714.1

Gene names

Name:	AT4g12440 EMBL CAB41714.1
Synonyms:	APT4 EMBL AEE83133.1
Ordered Locus Names:	At4g12440 TAIR At4g12440
ORF Names:	AT4G12440 EMBL AEE83133.1

Organism

Arabidopsis thaliana (Mouse-ear cress) EMBL CAB41714.1

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

Ontologies

Keywords
Molecular function	Glycosyltransferase EMBL CAB41714.1 Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	adenine salvage Inferred from electronic annotation. Source: InterPro nucleoside metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	adenine phosphoribosyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9SU38 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 976CA5085032935B	FASTA	182	20,355
	10 20 30 40 50 60 MSENEVKDPR IDGIKTKIRV VPDFPKKGIM FQDITTLLLD PKAFKDTIDL FVERYRDMNI 70 80 90 100 110 120 SVVAGIEARG FIFGSPIALA IGAKFVPLRK PKKLPGQIIF EEYELEYGSD RLEMHVEAVD 130 140 150 160 170 180 SGDRALVVDD LIATGGTLCA AMNLLKRVGA EVIECACVIE LPELKGRERL EGKPLYVLVE YR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." EU, CSHL and WU Arabidopsis Sequencing Project Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	EU Arabidopsis sequencing project Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Arabidopsis Open Reading Frame (ORF) Clones." Yamada K., Chan M.M., Chang C.H., Dale J.M., Deng J.M., Hsuan V.W., Lee J.M., Quach H.L., Tang C.C., Toriumi M., Wu H.C., Yu G., Bowser L., Chen H., Cheuk R., Jones T., Karlin-Neumann G., Kim C. , Lam B., Lin J., Miranda M., Nguyen M., Palm C.J., Shinn P., Southwick A., Davis R.W., Ecker J.R., Theologis A. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	Peters S.A., van Staveren M., Dirkse W., Stiekema W., Mewes H.W., Lemcke K., Mayer K.F.X. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY133689 mRNA. Translation: AAM91623.1. CP002687 Genomic DNA. Translation: AEE83133.1. AL049730 Genomic DNA. Translation: CAB41714.1. AL161534 Genomic DNA. Translation: CAB78287.1.
IPI	IPI00546006.
PIR	T07636.
RefSeq	NP_192981.1. NM_117314.2.
UniGene	At.33474.
3D structure databases
HSSP	HSSP built from PDB template 1G2Q based on UniProtKB P49435.
ProteinModelPortal	Q9SU38.
SMR	Q9SU38. Positions 7-182.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SU38.
Proteomic databases
PRIDE	Q9SU38.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G12440.2; AT4G12440.2; AT4G12440.
GeneID	826856.
KEGG	ath:AT4G12440.
NMPDR	fig|3702.1.peg.18919.
Organism-specific databases
TAIR	At4g12440.
Phylogenomic databases
GeneTree	EPGT00050000006146.
InParanoid	Q9SU38.
OMA	ILECLVV.
PhylomeDB	Q9SU38.
ProtClustDB	PLN02293.
Enzyme and pathway databases
BRENDA	2.4.2.7. 302.
Gene expression databases
Genevestigator	Q9SU38.
Family and domain databases
HAMAP	MF_00004. Aden_phosphoribosyltr. [Tree]
InterPro	IPR005764. Ade_phspho_trans. IPR000836. PRibTrfase. [Graphical view]
KO	K00759.
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01090. Apt. 1 hit.
ProtoNet	Search...

Entry information

Entry name

Q9SU38_ARATH

Accession

Primary (citable) accession number: Q9SU38

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)