Q93Z53 (PKP3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plastidial pyruvate kinase 3, chloroplastic
Short name=PKp3
EC=2.7.1.40

Alternative name(s):
Pyruvate kinase I
Pyruvate kinase isozyme B2, chloroplastic
Short name=PKP-BETA2
Short name=Plastidic pyruvate kinase beta subunit 2

Gene names

Name:	PKP3
Ordered Locus Names:	At1g32440
ORF Names:	F5D14.22

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

General annotation (Comments)

Function	Required for plastidial pyruvate kinase activity By similarity.
Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Ref.4 Potassium. Ref.4
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Oligomer of alpha and beta subunits. Ref.4
Subcellular location	Plastid › chloroplast stroma Ref.4 Ref.6.
Tissue specificity	Expressed at low levels in roots, leaves, inflorescences, siliques, pollen, seeds and flowers. Ref.4 Ref.5
Sequence similarities	Belongs to the pyruvate kinase family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.8-8.0. Ref.4
Sequence caution	The sequence AAF81342.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from genetic interaction Ref.4. Source: TAIR glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway seed maturation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	chloroplast stroma Inferred from direct assay Ref.4. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from direct assay Ref.4. Source: UniProtKB potassium ion binding Inferred from direct assay Ref.4. Source: UniProtKB pyruvate kinase activity Inferred from direct assay Ref.4. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 55	55	Chloroplast Potential
	Chain	56 – 571	516	Plastidial pyruvate kinase 3, chloroplastic		PRO_0000416989
Sites
	Metal binding	131	1	Potassium By similarity
	Metal binding	164	1	Potassium By similarity
	Metal binding	165	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	316	1	Magnesium Potential
	Metal binding	340	1	Magnesium By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	339	1	Substrate; via amide nitrogen By similarity
	Binding site	340	1	Substrate; via amide nitrogen By similarity
	Binding site	372	1	Substrate By similarity
	Site	314	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q93Z53 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 4C61979F639274B1	FASTA	571	62,615
	10 20 30 40 50 60 MAAYGQISSG MTVDPQVLSS SRNIGVSLSP LRRTLIGAGV RSTSISLRQC SLSVRSIKIS 70 80 90 100 110 120 EDSRKPKAYA ENGAFDVGVL DSSSYRLADS RTSSNDSRRK TKIVCTIGPS SSSREMIWKL 130 140 150 160 170 180 AEAGMNVARL NMSHGDHASH QITIDLVKEY NSLFVDKAIA IMLDTKGPEV RSGDVPQPIF 190 200 210 220 230 240 LEEGQEFNFT IKRGVSLKDT VSVNYDDFVN DVEVGDILLV DGGMMSLAVK SKTSDLVKCV 250 260 270 280 290 300 VIDGGELQSR RHLNVRGKSA TLPSITDKDW EDIKFGVDNQ VDFYAVSFVK DAKVVHELKN 310 320 330 340 350 360 YLKTCSADIS VIVKIESADS IKNLPSIISA CDGAMVARGD LGAELPIEEV PLLQEEIIRR 370 380 390 400 410 420 CRSIHKPVIV ATNMLESMIN HPTPTRAEVS DIAIAVREGA DAIMLSGETA HGKFPLKAVN 430 440 450 460 470 480 VMHTVALRTE ASLPVRTSAS RTTAYKGHMG QMFAFHASIM ANTLSSPLIV FTRTGSMAVL 490 500 510 520 530 540 LSHYRPSATI FAFTNQRRIM QRLALYQGVM PIYMEFSDDA EDTYARSLKL LQDENMLKEG 550 560 570 QHVTLVQSGS QPIWREESTH LIQVRKIKIG G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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]. Strain: cv. Columbia.
[4]	"A heteromeric plastidic pyruvate kinase complex involved in seed oil biosynthesis in Arabidopsis." Andre C., Froehlich J.E., Moll M.R., Benning C. Plant Cell 19:2006-2022(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY.
[5]	"Function of plastidial pyruvate kinases in seeds of Arabidopsis thaliana." Baud S., Wuilleme S., Dubreucq B., de Almeida A., Vuagnat C., Lepiniec L., Miquel M., Rochat C. Plant J. 52:405-419(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE. Strain: cv. Wassilewskija.
[6]	"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome." Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J. PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC007767 Genomic DNA. Translation: AAF81342.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE31487.1. AY058121 mRNA. Translation: AAL25538.1. BT001147 mRNA. Translation: AAN64538.1.
IPI	IPI00519857.
PIR	F86449.
RefSeq	NP_564402.1. NM_102979.1.
UniGene	At.66798.
3D structure databases
HSSP	HSSP built from PDB template 1E0T based on UniProtKB P14178.
ProteinModelPortal	Q93Z53.
SMR	Q93Z53. Positions 99-512.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G32440.1-P.
Proteomic databases
PaxDb	Q93Z53.
PRIDE	Q93Z53.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G32440.1; AT1G32440.1; AT1G32440.
GeneID	840138.
KEGG	ath:AT1G32440.
Organism-specific databases
TAIR	At1g32440.
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021559.
InParanoid	Q93Z53.
KO	K00873.
OMA	MHYSLEE.
PhylomeDB	Q93Z53.
ProtClustDB	PLN02623.
Enzyme and pathway databases
SABIO-RK	Q93Z53.
UniPathway	UPA00109; UER00188.
Gene expression databases
ArrayExpress	Q93Z53.
Genevestigator	Q93Z53.
Family and domain databases
Gene3D	2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit.
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. IPR011037. Pyrv_Knase-like_insert_dom. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. IPR015795. Pyrv_Knase_C. IPR015806. Pyrv_Knase_insert_dom. [Graphical view]
PANTHER	PTHR11817. PTHR11817. 1 hit.
Pfam	PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01064. pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PKP3_ARATH

Accession

Primary (citable) accession number: Q93Z53
Secondary accession number(s): Q9LQL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2012
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program