P55964 (KPYG_RICCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Pyruvate kinase isozyme G, chloroplastic EC=2.7.1.40
Organism	Ricinus communis (Castor bean) [Complete proteome]
Taxonomic identifier	3988 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

Protein attributes

Sequence length	418 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium By similarity. Potassium By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subcellular location	Plastid › chloroplast.
Tissue specificity	Expressed in developing and germinating endosperm and in roots.
Sequence similarities	Belongs to the pyruvate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Chloroplast Plastid
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 418	›418	Pyruvate kinase isozyme G, chloroplastic		PRO_0000112126
Sites
	Metal binding	14	1	Potassium By similarity
	Metal binding	15	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	165	1	Magnesium By similarity
	Metal binding	189	1	Magnesium By similarity
	Binding site	188	1	Substrate; via amide nitrogen By similarity
	Binding site	189	1	Substrate; via amide nitrogen By similarity
	Binding site	221	1	Substrate By similarity
	Site	163	1	Transition state stabilizer By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P55964 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: D22531C1B25ECF85	FASTA	418	46,007
	10 20 30 40 50 60 NAQSHDNVVS IMLDTKGPEV RSGDVPQPML KEGQEFNPTI RRGVSTQDTV SVNYDDFVND 70 80 90 100 110 120 VVVGDILLVD GGMMSLAVKS KTSDLVKCVV VDGGELKSRR HLNVRGKSAR LPSITDKDWG 130 140 150 160 170 180 DIKFGVDNQV DFYAVSFVKD AKVVHELKEY LKRCNADIHV IVKIESADSI PNLHSIISAS 190 200 210 220 230 240 DGAMVARGDL GAELPIEEVP LLQEDIIRRC HSMQKPVIVA TNMLESMINH PTPTRAEVSD 250 260 270 280 290 300 IAIAVREGAD AVMLSGETAH GKYPLKAVRV MHTVALRTES SSPVNTTPPA QGAYKGHMGE 310 320 330 340 350 360 MFAFHATIMA NTLNTPIIVF TRTGSMAVLL SHYQPASTIF AFTNEERIKQ RLSLYRGVMP 370 380 390 400 410 IYMEFSSDAE ETFSRALQLL LNKGLLVEGE HVTLVQSGAQ PIWRQESTHH IQVRKVQN

References

[1]	"Molecular characterization of plastid pyruvate kinase from castor and tobacco." Blakeley S.D., Gottlob-Mchugh S., Wan J., Crews L., Miki B., Ko K., Dennis D.T. Plant Mol. Biol. 27:79-89(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Baker 296. Tissue: Seed.

Cross-references

3D structure databases
ProteinModelPortal	P55964.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00109; UER00188.
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

KPYG_RICCO

Accession

Primary (citable) accession number: P55964

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program