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P55964 (KPYG_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate kinase isozyme G, chloroplastic

EC=2.7.1.40
OrganismRicinus communis (Castor bean)
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Protein attributes

Sequence length418 AA.
Sequence statusFragment.
Protein existenceEvidence 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

Plastidchloroplast.

Tissue specificity

Expressed in developing and germinating endosperm and in roots.

Sequence similarities

Belongs to the pyruvate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentChloroplast
Plastid
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Pyruvate
   Molecular functionKinase
Transferase
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 418›418Pyruvate kinase isozyme G, chloroplastic
PRO_0000112126

Sites

Metal binding141Potassium By similarity
Metal binding151Potassium; via carbonyl oxygen By similarity
Metal binding1651Magnesium By similarity
Metal binding1891Magnesium By similarity
Binding site1881Substrate; via amide nitrogen By similarity
Binding site1891Substrate; via amide nitrogen By similarity
Binding site2211Substrate By similarity
Site1631Transition state stabilizer By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P55964 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: D22531C1B25ECF85

FASTA41846,007
        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 

« Hide

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

ProteinModelPortalP55964.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00188.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
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]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPYG_RICCO
AccessionPrimary (citable) accession number: P55964
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways