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P55964

- KPYG_RICCO

UniProt

P55964 - KPYG_RICCO

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Protein

Pyruvate kinase isozyme G, chloroplastic

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141PotassiumBy similarity
Metal bindingi15 – 151Potassium; via carbonyl oxygenBy similarity
Sitei163 – 1631Transition state stabilizerBy similarity
Metal bindingi165 – 1651MagnesiumBy similarity
Binding sitei188 – 1881Substrate; via amide nitrogenBy similarity
Metal bindingi189 – 1891MagnesiumBy similarity
Binding sitei189 – 1891Substrate; via amide nitrogenBy similarity
Binding sitei221 – 2211SubstrateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Pyruvate

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase isozyme G, chloroplastic (EC:2.7.1.40)
OrganismiRicinus communis (Castor bean)
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 418›418Pyruvate kinase isozyme G, chloroplasticPRO_0000112126Add
BLAST

Expressioni

Tissue specificityi

Expressed in developing and germinating endosperm and in roots.

Structurei

3D structure databases

ProteinModelPortaliP55964.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P55964-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
NAQSHDNVVS IMLDTKGPEV RSGDVPQPML KEGQEFNPTI RRGVSTQDTV
60 70 80 90 100
SVNYDDFVND VVVGDILLVD GGMMSLAVKS KTSDLVKCVV VDGGELKSRR
110 120 130 140 150
HLNVRGKSAR LPSITDKDWG DIKFGVDNQV DFYAVSFVKD AKVVHELKEY
160 170 180 190 200
LKRCNADIHV IVKIESADSI PNLHSIISAS DGAMVARGDL GAELPIEEVP
210 220 230 240 250
LLQEDIIRRC HSMQKPVIVA TNMLESMINH PTPTRAEVSD IAIAVREGAD
260 270 280 290 300
AVMLSGETAH GKYPLKAVRV MHTVALRTES SSPVNTTPPA QGAYKGHMGE
310 320 330 340 350
MFAFHATIMA NTLNTPIIVF TRTGSMAVLL SHYQPASTIF AFTNEERIKQ
360 370 380 390 400
RLSLYRGVMP IYMEFSSDAE ETFSRALQLL LNKGLLVEGE HVTLVQSGAQ
410
PIWRQESTHH IQVRKVQN
Length:418
Mass (Da):46,007
Last modified:November 1, 1997 - v1
Checksum:iD22531C1B25ECF85
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Cross-referencesi

3D structure databases

ProteinModelPortali P55964.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. 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 ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiKPYG_RICCO
AccessioniPrimary (citable) accession number: P55964
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3