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Protein

Pyruvate kinase

Gene
N/A
Organism
Leishmania braziliensis
Status
Reviewed-Annotation score: 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:

Pathway:iglycolysis

This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (LBRM_30_2950)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Enolase, Enolase (ENOL)
  5. Pyruvate kinase (LBRM_34_0010), Pyruvate kinase, Pyruvate kinase (LBRM_34_0040), Pyruvate kinase (LBRM_34_0060)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481SubstrateBy similarity
Metal bindingi50 – 501PotassiumBy similarity
Metal bindingi52 – 521PotassiumBy similarity
Metal bindingi82 – 821PotassiumBy similarity
Metal bindingi83 – 831Potassium; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

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

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
OrganismiLeishmania braziliensis
Taxonomic identifieri5660 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmaniaLeishmania braziliensis species complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›91›91Pyruvate kinasePRO_0000112101Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi420245.XP_001562199.1.

Structurei

3D structure databases

ProteinModelPortaliQ04668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR015793. Pyrv_Knase_brl.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q04668-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLAHNLTL SIFEPLRTTG TIVCTIGPST QSVEALKGLI KSGMSVARMN
60 70 80 90
FSHGSHEYHQ TTINNVRQAA AELGVNIAIA LDTKGPEIRT G
Length:91
Mass (Da):9,704
Last modified:February 1, 1994 - v1
Checksum:i6D5E18C18D5E759D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei91 – 911

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08597 mRNA. Translation: AAA29260.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08597 mRNA. Translation: AAA29260.1.

3D structure databases

ProteinModelPortaliQ04668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420245.XP_001562199.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR015793. Pyrv_Knase_brl.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Martinez C., Hung A., Alonso G., Ponte A., Ramirez J.L.
    Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiKPYK_LEIBR
AccessioniPrimary (citable) accession number: Q04668
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 22, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.