Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q27686

- KPYK_LEIME

UniProt

Q27686 - KPYK_LEIME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pyruvate kinase

Gene

PYK

Organism
Leishmania mexicana
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Activated by fructose 2,6-bisphosphate, activated by the effector in a non cooperative manner.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501SubstrateBy similarity
Metal bindingi52 – 521PotassiumBy similarity
Metal bindingi54 – 541PotassiumBy similarity
Metal bindingi84 – 841PotassiumBy similarity
Metal bindingi85 – 851Potassium; via carbonyl oxygenBy similarity
Sitei239 – 2391Transition state stabilizer
Metal bindingi241 – 2411MagnesiumBy similarity
Binding sitei264 – 2641Substrate; via amide nitrogenBy similarity
Metal bindingi265 – 2651MagnesiumBy similarity
Binding sitei265 – 2651Substrate; via amide nitrogenBy similarity
Binding sitei297 – 2971SubstrateBy 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, Potassium, Pyruvate

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:PYK
OrganismiLeishmania mexicana
Taxonomic identifieri5665 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Pyruvate kinasePRO_0000112102Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 86Combined sources
Beta strandi18 – 203Combined sources
Beta strandi22 – 298Combined sources
Turni30 – 323Combined sources
Helixi35 – 4410Combined sources
Beta strandi46 – 527Combined sources
Helixi58 – 7518Combined sources
Beta strandi80 – 845Combined sources
Beta strandi90 – 923Combined sources
Helixi96 – 983Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi107 – 1115Combined sources
Helixi114 – 1163Combined sources
Beta strandi117 – 1204Combined sources
Beta strandi122 – 1287Combined sources
Helixi132 – 1354Combined sources
Beta strandi141 – 1444Combined sources
Turni145 – 1484Combined sources
Beta strandi149 – 15810Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi177 – 1793Combined sources
Helixi192 – 20312Combined sources
Beta strandi207 – 2115Combined sources
Helixi217 – 22711Combined sources
Helixi229 – 2313Combined sources
Beta strandi234 – 2407Combined sources
Helixi243 – 2475Combined sources
Helixi249 – 2557Combined sources
Beta strandi256 – 2627Combined sources
Helixi263 – 2697Combined sources
Helixi272 – 28918Combined sources
Beta strandi293 – 3008Combined sources
Helixi301 – 3044Combined sources
Beta strandi306 – 3083Combined sources
Helixi311 – 32313Combined sources
Beta strandi326 – 3316Combined sources
Helixi332 – 3354Combined sources
Helixi340 – 35718Combined sources
Helixi360 – 36910Combined sources
Helixi377 – 39216Combined sources
Beta strandi395 – 4006Combined sources
Beta strandi402 – 4043Combined sources
Helixi405 – 4128Combined sources
Beta strandi419 – 4246Combined sources
Helixi426 – 4316Combined sources
Helixi432 – 4343Combined sources
Beta strandi438 – 4425Combined sources
Helixi445 – 4484Combined sources
Helixi455 – 46713Combined sources
Beta strandi476 – 4827Combined sources
Beta strandi491 – 4977Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PKLX-ray2.35A/B/C/D/E/F/G/H1-499[»]
3E0VX-ray3.30A/B/C/D/E/F1-499[»]
3E0WX-ray3.10A1-499[»]
3HQNX-ray2.00A/D1-499[»]
3HQOX-ray3.40A/B/C/K1-499[»]
3HQPX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-499[»]
3HQQX-ray5.07A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-499[»]
3IS4X-ray2.10A/B1-499[»]
3KTXX-ray2.10A/B1-499[»]
3PP7X-ray2.35A/B2-499[»]
3QV6X-ray2.85A/D1-499[»]
3QV7X-ray2.70A/B/C/D1-499[»]
3QV8X-ray2.45A/D1-499[»]
3SRKX-ray2.65A/B1-499[»]
ProteinModelPortaliQ27686.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ27686.

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: Complete.

Q27686-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQLAHNLTL SIFDPVANYR AARIICTIGP STQSVEALKG LIQSGMSVAR
60 70 80 90 100
MNFSHGSHEY HQTTINNVRQ AAAELGVNIA IALDTKGPEI RTGQFVGGDA
110 120 130 140 150
VMERGATCYV TTDPAFADKG TKDKFYIDYQ NLSKVVRPGN YIYIDDGILI
160 170 180 190 200
LQVQSHEDEQ TLECTVTNSH TISDRRGVNL PGCDVDLPAV SAKDRVDLQF
210 220 230 240 250
GVEQGVDMIF ASFIRSAEQV GDVRKALGPK GRDIMIICKI ENHQGVQNID
260 270 280 290 300
SIIEESDGIM VARGDLGVEI PAEKVVVAQK ILISKCNVAG KPVICATQML
310 320 330 340 350
ESMTYNPRPT RAEVSDVANA VFNGADCVML SGETAKGKYP NEVVQYMARI
360 370 380 390 400
CLEAQSALNE YVFFNSIKKL QHIPMSADEA VCSSAVNSVY ETKAKAMVVL
410 420 430 440 450
SNTGRSARLV AKYRPNCPIV CVTTRLQTCR QLNITQGVES VFFDADKLGH
460 470 480 490
DEGKEHRVAA GVEFAKSKGY VQTGDYCVVI HADHKVKGYA NQTRILLVE
Length:499
Mass (Da):54,405
Last modified:October 5, 2010 - v2
Checksum:i7B8CB0F9D3EDEBA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74944 Genomic DNA. Translation: CAA52898.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74944 Genomic DNA. Translation: CAA52898.2 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PKL X-ray 2.35 A/B/C/D/E/F/G/H 1-499 [» ]
3E0V X-ray 3.30 A/B/C/D/E/F 1-499 [» ]
3E0W X-ray 3.10 A 1-499 [» ]
3HQN X-ray 2.00 A/D 1-499 [» ]
3HQO X-ray 3.40 A/B/C/K 1-499 [» ]
3HQP X-ray 2.30 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-499 [» ]
3HQQ X-ray 5.07 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-499 [» ]
3IS4 X-ray 2.10 A/B 1-499 [» ]
3KTX X-ray 2.10 A/B 1-499 [» ]
3PP7 X-ray 2.35 A/B 2-499 [» ]
3QV6 X-ray 2.85 A/D 1-499 [» ]
3QV7 X-ray 2.70 A/B/C/D 1-499 [» ]
3QV8 X-ray 2.45 A/D 1-499 [» ]
3SRK X-ray 2.65 A/B 1-499 [» ]
ProteinModelPortali Q27686.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL5149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .

Miscellaneous databases

EvolutionaryTracei Q27686.

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. "Pyruvate kinase of Leishmania mexicana mexicana. Cloning and analysis of the gene, overexpression in Escherichia coli and characterization of the enzyme."
    Ernest I., Callens M., Opperdoes F.R., Michels P.A.M.
    Mol. Biochem. Parasitol. 64:43-54(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Michels P.A.M.
    Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO SER-383; TYR-390; ARG-405 AND SER-406.
  3. "The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity."
    Rigden D.J., Phillips S.E.V., Michels P.A.M., Fothergill-Gilmore L.A.
    J. Mol. Biol. 291:615-635(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
    Strain: MHOM/BZ/84/BEL46.

Entry informationi

Entry nameiKPYK_LEIME
AccessioniPrimary (citable) accession number: Q27686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 5, 2010
Last modified: November 26, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3