Pyruvate kinase - Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

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Q9YEU2 (KPYK_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Pyruvate kinase
Short name=PK
EC=2.7.1.40

Gene names

Name:	pyk
Ordered Locus Names:	APE_0489

Organism

Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]

Taxonomic identifier

272557 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum ›

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Divalent metal cations. Ref.2
Enzyme regulation	Not activated by classical allosteric effectors.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer. Ref.2
Sequence similarities	Belongs to the pyruvate kinase family.
Biophysicochemical properties	Kinetic parameters: V_max=53 µmol/min/mg enzyme (at 65 degrees Celsius) Ref.2 pH dependence: Optimum pH is 6.1. Temperature dependence: Optimum temperature is higher than 95 degrees Celsius. Still active after 120 minutes at 100 degrees Celsius.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 458

458

Pyruvate kinase

PRO_0000295180

Sites

Metal binding

Potassium By similarity

Metal binding

Potassium By similarity

Metal binding

Potassium By similarity

Metal binding

214

Magnesium By similarity

Metal binding

238

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

237

Substrate; via amide nitrogen By similarity

Binding site

238

Substrate; via amide nitrogen By similarity

Binding site

270

Substrate By similarity

Site

212

Transition state stabilizer By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9YEU2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3D8E11A37A0088E3
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FASTA

458

50,487

        10         20         30         40         50         60 
MRGPVKIVAT VGPSSSSASI LAQMLSLGVD VARINASHGG VEQWNSMLES LRRAEEAVGK 

        70         80         90        100        110        120 
RVGVAVDLEG PRVRTGNSEP VKLEKGDLVT LGFMEGDVPV DARQFFETID EGDIVLLDDG 

       130        140        150        160        170        180 
KIILQVESVE GFRVKARVLE GGVLGPRKGV VVRGKEPDLP PLSAKDRRAL EFFADKGVSH 

       190        200        210        220        230        240 
VYVSFARSAE HVEKVRTVVR RLGLRQARIF AKIEGPSGVS RIGEIAEASD GVIIARGDLG 

       250        260        270        280        290        300 
MHYSLEELPE IQELIVWEAR KRYKTVVLAT EFLSSMIEKP VPTRSEVVDI YQAVLQTADA 

       310        320        330        340        350        360 
LMLTGETAIG KYPVKSVQWM AKISSRAYKK LATSPPERPR PTSTPYKLAL GLVELAESLD 

       370        380        390        400        410        420 
SPLVVYSKTG RFAERLASFK PLKTFYVGVP SREVERVVRH LWGAEPIVVG DYPYEAGLAK 

       430        440        450 
TYEKLRRENI IHGDETVVEA AWSSERGIYI IRVRNLEF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. Kikuchi H. DNA Res. 6:83-101(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
[2]	"Comparative analysis of pyruvate kinases from the hyperthermophilic archaea Archaeoglobus fulgidus, Aeropyrum pernix, and Pyrobaculum aerophilum and the hyperthermophilic bacterium Thermotoga maritima: unusual regulatory properties in hyperthermophilic archaea." Johnsen U., Hansen T., Schoenheit P. J. Biol. Chem. 278:25417-25427(2003) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, REGULATION. Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000002 Genomic DNA. Translation: BAA79454.1.
PIR	B72745.
RefSeq	NP_147274.1. NC_000854.2.
3D structure databases
HSSP	HSSP built from PDB template 2G50 based on UniProtKB P11974.
ProteinModelPortal	Q9YEU2.
ModBase	Search...
Protein-protein interaction databases
STRING	272557.APE_0489.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA79454; BAA79454; APE_0489.
GeneID	1444673.
KEGG	ape:APE_0489.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021558.
KO	K00873.
OMA	MHYSLEE.
ProtClustDB	CLSK2747737.
Enzyme and pathway databases
BioCyc	APER272557:GJD6-377-MONOMER.
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. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK_AERPE

Accession

Primary (citable) accession number: Q9YEU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents