Reviewed, UniProtKB/Swiss-Prot Q9YEU2 (KPYK_AERPE)

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 [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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: Vmax=53 µmol/min/mg enzyme (at 65 degrees Celsius) 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 Pyruvate
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Active site	212	1	By similarity
	Metal binding	214	1	Magnesium By similarity
	Metal binding	235	1	Magnesium By similarity
	Metal binding	236	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YEU2-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 3D8E11A37A0088E3	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

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. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 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: 12654928] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, REGULATION. Strain: K1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000002 Genomic DNA. Translation: BAA79454.1.
PIR	B72745.
RefSeq	NP_147274.1.
3D structure databases
HSSP	HSSP built from PDB template 1PKN based on UniProtKB P11974.
ModBase	Search...
Genome annotation databases
GeneID	1444673.
GenomeReviews	Gene locus APE_0489 in contig BA000002_GR.
KEGG	ape:APE_0489.
NMPDR	fig|272557.1.peg.382.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9YEU2.
OMA	Q9YEU2. IMLSDET.
Enzyme and pathway databases
BRENDA	2.7.1.40. 256344.
Family and domain databases
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PANTHER	PTHR11817. Pyruvate_kinase. 1 hit.
Pfam	PF00224. PK. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
ProDom	PD001009. Pyruvate_kinase. 2 hits. [Graphical view] [Entries sharing at least one domain]
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:	June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)