Q4L739 (KPYK_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	pyk
Ordered Locus Names:	SH1227

Organism

Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]

Taxonomic identifier

279808 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus haemolyticus

Protein attributes

Sequence length	586 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium By similarity. Potassium By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Sequence similarities	Belongs to the pyruvate kinase family. In the C-terminal section; belongs to the PEP-utilizing enzyme family.

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 – 586	586	Pyruvate kinase		PRO_0000294139
Sites
	Metal binding	34	1	Potassium By similarity
	Metal binding	36	1	Potassium By similarity
	Metal binding	66	1	Potassium By similarity
	Metal binding	67	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	222	1	Magnesium By similarity
	Metal binding	246	1	Magnesium By similarity
	Binding site	32	1	Substrate By similarity
	Binding site	245	1	Substrate; via amide nitrogen By similarity
	Binding site	246	1	Substrate; via amide nitrogen By similarity
	Binding site	278	1	Substrate By similarity
	Site	220	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4L739 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: E6C0B61B47DCE8CE	FASTA	586	63,019
	10 20 30 40 50 60 MRKTKIVCTI GPASESEEML EKLMKAGMNV ARLNFSHGSH EEHKARIDTI RKVADRLGKT 70 80 90 100 110 120 IGILLDTKGP EIRTHDMKDG LIMLEKGKEV IVSMSQVEGT PEKFSVTYED LINDVQVGSY 130 140 150 160 170 180 ILLDDGLVEL QVKDIDKTKG EVKCDILNTG ELKNKKGVNL PGVKVNLPGI TDKDADDILF 190 200 210 220 230 240 GIKEDVDYIA ASFVRRPSDV LDIREILERE NNHNITIFPK IENQEGIDNI EEILEVSDGL 250 260 270 280 290 300 MVARGDMGVE IPPESVPIVQ KDLIRKCNKL GKPVITATQM LDSMQRNPRA TRAEASDVAN 310 320 330 340 350 360 AIYDGTDAVM LSGETAAGLY PEEAVKTMRN IAVSAEAAQD YKKLLSDRTK LVETSLVNAI 370 380 390 400 410 420 GVSVAHTALN LNVKAIVAAT ESGSTAVTIS KYRPHSDIIA VTPSEHTARQ LALVWGAYPV 430 440 450 460 470 480 IKKGRKTTDD LLNNAVATAV ETGRVTNGDL IIITAGVPTG EKGTTNMMKL HLVGDEIAKG 490 500 510 520 530 540 QGVGRGSVVG KTVVANSASD LEGVDLSESV IVTNSVDETL VPYIEQAVGL ITEENGITSP 550 560 570 580 SAIIGLEKSI PTIIGVENAT KELKDGILVT VDAAQGKIFE GYANVL

References

[1]

"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCSC1435.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006716 Genomic DNA. Translation: BAE04536.1.
RefSeq	YP_253142.1. NC_007168.1.
3D structure databases
HSSP	HSSP built from PDB template 1LIU based on UniProtKB P30613.
ProteinModelPortal	Q4L739.
SMR	Q4L739. Positions 2-586.
ModBase	Search...
Protein-protein interaction databases
STRING	279808.SH1227.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAE04536; BAE04536; SH1227.
GeneID	3481929.
KEGG	sha:SH1227.
PATRIC	19618573. VBIStaHae67511_1210.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021559.
KO	K00873.
OMA	VFGIEQG.
ProtClustDB	CLSK885504.
Enzyme and pathway databases
BioCyc	SHAE279808:GJX7-1281-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	IPR008279. PEP-util_enz_mobile_dom. 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	PF00391. PEP-utilizers. 1 hit. PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF52009. PEP_mobile. 1 hit. 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_STAHJ

Accession

Primary (citable) accession number: Q4L739

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	August 2, 2005
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program