Q5HNK7 (KPYK_STAEQ) 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:	SERP1261

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]

Taxonomic identifier

176279 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	585 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 – 585	585	Pyruvate kinase		PRO_0000294138
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	221	1	Magnesium By similarity
	Metal binding	245	1	Magnesium By similarity
	Binding site	32	1	Substrate By similarity
	Binding site	244	1	Substrate; via amide nitrogen By similarity
	Binding site	245	1	Substrate; via amide nitrogen By similarity
	Binding site	277	1	Substrate By similarity
	Site	219	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HNK7 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 7756EDD80D49128C	FASTA	585	63,033
	10 20 30 40 50 60 MRKTKIVCTI GPASESEEML EKLMNAGMNV ARLNFSHGSH EEHKARIDTI RKVAKRLNKT 70 80 90 100 110 120 IGLLLDTKGP EIRTHNMKDG LIVLEKGKEV IVSMNEVEGT PEKFSVTYEN LINDVNIGSY 130 140 150 160 170 180 ILLDDGLVEL QVKEINKDKG EVKCDILNTG ELKNKKGVNL PGVKVNLPGI TDKDADDIRF 190 200 210 220 230 240 GIKENVDFIA ASFVRRPSDV LDIRQILEEE KAEITIFPKI ENQEGIDNIE EILEVSDGLM 250 260 270 280 290 300 VARGDMGVEI PPESVPMVQK DLIRKCNKLG KPVITATQML DSMQRNPRAT RAEASDVANA 310 320 330 340 350 360 IYDGTDAVML SGETAAGQYP EEAVKTMRNI AVSAEAAQDY KKLLSDRTKL VETSLVNAIG 370 380 390 400 410 420 VSVAHTALNL NVKAIVAATE SGSTARTISK YRPHSDIIAV TPSEKTARQC AIVWGVNPVV 430 440 450 460 470 480 KEGRKTTDAL LNNAVATAVE TGRVSNGDLI IITAGVPTGE KGTTNMMKIH LVGDEIAKGQ 490 500 510 520 530 540 GVGRGSVVGH AIVADSASDL EGKDLSDKVI ITNSVDETLV PYVEKAIGLI TEENGITSPS 550 560 570 580 AIIGLEKGIP TVVGVEQATK EIKNDMLVTL DASQGKVFEG YANVL

References

[1]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000029 Genomic DNA. Translation: AAW54633.1.
RefSeq	YP_188834.1. NC_002976.3.
3D structure databases
HSSP	HSSP built from PDB template 2G50 based on UniProtKB P11974.
ProteinModelPortal	Q5HNK7.
SMR	Q5HNK7. Positions 2-585.
ModBase	Search...
Protein-protein interaction databases
STRING	176279.SERP1261.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAW54633; AAW54633; SERP1261.
GeneID	3240853.
KEGG	ser:SERP1261.
PATRIC	19613373. VBIStaEpi130894_1229.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021559.
KO	K00873.
OMA	NSGYTAR.
ProtClustDB	CLSK885504.
Enzyme and pathway databases
BioCyc	SEPI176279:GJJB-1288-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_STAEQ

Accession

Primary (citable) accession number: Q5HNK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program