Q8K9M3 (KPYK_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	pykA
Ordered Locus Names:	BUsg_311

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	481 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.
Enzyme regulation	Allosterically activated by AMP and by several sugar phosphates. Belongs to type II PK By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the pyruvate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Technical term	Allosteric enzyme 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 – 481	481	Pyruvate kinase		PRO_0000112059
Sites
	Metal binding	38	1	Potassium By similarity
	Metal binding	40	1	Potassium By similarity
	Metal binding	70	1	Potassium By similarity
	Metal binding	225	1	Magnesium By similarity
	Metal binding	252	1	Magnesium By similarity
	Binding site	36	1	Substrate By similarity
	Binding site	251	1	Substrate; via amide nitrogen By similarity
	Binding site	252	1	Substrate; via amide nitrogen By similarity
	Binding site	284	1	Substrate By similarity
	Site	223	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9M3 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 8A11ECA79EAB8A3B	FASTA	481	52,632
	10 20 30 40 50 60 MLNRVRRTKI VATLGPSTDK ANNLEKIILS GANVLRLNFS HGSSEEHKKR AKKAKEIMFK 70 80 90 100 110 120 LNCHIALLGD LQGPKIRISK FKKNSIFLKV NDVFILDANL NEKNGNNERV GIDYKKLPND 130 140 150 160 170 180 LNVNDILLLD DGRIQLKVIK IEKCAIFTKV IIGGILSNNK GINKLGGGLS ADALTEKDKK 190 200 210 220 230 240 DIILASEIDV DYLAVSFPRC ADDLIKAREL LKKSGSNAQI IAKIERAEAV FDQNAIENII 250 260 270 280 290 300 LSSDAIMIAR GDLGVEIGDA ELVGIQKKLI RTARKLNKVA ITATQMMESM ILNPLPTRAE 310 320 330 340 350 360 VMDVANAVLD GSDAVMLSAE TASGKYPSET VISMAKVCKG AEKVPSINVS RHRLNVEFQS 370 380 390 400 410 420 IEEAIAMSSM YAANHLKGIT AIITMTESGK TALMTSRITS GLPIFALSKH KKTLNLTALY 430 440 450 460 470 480 RGVIPIYFDS DKDGVEAANE AIILLCKKKF LFNNDLVIVT QGDIMGKIGK TNTSRILRVT Y

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67865.1.
RefSeq	NP_660654.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9M3.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg311.
Proteomic databases
PRIDE	Q8K9M3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67865; AAM67865; BUsg_311.
GeneID	1005515.
KEGG	bas:BUsg311.
PATRIC	21247429. VBIBucAph100086_0324.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0469.
KO	K00873.
OMA	VQVSKHR.
ProtClustDB	CLSK315882.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-367-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. IPR018209. Pyrv_Knase_AS. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK_BUCAP

Accession

Primary (citable) accession number: Q8K9M3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program