P73534 (KPYK2_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate kinase 2
Short name=PK 2
EC=2.7.1.40

Gene names

Name:	pyk2
Ordered Locus Names:	sll1275

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › Synechocystis sp. PCC 6803

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
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. 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 Reference 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 – 591	591	Pyruvate kinase 2		PRO_0000112086
Sites
	Metal binding	40	1	Potassium By similarity
	Metal binding	42	1	Potassium By similarity
	Metal binding	72	1	Potassium By similarity
	Metal binding	229	1	Magnesium By similarity
	Metal binding	253	1	Magnesium By similarity
	Binding site	38	1	Substrate By similarity
	Binding site	252	1	Substrate; via amide nitrogen By similarity
	Binding site	253	1	Substrate; via amide nitrogen By similarity
	Binding site	285	1	Substrate By similarity
	Site	227	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P73534 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 2520AA81145C11EB	FASTA	591	62,986
	10 20 30 40 50 60 MQTSPLPRRT KIVATIGPAT QSKEVLRQLI QAGATTFRLN FSHGDHAYHQ QSIRLIRQIA 70 80 90 100 110 120 FELNQPVGIL QDLQGPKIRV GKFLNDAGSV QLKNGDPYTL TSRPVECTET ISSISYEYLA 130 140 150 160 170 180 DEVPSGARIL LDDGKLEMLV EEVDTVARDL HCRVIVGGTL SSNKGVNFPG VCLSVKAMTD 190 200 210 220 230 240 KDKEDLMFGL DQGVDWVALS FVRNPQDIDE IKGLIAAAGK SVPVIAKIEK HEAIKDMQAV 250 260 270 280 290 300 LEKCDGVMVA RGDLGVELPA EDVPILQKKL IATANRLGIP VITATQMLDS MVNSPRPTRA 310 320 330 340 350 360 EVSDVANAIL DGTDAVMLSN ETAIGKFPVE AVAIMAKIAE RIEQEDINPS QAEASRTSIP 370 380 390 400 410 420 NAISSAVSQI AETLNAAAIM SLTKTGSTAR HVSKFRPKTP ILAVTPHVDV SRQLQLVWGV 430 440 450 460 470 480 KPLLVLDLPS TSQTFQAAIN VAQENHFLRD GDLVVMTAGT LQGVAGSTDL IKVEVVKAIL 490 500 510 520 530 540 GRGVGIGQGA VSGRARVASR PQAIAQFTQG EILVVPSTNA DCVDMMRRAA GIITEEESLT 550 560 570 580 590 SHAAIIGLRL GVPVIVGFKG ATQKIRDGAI VTIDAQKGLI YSGALPPVSK G

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA17574.1.
PIR	S77240.
RefSeq	NP_440894.1. NC_000911.1. YP_005650953.1. NC_017277.1. YP_007450777.1. NC_020286.1.
3D structure databases
ProteinModelPortal	P73534.
ModBase	Search...
Protein-protein interaction databases
IntAct	P73534. 2 interactions.
STRING	1148.sll1275.
Proteomic databases
PaxDb	P73534.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA17574; BAA17574; BAA17574.
GeneID	12255039. 14616431. 954197.
KEGG	syn:sll1275. syy:SYNGTS_1000.
PATRIC	23839046. VBISynSp132158_1087.
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021558.
KO	K00873.
OMA	RRLTVAW.
ProtClustDB	PRK06354.
Enzyme and pathway databases
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. 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	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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK2_SYNY3

Accession

Primary (citable) accession number: P73534

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program