Reviewed, UniProtKB/Swiss-Prot P22360 (KPYK_EMENI)

Names and origin

Protein names

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

Gene names

Name:	pkiA
Synonyms:	pki
ORF Names:	AN5210

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
Enzyme regulation	Regulated by phosphoenolpyruvate substrate and allosteric effectors such as fructose 1,6 diphosphate and magnesium.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the pyruvate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme
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 – 526	526	Pyruvate kinase		PRO_0000112113
Sites
	Active site	254	1	By similarity
	Metal binding	256	1	Magnesium Potential
	Metal binding	277	1	Magnesium Potential
	Metal binding	278	1	Magnesium Potential
	Binding site	351	1	ADP Potential
Amino acid modifications
	Modified residue	36	1	Phosphoserine Potential
Experimental info
	Sequence conflict	88	1	Q → A in AAA33320. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22360-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: BCD3A6F35F5D28B2	FASTA	526	58,133
	10 20 30 40 50 60 MAASSSLDHL SNRMKLEWHS KLNTEMVPAK NFRRTSIICT IGPKTNSVEK INALRRAGLN 70 80 90 100 110 120 VVRMNFSHGS YEYHQSVIDH AREAEKQQAG RPVAIALDTK GPEIRTGNTV GDKDIPIKAG 130 140 150 160 170 180 HEMNISTDEQ YATASDDQNM YVDYKNITKV ISAGKLIYVD DGILSFEVLE VVDDKTLRVR 190 200 210 220 230 240 CLNNGNISSR KGVNLPGTDV DLPALSEKDI SDLKFGVKNK VDMVFASFIR RGSDIRHIRE 250 260 270 280 290 300 VLGEEGREIQ IIAKIENQQG VNNFDEILEE TDGVMVARGD LGIEIPAPKV FIAQKMMIAK 310 320 330 340 350 360 CNIKGKPVIC ATQMLESMTY NPRPTRAEVS DVANAVLDGA DCVMLSGETA KGNYPCEAVT 370 380 390 400 410 420 MMSETCLLAE VAIPHFNVFD ELRNLAPRPT DTVESIAMAA VSASLELNAG AIVVLTTSGN 430 440 450 460 470 480 TARMISKYRP VCPIIMVSRN PAATRYSHLY RGVWPFYFPE KKPDFNVKIW QEDVDRRLKW 490 500 510 520 GINHGLKLGI INKGDNIVCV QGWRGGMGHT NTVRVVPAEE NLGLSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the Aspergillus nidulans pyruvate kinase gene." de Graaff L., Visser J. Curr. Genet. 14:553-560(1988) [PubMed: 3072099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WG096.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M36918 Genomic DNA. Translation: AAA33320.1. AACD01000089 Genomic DNA. Translation: EAA62391.1.
PIR	S27364.
RefSeq	XP_662814.1.
3D structure databases
HSSP	HSSP built from PDB template 1E0T based on UniProtKB P14178.
ModBase	Search...
Genome annotation databases
GeneID	2871501.
KEGG	ani:AN5210.2.
Enzyme and pathway databases
BRENDA	2.7.1.40. 3859.
Family and domain databases
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit. G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit.
PANTHER	PTHR11817. Pyruvate_kinase. 1 hit.
Pfam	PF00224. PK. 1 hit. PF02887. PK_C. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK_EMENI

Accession

Primary (citable) accession number: P22360
Secondary accession number(s): Q5B2M0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	May 1, 2007
Last modified:	June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)