NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=WG096;
DOI=10.1007/BF00434080; PubMed=3072099 [NCBI, ExPASy, EBI, Israel, Japan]
de Graaff L., Visser J.;
"Structure of the Aspergillus nidulans pyruvate kinase gene.";
Curr. Genet. 14:553-560(1988).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC 4;
DOI=10.1038/nature04341; PubMed=16372000 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).

Comments

CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
COFACTOR: Magnesium.
COFACTOR: 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: Homotetramer.
SIMILARITY: Belongs to the pyruvate kinase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M36918; AAA33320.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACD01000089; EAA62391.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S27364; S27364.

RefSeq

XP_662814.1; -.

3D structure databases

HSSP

P14178; 1E0T. [HSSP ENTRY / PDB]

ModBase

P22360.

Ontologies

GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
GO:0030955;	Molecular function: potassium ion binding (inferred from electronic annotation from InterPro).
GO:0004743;	Molecular function: pyruvate kinase activity (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001697; Pyr_Knase.
IPR015813; Pyrv/PenolPyrv_Kinase_cat.
IPR015794; Pyrv_Knase_a/b.
IPR015793; Pyrv_Knase_brl.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.

PANTHER

PTHR11817; Pyruvate_kinase; 1.

Pfam

PF00224; PK; 1.
PF02887; PK_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR01050; PYRUVTKNASE.

ProDom

PD001009; Pyruvate_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01064; pyruv_kin; 1.

PROSITE

PS00110; PYRUVATE_KINASE; 1.

ProtoNet

P22360.

Genome annotation databases

GeneID

2871501; -.

KEGG

ani:AN5210.2; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allosteric enzyme; Glycolysis; Kinase; Magnesium; Metal-binding; Phosphoprotein; Pyruvate; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 526`	`526`	`Pyruvate kinase.`	`PRO_0000112113`
`ACT_SITE`	`254 254`		`By similarity.`
`METAL`	`256 256`		`Magnesium (Potential).`
`METAL`	`277 277`		`Magnesium (Potential).`
`METAL`	`278 278`		`Magnesium (Potential).`
`BINDING`	`351 351`		`ADP (Potential).`
`MOD_RES`	`36 36`		`Phosphoserine (Potential).`
`CONFLICT`	`88 88`		`Q -> A (in Ref. 1; AAA33320).`

Sequence information

Length: 526 AA [This is the length of the unprocessed precursor]

Molecular weight: 58133 Da [This is the MW of the unprocessed precursor]

CRC64: BCD3A6F35F5D28B2 [This is a checksum on the sequence]

        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

P22360 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools