P22360 (KPYK_EMENI) Reviewed, UniProtKB/Swiss-Prot

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 (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella › Emericella nidulans › mitosporic Emericella nidulans

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
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 Potassium Pyruvate
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme 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 – 526	526	Pyruvate kinase		PRO_0000112113
Sites
	Metal binding	65	1	Potassium By similarity
	Metal binding	67	1	Potassium By similarity
	Metal binding	98	1	Potassium By similarity
	Metal binding	99	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	256	1	Magnesium Potential
	Metal binding	280	1	Magnesium By similarity
	Binding site	63	1	Substrate By similarity
	Binding site	279	1	Substrate; via amide nitrogen By similarity
	Binding site	280	1	Substrate; via amide nitrogen By similarity
	Binding site	312	1	Substrate By similarity
	Binding site	351	1	ADP Potential
	Site	254	1	Transition state stabilizer By similarity
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 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M36918 Genomic DNA. Translation: AAA33320.1. AACD01000089 Genomic DNA. Translation: EAA62391.1. BN001305 Genomic DNA. Translation: CBF81089.1.
PIR	S27364.
RefSeq	XP_662814.1. XM_657722.1.
3D structure databases
ProteinModelPortal	P22360.
SMR	P22360. Positions 31-515.
ModBase	Search...
Protein-protein interaction databases
STRING	162425.CADANIAP00003208.
Proteomic databases
PRIDE	P22360.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00003208; CADANIAP00003208; CADANIAG00003208.
GeneID	2871501.
KEGG	ani:AN5210.2.
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021559.
KO	K00873.
OMA	NSGYTAR.
OrthoDB	EOG43XZC1.
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	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase-like_dom. 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_EMENI

Accession

Primary (citable) accession number: P22360
Secondary accession number(s): C8VF86, Q5B2M0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	May 1, 2007
Last modified:	May 29, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program