ID   KPYK_EMENI              Reviewed;         526 AA.
AC   P22360; C8VF86; Q5B2M0;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pkiA; Synonyms=pki; ORFNames=AN5210;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WG096;
RX   PubMed=3072099; DOI=10.1007/bf00434080;
RA   de Graaff L., Visser J.;
RT   "Structure of the Aspergillus nidulans pyruvate kinase gene.";
RL   Curr. Genet. 14:553-560(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=2.7.1.40;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC   -!- ACTIVITY REGULATION: Regulated by phosphoenolpyruvate substrate and
CC       allosteric effectors such as fructose 1,6 diphosphate and magnesium.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; M36918; AAA33320.1; -; Genomic_DNA.
DR   EMBL; AACD01000089; EAA62391.1; -; Genomic_DNA.
DR   EMBL; BN001305; CBF81089.1; -; Genomic_DNA.
DR   PIR; S27364; S27364.
DR   RefSeq; XP_662814.1; XM_657722.1.
DR   AlphaFoldDB; P22360; -.
DR   SMR; P22360; -.
DR   STRING; 162425.CADANIAP00003208; -.
DR   PRIDE; P22360; -.
DR   EnsemblFungi; CBF81089; CBF81089; ANIA_05210.
DR   EnsemblFungi; EAA62391; EAA62391; AN5210.2.
DR   GeneID; 2871501; -.
DR   KEGG; ani:AN5210.2; -.
DR   eggNOG; KOG2323; Eukaryota.
DR   HOGENOM; CLU_015439_0_1_1; -.
DR   InParanoid; P22360; -.
DR   OMA; QVPIVQK; -.
DR   OrthoDB; 933620at2759; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000000560; Chromosome V.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd00288; Pyruvate_Kinase; 1.
DR   Gene3D; 2.40.33.10; -; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   Gene3D; 3.40.1380.20; -; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR036918; Pyrv_Knase_C_sf.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   PANTHER; PTHR11817; PTHR11817; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF50800; SSF50800; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52935; SSF52935; 1.
DR   TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..526
FT                   /note="Pyruvate kinase"
FT                   /id="PRO_0000112113"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         65..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         65
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            254
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        88
FT                   /note="Q -> A (in Ref. 1; AAA33320)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   526 AA;  58133 MW;  BCD3A6F35F5D28B2 CRC64;
     MAASSSLDHL SNRMKLEWHS KLNTEMVPAK NFRRTSIICT IGPKTNSVEK INALRRAGLN
     VVRMNFSHGS YEYHQSVIDH AREAEKQQAG RPVAIALDTK GPEIRTGNTV GDKDIPIKAG
     HEMNISTDEQ YATASDDQNM YVDYKNITKV ISAGKLIYVD DGILSFEVLE VVDDKTLRVR
     CLNNGNISSR KGVNLPGTDV DLPALSEKDI SDLKFGVKNK VDMVFASFIR RGSDIRHIRE
     VLGEEGREIQ IIAKIENQQG VNNFDEILEE TDGVMVARGD LGIEIPAPKV FIAQKMMIAK
     CNIKGKPVIC ATQMLESMTY NPRPTRAEVS DVANAVLDGA DCVMLSGETA KGNYPCEAVT
     MMSETCLLAE VAIPHFNVFD ELRNLAPRPT DTVESIAMAA VSASLELNAG AIVVLTTSGN
     TARMISKYRP VCPIIMVSRN PAATRYSHLY RGVWPFYFPE KKPDFNVKIW QEDVDRRLKW
     GINHGLKLGI INKGDNIVCV QGWRGGMGHT NTVRVVPAEE NLGLSE