KPYK_ASPNG
ID KPYK_ASPNG Reviewed; 526 AA.
AC Q12669;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pkiA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9089 / N402;
RX PubMed=1611667; DOI=10.1007/bf00351737;
RA de Graaff L., van den Broeck H., Visser J.;
RT "Isolation and characterization of the Aspergillus niger pyruvate kinase
RT gene.";
RL Curr. Genet. 22:21-27(1992).
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; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; S38698; AAB22392.1; -; Genomic_DNA.
DR PIR; S26869; S26869.
DR AlphaFoldDB; Q12669; -.
DR SMR; Q12669; -.
DR STRING; 5061.CADANGAP00006051; -.
DR PRIDE; Q12669; -.
DR VEuPathDB; FungiDB:An07g08990; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1184374; -.
DR VEuPathDB; FungiDB:ATCC64974_49600; -.
DR VEuPathDB; FungiDB:M747DRAFT_268430; -.
DR eggNOG; KOG2323; Eukaryota.
DR UniPathway; UPA00109; UER00188.
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; IEA:UniProtKB-EC.
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 ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT CHAIN 1..526
FT /note="Pyruvate kinase"
FT /id="PRO_0000112108"
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"
SQ SEQUENCE 526 AA; 58134 MW; 8B7ED999C46D780C CRC64;
MAASSSLDHL SNRMKLEWHS KLNTEMVPSK NFRRTSIIGT IGPKTNSVEK INSLRTAGLN
VVRMNFSHGS YQYHQSVIDN AREAAKTQVG RPLAIALDTK GPEIRTGNTP DDKDIPIKQG
HELNITTDEQ YATASDDKNM YLDYKNITKV ISPGKLIYVD DGILSFEVLE VVDDKTIRVR
CLNNGNISSR KGVNLPGTDV DLPALSEKDI ADLKFGVRNK VDMVFASFIR RGSDIRHIRE
VLGEEGKEIQ IIAKIENQQG VNNFDEILEE TDGVMVARGD LGIEIPAPKV FIAQKMMIAK
CNIKGKPVIC ATQMLESMTY NPRPTRAEVS DVANAVLDGA DCVMLSGETA KGNYPNEAVK
MMSETCLLAE VAIPHFNVFD ELRNLAPRPT DTVESIAMAA VSASLELNAG AIVVLTTSGK
TARYLSKYRP VCPIVMVTRN PAASRYSHLY RGVWPFLFPE KKPDFNVKVW QEDVDRRLKW
GINHALKLGI INKGDNIVCV QGWRGGMGHT NTVRVVPAEE NLGLAE
