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   16-JUN-2009, entry version 53.
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; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9089 / N402;
RX   MEDLINE=92306163; 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
RT   kinase gene.";
RL   Curr. Genet. 22:21-27(1992).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Potassium (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR   EMBL; S38698; AAB22392.1; -; Genomic_DNA.
DR   PIR; S26869; S26869.
DR   HSSP; P14178; 1E0T.
DR   BRENDA; 2.7.1.40; 277.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat.
DR   InterPro; IPR015794; Pyrv_Knase_a/b.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Gene3D; G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
DR   PANTHER; PTHR11817; Pyruvate_kinase; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   ProDom; PD001009; Pyruvate_kinase; 2.
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; Pyruvate; Transferase.
FT   CHAIN         1    526       Pyruvate kinase.
FT                                /FTId=PRO_0000112108.
FT   ACT_SITE    254    254       By similarity.
FT   METAL       256    256       Magnesium (Potential).
FT   METAL       277    277       Magnesium (Potential).
FT   METAL       278    278       Magnesium (Potential).
FT   BINDING     351    351       ADP (Potential).
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
//