ID KPYC_SOYBN Reviewed; 511 AA. AC Q42806; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=Pyruvate kinase, cytosolic isozyme; DE Short=PK; DE EC=2.7.1.40; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94105349; PubMed=8278551; DOI=10.1104/pp.102.4.1345; RA Ma H., McMullen M.D., Finer J.J.; RT "A pyruvate kinase cDNA from soybean somatic embryos."; RL Plant Physiol. 102:1345-1345(1993). 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 -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L08632; AAA17000.1; -; mRNA. DR PIR; T07787; T07787. DR UniGene; Gma.4073; -. DR HSSP; P14178; 1E0T. DR BRENDA; 2.7.1.40; 299. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Pyruvate; Transferase. FT CHAIN 1 511 Pyruvate kinase, cytosolic isozyme. FT /FTId=PRO_0000112125. FT ACT_SITE 241 241 By similarity. FT METAL 243 243 Magnesium (Potential). FT METAL 264 264 Magnesium (Potential). FT METAL 265 265 Magnesium (Potential). SQ SEQUENCE 511 AA; 55302 MW; BF0C06DAC6FD95F1 CRC64; MANIDIEGIL KQQQPYDGRV PKTKIVCTLG PASRSVEMTE KLLRAGMNVA RFNFSHGTHD YHQETLNNLK TAMHNTGILC AVMLDTKGPE IRTGFLKDGK PIQLKEGQEV TITTDYDIKG DPEMISMSYK KLPVHLKPGN TILCSDGTIT LTVLSCDPDA GTVRCRCENT ATLGERKNVN LPGVVVDLPT LTEKDKEDIL GWGVPNKIDM IALSFVRKGS DLVNVRKVLG PHAKNIQLMS KVENQEGVLN FDEILRETDA FMVARGDLGM EIPVEKIFLA QKMMIYKCNL VGKPVVTATQ MLESMIKSPR PTRAEATDVA NAVLDGTDCV MLSGESAAGA YPELAVKIMA RICIEAESSL DYGAIFKEMI RSTPLPMSPL ESLASSAVRT ANKAKAKLIV VLTRGGSTAK LVAKYRPAVP ILSVVVPVLS TDSFDWTCSD ETPARHSLIY RGLIPILGEG SAKATDAEST EVILEAALKS ATERALCKPG DAVVALHRIG AASVIKICIV K //