KPYK_SPOPS
ID KPYK_SPOPS Reviewed; 586 AA.
AC P51182;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk;
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7549104; DOI=10.1271/bbb.59.1536;
RA Tanaka K., Sakai H., Ohta T., Matsuzawa H.;
RT "Molecular cloning of the genes for pyruvate kinase of two bacilli,
RT Bacillus psychrophilus and Bacillus licheniformis, and comparison of the
RT properties of the enzymes produced in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 59:1536-1542(1995).
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 -!- 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}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; D31954; BAA06725.1; -; Genomic_DNA.
DR PIR; JC4219; JC4219.
DR RefSeq; WP_067207646.1; NZ_CP014616.1.
DR AlphaFoldDB; P51182; -.
DR SMR; P51182; -.
DR STRING; 1476.AZE41_07700; -.
DR OrthoDB; 1098983at2; -.
DR BRENDA; 2.7.1.40; 685.
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 Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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; PF00391; PEP-utilizers; 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; SSF52009; SSF52009; 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..586
FT /note="Pyruvate kinase"
FT /id="PRO_0000112054"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 34..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 34
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 66
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 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 220
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 586 AA; 62571 MW; 8C0B7017C9C6D5CE CRC64;
MRKTKIVCTI GPASESPELL EQLIEAGMNV ARLNFSHGNH AEHKARIDSI RKVAREKGKV
VGILLDTKGP EIRTHSMMNG KLELVTGQKI DISMTQVEGN NDVFSVSYDK LIEDVNEGSV
ILLDDGLIQL EVTGKDVARG LIHTLIINSG SLSNNKGVNI PGVSVQLPGM TEKDAEDILF
GIREGVDFIA ASFVRRASDV MEIRALLENN NGSNLQIIPK IENQEGVDNI DEILNVSDGL
MVARGDLGVE IPPEEVPLVQ KNLIEKCNQA GKPVITATQM LDSMQRNPRP TRAEASDVAN
AIFDGTDAIM LSGETAAGIY PVESVQTMDR IALTTEAAID YRSVVSTRRR EKHGNMTEAI
GQAAAYTAIN LKVKAVLAPT ESGHTAKMIA KYRPGCPVIA VTSSEMCSRK LSLIWGVYPI
VGKKASSIDE ILQESVEESV KHQYVGHGDV VIITAGVPVG EAGTTNLMKI HVIGDLLARG
QGIGKDVAYG RTVVAKNAAE ALAYDTEGAI LVTNASDRDM MPAIEKCAGL ITEEGGLTSH
GAIVGLSLGI PIIVGVENAT ELIQHGKEIT MDAESGVIYN GHASVL
