KPYK_STAAR
ID KPYK_STAAR Reviewed; 585 AA.
AC Q6GG09;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk; OrderedLocusNames=SAR1776;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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 -!- 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; BX571856; CAG40767.1; -; Genomic_DNA.
DR RefSeq; WP_001232655.1; NC_002952.2.
DR PDB; 3T05; X-ray; 3.05 A; A/B/C/D=1-585.
DR PDB; 3T07; X-ray; 3.30 A; A/B/C/D=1-585.
DR PDB; 3T0T; X-ray; 3.10 A; A/B/C/D=1-585.
DR PDBsum; 3T05; -.
DR PDBsum; 3T07; -.
DR PDBsum; 3T0T; -.
DR AlphaFoldDB; Q6GG09; -.
DR SMR; Q6GG09; -.
DR BindingDB; Q6GG09; -.
DR ChEMBL; CHEMBL2189162; -.
DR KEGG; sar:SAR1776; -.
DR HOGENOM; CLU_015439_0_2_9; -.
DR OMA; QVPIVQK; -.
DR OrthoDB; 1098983at2; -.
DR BRENDA; 2.7.1.40; 3352.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:Q6GG09; -.
DR Proteomes; UP000000596; Chromosome.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT CHAIN 1..585
FT /note="Pyruvate kinase"
FT /id="PRO_0000294130"
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 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
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 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 219
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 40..56
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3T0T"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3T05"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:3T05"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 255..269
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3T07"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 321..336
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 355..370
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 404..411
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 413..420
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 427..440
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:3T05"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 506..513
FT /evidence="ECO:0007829|PDB:3T05"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 526..533
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 539..546
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:3T05"
FT HELIX 558..561
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:3T05"
FT TURN 572..575
FT /evidence="ECO:0007829|PDB:3T05"
FT STRAND 576..580
FT /evidence="ECO:0007829|PDB:3T05"
SQ SEQUENCE 585 AA; 63142 MW; 87D790B356585362 CRC64;
MRKTKIVCTI GPASESEEMI EKLINAGMNV ARLNFSHGSH EEHKGRIDTI RKVAKRLDKI
VAILLDTKGP EIRTHNMKDG IIELERGNEV IVSMNEVEGT PEKFSVTYEN LINDVQVGSY
ILLDDGLIEL QVKDIDHAKK EVKCDILNSG ELKNKKGVNL PGVRVSLPGI TEKDAEDIRF
GIKENVDFIA ASFVRRPSDV LEIREILEEQ KANISVFPKI ENQEGIDNIE EILEVSDGLM
VARGDMGVEI PPEKVPMVQK DLIRQCNKLG KPVITATQML DSMQRNPRAT RAEASDVANA
IYDGTDAVML SGETAAGLYP EEAVKTMRNI AVSAEAAQDY KKLLSDRTKL VETSLVNAIG
ISVAHTALNL NVKAIVAATE SGSTARTISK YRPHSDIIAV TPSEETARQC SIVWGVQPVV
KKGRKSTDAL LNNAVATAVE TGRVTNGDLI IITAGVPTGE TGTTNMMKIH LVGDEIANGQ
GIGRGSVVGT TLVAETVKDL EGKDLSDKVI VTNSIDETFV PYVEKALGLI TEENGITSPS
AIVGLEKGIP TVVGVEKAVK NISNNVLVTI DAAQGKIFEG YANVL
