KPYK_MYCTU
ID KPYK_MYCTU Reviewed; 472 AA.
AC P9WKE5; L0T783; O06134;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk; Synonyms=pykA; OrderedLocusNames=Rv1617; ORFNames=MTCY01B2.09;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-37, DEPHOSPHORYLATION, AND
RP MUTAGENESIS OF SER-37.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20520732; DOI=10.1371/journal.pone.0010772;
RA Arora G., Sajid A., Gupta M., Bhaduri A., Kumar P., Basu-Modak S.,
RA Singh Y.;
RT "Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical
RT characterization and identification of novel substrate pyruvate kinase A.";
RL PLoS ONE 5:E10772-E10772(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; Evidence={ECO:0000269|PubMed:20520732};
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 -!- PTM: Phosphorylated by PknJ. Dephosphorylated by PstP.
CC {ECO:0000269|PubMed:20520732}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44381.1; -; Genomic_DNA.
DR PIR; G70557; G70557.
DR RefSeq; NP_216133.1; NC_000962.3.
DR RefSeq; WP_003898945.1; NZ_NVQJ01000016.1.
DR PDB; 5WRP; X-ray; 2.85 A; A/B/C/D=1-472.
DR PDB; 5WS8; X-ray; 2.62 A; A/B/C/D=1-472.
DR PDB; 5WS9; X-ray; 1.90 A; A/B/C/D=1-472.
DR PDB; 5WSA; X-ray; 2.85 A; A/B/C/D=1-472.
DR PDB; 5WSB; X-ray; 2.25 A; A/B/C/D=1-472.
DR PDB; 5WSC; X-ray; 2.40 A; A/B/C/D=1-472.
DR PDB; 6ITO; X-ray; 2.55 A; A/B/C/D=1-472.
DR PDBsum; 5WRP; -.
DR PDBsum; 5WS8; -.
DR PDBsum; 5WS9; -.
DR PDBsum; 5WSA; -.
DR PDBsum; 5WSB; -.
DR PDBsum; 5WSC; -.
DR PDBsum; 6ITO; -.
DR AlphaFoldDB; P9WKE5; -.
DR SMR; P9WKE5; -.
DR STRING; 83332.Rv1617; -.
DR iPTMnet; P9WKE5; -.
DR PaxDb; P9WKE5; -.
DR GeneID; 45425585; -.
DR GeneID; 885501; -.
DR KEGG; mtu:Rv1617; -.
DR TubercuList; Rv1617; -.
DR eggNOG; COG0469; Bacteria.
DR OMA; QVPIVQK; -.
DR PhylomeDB; P9WKE5; -.
DR BRENDA; 2.7.1.40; 3445.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate;
KW Reference proteome; Transferase.
FT CHAIN 1..472
FT /note="Pyruvate kinase"
FT /id="PRO_0000112082"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 35..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 35
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 37
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 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
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 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 218
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="Phosphoserine; by PknJ; in vitro"
FT /evidence="ECO:0000269|PubMed:20520732"
FT MUTAGEN 37
FT /note="S->A: Partial loss of phosphorylation. Decrease in
FT activity."
FT /evidence="ECO:0000269|PubMed:20520732"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5WS9"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 319..336
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 378..384
FT /evidence="ECO:0007829|PDB:5WS9"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:5WS8"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:5WS9"
FT HELIX 422..434
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 444..452
FT /evidence="ECO:0007829|PDB:5WS9"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:5WS9"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:5WRP"
SQ SEQUENCE 472 AA; 50699 MW; 2228960E0A45806B CRC64;
MTRRGKIVCT LGPATQRDDL VRALVEAGMD VARMNFSHGD YDDHKVAYER VRVASDATGR
AVGVLADLQG PKIRLGRFAS GATHWAEGET VRITVGACEG SHDRVSTTYK RLAQDAVAGD
RVLVDDGKVA LVVDAVEGDD VVCTVVEGGP VSDNKGISLP GMNVTAPALS EKDIEDLTFA
LNLGVDMVAL SFVRSPADVE LVHEVMDRIG RRVPVIAKLE KPEAIDNLEA IVLAFDAVMV
ARGDLGVELP LEEVPLVQKR AIQMARENAK PVIVATQMLD SMIENSRPTR AEASDVANAV
LDGADALMLS GETSVGKYPL AAVRTMSRII CAVEENSTAA PPLTHIPRTK RGVISYAARD
IGERLDAKAL VAFTQSGDTV RRLARLHTPL PLLAFTAWPE VRSQLAMTWG TETFIVPKMQ
STDGMIRQVD KSLLELARYK RGDLVVIVAG APPGTVGSTN LIHVHRIGED DV
