PGK_STAAR
ID PGK_STAAR Reviewed; 396 AA.
AC Q6GIL7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145};
DE EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145};
GN Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=SAR0829;
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=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00145};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-
CC Rule:MF_00145}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00145}.
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DR EMBL; BX571856; CAG39838.1; -; Genomic_DNA.
DR RefSeq; WP_001074749.1; NC_002952.2.
DR PDB; 4DG5; X-ray; 2.30 A; A=2-396.
DR PDBsum; 4DG5; -.
DR AlphaFoldDB; Q6GIL7; -.
DR SMR; Q6GIL7; -.
DR KEGG; sar:SAR0829; -.
DR HOGENOM; CLU_025427_0_2_9; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 462069at2; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..396
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000146004"
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 352..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:4DG5"
FT TURN 123..131
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4DG5"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:4DG5"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:4DG5"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:4DG5"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:4DG5"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:4DG5"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:4DG5"
SQ SEQUENCE 396 AA; 42602 MW; C8383CFDBC5BF4EC CRC64;
MAKKIVSDLD LKGKTVLVRA DFNVPLKDGE ITNDNRIVQA LPTIQYIIEQ GGKIVLFSHL
GKVKEESDKA KLTLRPVAED LSKKLDKEVV FVPETRGEKL EAAIKDLKEG DVLLVENTRY
EDLDGKKESK NDPELGKYWA SLGDVFVNDA FGTAHREHAS NVGISTHLET AAGFLMDKEI
KFIGGVVNDP HKPVVAILGG AKVSDKINVI KNLVNIADKI IIGGGMAYTF LKAQGKEIGI
SLLEEDKIDF AKDLLEKHGD KIVLPVDTKV AKEFSNDAKI TVVPSDSIPA DQEGMDIGPN
TVKLFADELE GAHTVVWNGP MGVFEFSNFA QGTIGVCKAI ANLKDAITII GGGDSAAAAI
SLGFENDFTH ISTGGGASLE YLEGKELPGI KAINNK
