PGK_GEOSE
ID PGK_GEOSE Reviewed; 394 AA.
AC P18912;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145, ECO:0000303|PubMed:1756980};
DE EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145, ECO:0000269|PubMed:1433299};
GN Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145, ECO:0000303|PubMed:1756980};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1756980; DOI=10.1016/0378-1119(91)90586-z;
RA Davies G.J., Littlechild J.A., Watson H.C., Hall L.;
RT "Sequence and expression of the gene encoding 3-phosphoglycerate kinase
RT from Bacillus stearothermophilus.";
RL Gene 109:39-45(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
RX PubMed=2656407; DOI=10.1016/0378-1119(89)90391-0;
RA Branlant C., Oster T., Branlant G.;
RT "Nucleotide sequence determination of the DNA region coding for Bacillus
RT stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and of the
RT flanking DNA regions required for its expression in Escherichia coli.";
RL Gene 75:145-155(1989).
RN [3]
RP CRYSTALLIZATION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=1433299; DOI=10.1016/0022-2836(92)90538-u;
RA Davies G.J., Gamblin S.J., Littlechild J.A., Watson H.C.;
RT "Purification, crystallization and preliminary X-ray analysis of the 3-
RT phosphoglycerate kinase from Bacillus stearothermophilus.";
RL J. Mol. Biol. 227:1263-1264(1992).
RN [4] {ECO:0007744|PDB:1PHP}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.
RX PubMed=15299460; DOI=10.1107/s0907444993011138;
RA Davies G.J., Gamblin S.J., Littlechild J.A., Dauter Z., Wilson K.S.,
RA Watson H.C.;
RT "Structure of the ADP complex of the 3-phosphoglycerate kinase from
RT Bacillus stearothermophilus at 1.65 A.";
RL Acta Crystallogr. D 50:202-209(1994).
RN [5]
RP STRUCTURE BY NMR OF 1-174 IN COMPLEX WITH ADP.
RX PubMed=9003185; DOI=10.1021/bi961784p;
RA Hosszu L.L.P., Craven C.J., Spencer J., Parker M.J., Clarke A.R., Kelly M.,
RA Waltho J.P.;
RT "Is the structure of the N-domain of phosphoglycerate kinase affected by
RT isolation from the intact molecule?";
RL Biochemistry 36:333-340(1997).
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 ECO:0000269|PubMed:1433299};
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 ECO:0000269|PubMed:9003185}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X58059; CAA41093.1; -; Genomic_DNA.
DR EMBL; M24493; AAA22462.1; ALT_INIT; Genomic_DNA.
DR PIR; JQ1399; JQ1399.
DR RefSeq; WP_033015089.1; NZ_RCTK01000017.1.
DR PDB; 1PHP; X-ray; 1.65 A; A=1-394.
DR PDBsum; 1PHP; -.
DR AlphaFoldDB; P18912; -.
DR BMRB; P18912; -.
DR SMR; P18912; -.
DR GeneID; 58573428; -.
DR BRENDA; 2.7.2.3; 623.
DR SABIO-RK; P18912; -.
DR UniPathway; UPA00109; UER00185.
DR EvolutionaryTrace; P18912; -.
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; Phosphoprotein; Transferase.
FT CHAIN 1..394
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145904"
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 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145,
FT ECO:0000269|PubMed:15299460"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15299460"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145,
FT ECO:0000269|PubMed:15299460"
FT BINDING 350..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145,
FT ECO:0000269|PubMed:15299460"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1PHP"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:1PHP"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 264..273
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1PHP"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:1PHP"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:1PHP"
SQ SEQUENCE 394 AA; 42730 MW; 46BFA286F60E365A CRC64;
MNKKTIRDVD VRGKRVFCRV DFNVPMEQGA ITDDTRIRAA LPTIRYLIEH GAKVILASHL
GRPKGKVVEE LRLDAVAKRL GELLERPVAK TNEAVGDEVK AAVDRLNEGD VLLLENVRFY
PGEEKNDPEL AKAFAELADL YVNDAFGAAH RAHASTEGIA HYLPAVAGFL MEKELEVLGK
ALSNPDRPFT AIIGGAKVKD KIGVIDNLLE KVDNLIIGGG LAYTFVKALG HDVGKSLLEE
DKIELAKSFM EKAKEKGVRF YMPVDVVVAD RFANDANTKV VPIDAIPADW SALDIGPKTR
ELYRDVIRES KLVVWNGPMG VFEMDAFAHG TKAIAEALAE ALDTYSVIGG GDSAAAVEKF
GLADKMDHIS TGGGASLEFM EGKQLPGVVA LEDK
