PGK_PRIM3
ID PGK_PRIM3 Reviewed; 394 AA.
AC P24269; D5DNB0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=BMD_5037;
OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=592022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2123031; DOI=10.1093/nar/18.21.6423;
RA Schlaepfer B.S., Branlant C., Branlant G., Zuber H.;
RT "Nucleotide sequence of the phosphoglycerate kinase gene from Bacillus
RT megaterium.";
RL Nucleic Acids Res. 18:6423-6423(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1452037; DOI=10.1016/0378-1119(92)90031-j;
RA Schlaepfer B.S., Zuber H.;
RT "Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate
RT dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap
RT operon) from mesophilic Bacillus megaterium: comparison with corresponding
RT sequences from thermophilic Bacillus stearothermophilus.";
RL Gene 122:53-62(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 319 / IMG 1521;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; X54519; CAA38375.1; -; Genomic_DNA.
DR EMBL; M87647; AAA73203.1; -; Genomic_DNA.
DR EMBL; M87648; AAA73206.1; -; Genomic_DNA.
DR EMBL; CP001982; ADF41837.1; -; Genomic_DNA.
DR PIR; S13125; KIBSGM.
DR RefSeq; WP_013059701.1; NC_014103.1.
DR AlphaFoldDB; P24269; -.
DR SMR; P24269; -.
DR EnsemblBacteria; ADF41837; ADF41837; BMD_5037.
DR GeneID; 64144493; -.
DR KEGG; bmd:BMD_5037; -.
DR HOGENOM; CLU_025427_0_2_9; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000002365; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Phosphoprotein; Transferase.
FT CHAIN 1..394
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145903"
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 350..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 42457 MW; 7A2E6B978FA7008B CRC64;
MNKKTLKDID VKGKRVFCRV DFNVPMKDGK VTDETRIRAA IPTIQYLVEQ GAKVILASHL
GRPKGEVVEE LRLNAVAERL QALLGKDVAK ADEAFGEEVK KTIDGMSEGD VLVLENVRFY
PGEEKNDPEL AKAFAELADV YVNDAFGAAH RAHASTEGIA QHIPAVAGFL MEKELDVLSK
ALSNPERPFT AIVGGAKVKD KIGVIDHLLD KVDNLIIGGG LSYTFIKALG HEVGKSLLEE
DKIELAKSFM EKAKKNGVNF YMPVDVVVAD DFSNDANIQV VSIEDIPSDW EGLDAGPKTR
EIYADVIKNS KLVIWNGPMG VFELDAFANG TKAVAEALAE ATDTYSVIGG GDSAAAVEKF
NLADKMSHIS TGGGASLEFM EGKELPGVVA LNDK
