PGK_BUCAI
ID PGK_BUCAI Reviewed; 390 AA.
AC P57525;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=BU450;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; BA000003; BAB13148.1; -; Genomic_DNA.
DR RefSeq; NP_240262.1; NC_002528.1.
DR RefSeq; WP_010896123.1; NC_002528.1.
DR AlphaFoldDB; P57525; -.
DR SMR; P57525; -.
DR STRING; 107806.10039114; -.
DR EnsemblBacteria; BAB13148; BAB13148; BAB13148.
DR KEGG; buc:BU450; -.
DR PATRIC; fig|107806.10.peg.460; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_6; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000001806; 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 Gene3D; 3.40.50.1260; -; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..390
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145918"
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 114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 340..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 390 AA; 43653 MW; 8535BD49D2C72C7A CRC64;
MTIRKMTELN ITEKRILIRS DLNVPIENGI IQSDARILAA LPTIELALQK KAKVIIMSHL
GRPKEGYYTK KYSLFPIFEY FKKKFNNTKI YFSNNFLDGI KLNPGEIALL ENTRFNKGEL
NNDEQLSKKY SDLCDIFVMD AFGSAHRMQS STYGIGKFVK IACAGLLLIS EIDALKKALK
KPKRPMVAIV GGSKVSTKFN VLNKLSKIAD TIIVGGGIAN TFLAIDYKIG KSLYEPDFVF
EAKKLRDKYN IIVPIDSRVG KNFCKNEQAI IKSPDNIKED EEIMDFGDES IKKIISIITQ
SQTIMWNGPV GVFEFPNFRK GTEMIAKTIA NSNAFSIAGG GDTLSVIDMF NIKNNISYIS
TGGGAFLEFI EGKKLPAIQM LEENFKNKSK
