ID PGK_BRUAB Reviewed; 396 AA.
AC Q9L560; Q57BF1;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-MAY-2023, entry version 111.
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=BruAb1_1714;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rosinha G.M.S., Miyoshi A., Azevedo V., Campos E., Neto E.D.,
RA Oliveira S.C.;
RT "Molecular cloning and DNA sequence analysis of the phosphoglycerate kinase
RT (pgk) from Brucella abortus.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX75033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF256214; AAF71544.1; -; Genomic_DNA.
DR EMBL; AE017223; AAX75033.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002964816.1; NC_006932.1.
DR AlphaFoldDB; Q9L560; -.
DR SMR; Q9L560; -.
DR EnsemblBacteria; AAX75033; AAX75033; BruAb1_1714.
DR GeneID; 45125029; -.
DR KEGG; bmb:BruAb1_1714; -.
DR HOGENOM; CLU_025427_0_2_5; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000540; Chromosome I.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..396
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145915"
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 BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 353..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT CONFLICT 101
FT /note="A -> P (in Ref. 1; AAF71544)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="H -> N (in Ref. 1; AAF71544)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="R -> S (in Ref. 1; AAF71544)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 41796 MW; 1A5F9D738ACDCF89 CRC64;
MMFRTLDDAN VQSKRVLVRV DLNVPMANGE VTDLTRIERI VPTIAELSRK GAKVILLAHF
GRPKGVASDE NSLKHVVKPL SKVLDHSVHF AEDCIGDKAK AAVDALKDGD VLLLENTRFH
KGEEKNDPEF VQALAANGDL YVNDAFSAAH RAHASTEGLA HVLPAFAGRA MQAELEALEK
GLGNPARPVV AIVGGAKVST KLDLLSNLIE KVDALVIGGG MANTFLAAKG LDVGKSLCEH
ELASTAREIM AKAETTKCAI ILPVDAVVGW HFAADTPHQT YGVDSVPGDA MILDAGELST
DLIASAIDDA ATLVWNGPLG AFELRPFDTA TVKVARHVAK RTKEGKLVSV GGGGDTVAAL
NHAGVADDFT YISTAGGAFL EWMEGKPLPG VDVLKK
//
