PGK_CHESB
ID PGK_CHESB Reviewed; 398 AA.
AC Q11CR7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Meso_3437;
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX NCBI_TaxID=266779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNC1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG64808.1; -; Genomic_DNA.
DR RefSeq; WP_011582749.1; NC_008254.1.
DR AlphaFoldDB; Q11CR7; -.
DR SMR; Q11CR7; -.
DR STRING; 266779.Meso_3437; -.
DR EnsemblBacteria; ABG64808; ABG64808; Meso_3437.
DR KEGG; mes:Meso_3437; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_5; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 462069at2; -.
DR UniPathway; UPA00109; UER00185.
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 Transferase.
FT CHAIN 1..398
FT /note="Phosphoglycerate kinase"
FT /id="PRO_1000203338"
FT BINDING 23..25
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 61..64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 203
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 355..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ SEQUENCE 398 AA; 42214 MW; 9FB75EBCEC33CD59 CRC64;
MAGFKTLDDL KDVAGKRVLL RVDLNVPVKD GEVTDTTRIE RVAPTITELS DKGAKVILLA
HFGRPKGKPD AEASLQPIAH AVEAVLDRRV HFASSCIGEP AKKAVDEMTG GDILLLENTR
FHAGEEKNDP EFTKALAANG DIYVNDAFSA AHRAHASTEG LAHLLPAYAG RTIQAELEAL
QRGLGDPKRP VVAIVGGAKV STKIDLLTNL VKKVDCLVIG GGMANTFLAA RGTSVGKSLC
EHDLRETAKQ IMIDAAEAGC AIILPVDAVV ARKFEAGAET ETVDIDAVPE DAMILDVGPK
SVEKVKEWLD RADTLVWNGP LGAFELSPFD KATMEVAKYA ARRTRESLLV SVAGGGDTVA
ALNQADVSDD FSYVSTAGGA FLEWMEGKDL PGVAALQK