ID PGK_CAMC1 Reviewed; 399 AA.
AC A7ZEZ5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=Ccon26_15050;
GN ORFNames=CCC13826_0515;
OS Campylobacter concisus (strain 13826).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000792; EAT99369.1; -; Genomic_DNA.
DR RefSeq; WP_012140239.1; NC_009802.2.
DR AlphaFoldDB; A7ZEZ5; -.
DR SMR; A7ZEZ5; -.
DR STRING; 360104.CCC13826_0515; -.
DR KEGG; cco:CCC13826_0515; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_7; -.
DR OrthoDB; 9808460at2; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000001121; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
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..399
FT /note="Phosphoglycerate kinase"
FT /id="PRO_1000203321"
FT BINDING 22..24
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 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 354..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ SEQUENCE 399 AA; 43785 MW; 615B568AC8AE7270 CRC64;
MSDILSINDL ELNGAKVFIR CDFNVPMDEF LNITDDRRIR SAIPTIRYCL DNGCSVVLAS
HLGRPKNGYE EKFSLQGVAK RLSRLLDREV IFAEDVIGND AKTKAEALKA GEILMIENLR
FEKGETKNDE ALAKELSEFG EFYINDAFGV CHRAHSSVEA ITKFYDEKHK AAGFLLQKEI
NFAQNLIKHP SRPFVAVVGG SKVSGKLQAL HNLLPRVDKL IIGGGMAFTF LKSLGENIGN
SLLEEELIED ARQILQKGKE LGVKIYLPVD VVAAQTFSAE SAVKYVPAQE IPNGWMGLDI
GPASIRLFKE VIADAQTIWW NGPMGVFEMD KFSKGSIKMS HAIIDTHATT VVGGGDTADV
VERAGDADEM TFISTGGGAS LELIEGKELP GIKPLRKEE
//
