ID PGK_CAMJE Reviewed; 400 AA. AC Q9PMQ5; Q0P8L2; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 119. 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=Cj1402c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(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 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; AL111168; CAL35511.1; -; Genomic_DNA. DR PIR; B81285; B81285. DR RefSeq; WP_010891932.1; NZ_SZUC01000003.1. DR RefSeq; YP_002344785.1; NC_002163.1. DR PDB; 3Q3V; X-ray; 2.14 A; A/B=1-400. DR PDBsum; 3Q3V; -. DR AlphaFoldDB; Q9PMQ5; -. DR SMR; Q9PMQ5; -. DR IntAct; Q9PMQ5; 70. DR STRING; 192222.Cj1402c; -. DR PaxDb; 192222-Cj1402c; -. DR EnsemblBacteria; CAL35511; CAL35511; Cj1402c. DR GeneID; 905691; -. DR KEGG; cje:Cj1402c; -. DR PATRIC; fig|192222.6.peg.1383; -. DR eggNOG; COG0126; Bacteria. DR HOGENOM; CLU_025427_0_2_7; -. DR OrthoDB; 9808460at2; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000000799; 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 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Glycolysis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..400 FT /note="Phosphoglycerate kinase" FT /id="PRO_0000145921" 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 119 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 152 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 205 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 296 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 327 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 HELIX 7..9 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 16..20 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 37..51 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 55..59 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 75..85 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 98..106 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 129..137 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 140..144 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:3Q3V" FT TURN 155..158 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 159..163 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 173..185 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 191..197 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 202..212 FT /evidence="ECO:0007829|PDB:3Q3V" FT TURN 213..215 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 226..232 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 247..259 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 268..277 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 295..299 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 301..311 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 315..321 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 329..331 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 333..344 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 345..353 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 354..362 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:3Q3V" FT STRAND 369..372 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 376..383 FT /evidence="ECO:0007829|PDB:3Q3V" FT HELIX 389..392 FT /evidence="ECO:0007829|PDB:3Q3V" SQ SEQUENCE 400 AA; 43591 MW; 1DAB672AC4432BDF CRC64; MSDIISIKDI DLAKKKVFIR CDFNVPQDDF LNITDDRRIR SAIPTIRYCL DNGCSVILAS HLGRPKEISS KYSLEPVAKR LARLLDKEIV MAKDVIGEDA KTKAMNLKAG EILLLENLRF EKGETKNDEN LAKELASMVQ VYINDAFGVC HRAHSSVEAI TKFFDEKHKG AGFLLQKEID FASNLIKHPA RPFVAVVGGS KVSGKLQALT NLLPKVDKLI IGGGMAFTFL KALGYDIGNS LLEEELLEEA NKILTKGKNL GVKIYLPVDV VAAPACSQDV PMKFVPAQEI PNGWMGLDIG PASVRLFKEV ISDAQTIWWN GPMGVFEIDK FSKGSIKMSH YISEGHATSV VGGGDTADVV ARAGDADEMT FISTGGGASL ELIEGKELPG VKALRSKENE //