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 / NCTC
OS 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}.
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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
//
