PGK_COXBU
ID PGK_COXBU Reviewed; 391 AA.
AC Q83AU6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=CBU_1782;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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=AAO91276.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016828; AAO91276.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_820762.2; NC_002971.3.
DR PDB; 4NG4; X-ray; 2.78 A; A/B/C=1-388.
DR PDBsum; 4NG4; -.
DR AlphaFoldDB; Q83AU6; -.
DR SMR; Q83AU6; -.
DR STRING; 227377.CBU_1782; -.
DR DNASU; 1209693; -.
DR EnsemblBacteria; AAO91276; AAO91276; CBU_1782.
DR GeneID; 1209693; -.
DR KEGG; cbu:CBU_1782; -.
DR PATRIC; fig|227377.7.peg.1769; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_6; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..391
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145938"
FT BINDING 16..18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 54..57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 340..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT HELIX 1..3
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4NG4"
FT TURN 111..116
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4NG4"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4NG4"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:4NG4"
FT HELIX 376..385
FT /evidence="ECO:0007829|PDB:4NG4"
SQ SEQUENCE 391 AA; 42363 MW; A569E166D68D5ADE CRC64;
MSNLNLHNKR VMIREDLNVP MKNGKITNDE RIVRALPTIQ KAIEQKARVM ILSHLGRPEE
GKFEKEFSLA PVARLLSKKL NQKVPLINDW LKGVAVEPGQ AILCENVRFN KGENENNTEL
AKRMAELCDI FVMDAFATAH RAQASTAGVA AYAKLACAGP LLISEVEALS RALENPQKPL
VAVVGGSKVS TKIHLLENLL DKVDQLIVGG GIANTFLKAQ GYSIGKSLCE NEWLDAAQQF
WEKAAEKNVS LPLPVDVIVA DELSEDAKAT VKNIDAVTSN ESIFDVGPNT SATYAKLMAQ
AGTIVWNGPI GVFEIEAFSQ GTRALAQAVA KSTAYSIVGG GDTLAALDKF NLTDQMSYVS
TAGGAFLEFL EGKILPAIKI LTQRAKEYEQ K
