PGK_FRATT
ID PGK_FRATT Reviewed; 392 AA.
AC Q5NF76;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=FTT_1367c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG46000.1; -; Genomic_DNA.
DR RefSeq; WP_003022166.1; NZ_CP010290.1.
DR RefSeq; YP_170316.1; NC_006570.2.
DR PDB; 4EHJ; X-ray; 2.71 A; A/B=1-392.
DR PDB; 4FEY; X-ray; 2.30 A; A=1-392.
DR PDBsum; 4EHJ; -.
DR PDBsum; 4FEY; -.
DR AlphaFoldDB; Q5NF76; -.
DR SMR; Q5NF76; -.
DR STRING; 177416.FTT_1367c; -.
DR DNASU; 3191360; -.
DR EnsemblBacteria; CAG46000; CAG46000; FTT_1367c.
DR KEGG; ftu:FTT_1367c; -.
DR eggNOG; COG0126; Bacteria.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000001174; 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 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..392
FT /note="Phosphoglycerate kinase"
FT /id="PRO_1000057994"
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 345..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4FEY"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4FEY"
FT TURN 116..121
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4FEY"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:4FEY"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:4FEY"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 346..354
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:4EHJ"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:4FEY"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:4FEY"
SQ SEQUENCE 392 AA; 41937 MW; 15AEE0E9ED62DFD2 CRC64;
MSFLTLKDVD LKDKKVLVRV DFNVPVKDGK VTSKVRIEAA IPTIQYILDQ GGAVILMSHL
GRPTEGEYDS QFSLEPVAKA LSEIINKPVK FAKDWLDGVD VKAGEIVMCE NVRFNSGEKK
STDDLSKKIA SLGDVFVMDA FATAHRAQAS TYGVAKYIPV ACAGILLTNE IQALEKALKS
PKKPMAAIVG GSKVSTKLSV LNNLLDKVEI LIVGGGIANT FIKAEGFDVG NSLYEQDLVA
EATEILAKAK ALGVNIPVPV DVRVAKEFSE NAQAIIKKVS DVVADEMILD IGPESQKIIA
ELLKSANTIL WNGPVGVFEF DNFAEGTKAL SLAIAQSHAF SVAGGGDTIA AIEKFGIKDQ
VSYISTAGGA FLEFLEGKKL PAIEILKEKA IR
