PGK_STRP2
ID PGK_STRP2 Reviewed; 398 AA.
AC Q04LZ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=SPD_0445;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ54881.1; -; Genomic_DNA.
DR RefSeq; WP_001096759.1; NC_008533.2.
DR PDB; 3ZLB; X-ray; 1.78 A; A=1-398.
DR PDBsum; 3ZLB; -.
DR AlphaFoldDB; Q04LZ5; -.
DR SMR; Q04LZ5; -.
DR STRING; 373153.SPD_0445; -.
DR EnsemblBacteria; ABJ54881; ABJ54881; SPD_0445.
DR GeneID; 60233900; -.
DR KEGG; spd:SPD_0445; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_1_9; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 462069at2; -.
DR BioCyc; SPNE373153:G1G6V-486-MON; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000001452; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:CAFA.
DR GO; GO:0043532; F:angiostatin binding; IPI:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002020; F:protease binding; IPI:CAFA.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; IPI:CAFA.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IPI:CAFA.
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; Transferase.
FT CHAIN 1..398
FT /note="Phosphoglycerate kinase"
FT /id="PRO_1000009654"
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 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 208
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 354..357
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:3ZLB"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:3ZLB"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3ZLB"
FT TURN 127..131
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3ZLB"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:3ZLB"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:3ZLB"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 378..384
FT /evidence="ECO:0007829|PDB:3ZLB"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:3ZLB"
SQ SEQUENCE 398 AA; 41939 MW; BDDA8FD4B336BC91 CRC64;
MAKLTVKDVD LKGKKVLVRV DFNVPLKDGV ITNDNRITAA LPTIKYIIEQ GGRAILFSHL
GRVKEESDKA GKSLAPVAAD LAAKLGQDVV FPGVTRGAEL EAAINALEDG QVLLVENTRY
EDVDGKKESK NDPELGKYWA SLGDGIFVND AFGTAHRAHA SNVGISANVE KAVAGFLLEN
EIAYIQEAVE TPERPFVAIL GGSKVSDKIG VIENLLEKAD KVLIGGGMTY TFYKAQGIEI
GNSLVEEDKL DVAKALLEKA NGKLILPVDS KEANAFAGYT EVRDTEGEAV SEGFLGLDIG
PKSIAKFDEA LTGAKTVVWN GPMGVFENPD FQAGTIGVMD AIVKQPGVKS IIGGGDSAAA
AINLGRADKF SWISTGGGAS MELLEGKVLP GLAALTEK
