PGK_NOSS1
ID PGK_NOSS1 Reviewed; 400 AA.
AC Q8YPR1;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=all4131;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP PROTEIN SEQUENCE OF 306-315, AND MASS SPECTROMETRY.
RA Singh H., Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
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 -!- MASS SPECTROMETRY: Mass=42472; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00145}.
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DR EMBL; BA000019; BAB75830.1; -; Genomic_DNA.
DR PIR; AD2322; AD2322.
DR RefSeq; WP_010998270.1; NZ_RSCN01000010.1.
DR AlphaFoldDB; Q8YPR1; -.
DR SMR; Q8YPR1; -.
DR STRING; 103690.17133266; -.
DR EnsemblBacteria; BAB75830; BAB75830; BAB75830.
DR KEGG; ana:all4131; -.
DR eggNOG; COG0126; Bacteria.
DR OMA; DMIFDIG; -.
DR OrthoDB; 462069at2; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000002483; 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 CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..400
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145897"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 154
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 356..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ SEQUENCE 400 AA; 42441 MW; FA9EBE9015D4C0F9 CRC64;
MSKKTVASLS AADISGKRAL VRVDFNVPLD DQGNITDDTR IRAALPTIQD LTQKGAKVIL
ASHFGRPKGV DEKLRLTPVA KRLSELLGQE VIKTDDSIGD EVAAKVATLQ NGQVLLLENV
RFYKEEEKND PEFAKKLAAN ADFYVNDAFG TAHRAHASTE GVTKFLSPSV AGYLVEKELQ
YLQSAIENPQ RPLAAIIGGS KVSSKIGVIE TLLEKCDKLI IGGGMIFTFY KARGLNVGKS
LVEEDKLELA KSLEAKAKER GVSLLLPTDV VLADNFAPDA NSQTVSIENI PDGWMGLDIG
PDSVKVFQAA LADTKTVIWN GPMGVFEFDK FAAGTEAIAH TLAEIGKTGT TTIIGGGDSV
AAVEKVGLAD QMSHISTGGG ASLELLEGKV LPGIAALDEA