ID A0A0G1VV25_9BACT Unreviewed; 460 AA.
AC A0A0G1VV25;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 03-MAY-2023, entry version 39.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
GN Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145};
GN ORFNames=UX98_C0003G0015 {ECO:0000313|EMBL:KKU73940.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_26.
OC Bacteria.
OX NCBI_TaxID=1618844 {ECO:0000313|EMBL:KKU73940.1, ECO:0000313|Proteomes:UP000034356};
RN [1] {ECO:0000313|EMBL:KKU73940.1, ECO:0000313|Proteomes:UP000034356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:0000256|ARBA:ARBA00000642, ECO:0000256|HAMAP-
CC Rule:MF_00145, ECO:0000256|RuleBase:RU000532};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC Rule:MF_00145}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKU73940.1}.
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DR EMBL; LCOG01000003; KKU73940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1VV25; -.
DR STRING; 1618844.UX98_C0003G0015; -.
DR PATRIC; fig|1618844.3.peg.193; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000034356; Unassembled WGS sequence.
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; 2.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00145}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00145};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00145};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00145};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00145}.
FT BINDING 38..40
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 76..79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 411..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
SQ SEQUENCE 460 AA; 49880 MW; 2DAD0080816518C7 CRC64;
MTKGSVAVRG KSAQKTQTMK SVNELKNIRG KRVLVRVDFN VPVVHGEIED DTRIRTTVLT
IEWLAQKGAK VILMSHFGRP ILSRHPERSE GSRSRRELRD SSASGLRMTI FRLGELLKKK
VQMADKWDWV EIGQMIKAMK GGQVLMLPNL RLQTGEEKNS KPFAQGLAGL ADFYVNEAFS
VCHRKHASVV GVPKFLPSYA GFTLIKEVDT LGSILKAPKK PFIVLMGGAK ITDKIAMMQI
MTRKAEAVLV GGILALHFFK AMGYGVGGSR IEAEGVRLAK KLVGNRKIVL PLDVVVGKED
GEGARVVEMQ HVGPGLVLPP GRDVASTARQ QSSVRGRQGP ALQICSKPYA ILDIGPKTIL
EFAHYIKSAA TLLWNGPMGF YEVKRFSHGT SALGRLFAAR SRGKAFGVAG GGETIDALKQ
TGMMQDVDFV STGGGAILQF MSGKPLPGIT ALTYAKGFGN
//
