ID A0A0L0LDP8_9BACT Unreviewed; 379 AA.
AC A0A0L0LDP8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 03-MAY-2023, entry version 22.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN Name=pgk {ECO:0000313|EMBL:KND48030.1};
GN ORFNames=AB201_00310 {ECO:0000313|EMBL:KND48030.1};
OS Parcubacteria bacterium C7867-006.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659200 {ECO:0000313|EMBL:KND48030.1, ECO:0000313|Proteomes:UP000037457};
RN [1] {ECO:0000313|EMBL:KND48030.1, ECO:0000313|Proteomes:UP000037457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-006 {ECO:0000313|EMBL:KND48030.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(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,
CC ECO:0000256|RuleBase:RU000532};
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|RuleBase:RU000532}.
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:KND48030.1}.
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DR EMBL; LFCP01000001; KND48030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LDP8; -.
DR STRING; 1659200.AB201_00310; -.
DR PATRIC; fig|1659200.3.peg.272; -.
DR Proteomes; UP000037457; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
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; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 336..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 379 AA; 42212 MW; 8962B84AAC2B7504 CRC64;
MKYIDELKGD DLKGKYVLLR LDLNVPVSNG QVVNAYRIDR AIPTIDYLRE HGAKVIIIAH
TESDANMTLV PVAQYLSGFF KIDFCQTYFN PIAIDKISKL EDRGVLLFEN LRINPEEKEN
NIEFAKKLAQ MADIYVDDAF GAMHRKHASI IGVPEFLPHY GGLLLKQEIE NLSKVFSPKK
PFLFIVGGVK FSTKLPLIKK YLDKADYVFI VGALANGIFK EKGFTLGTSL SIDGDFGIKE
LMNKDNFLYP IDVTVQKSDG SFEFRNPDEI GNDEYIGDLG PKTMEKLKEL IGISKTVVWN
GPLGDFEKGF KDKTEQLAEV IMKATEEGKI ESIVGGGDTL ASININEFEH GFTFVSTGGG
AMLDYLVNET LPGIEALNK
//
