ID A0A6B3GBH8_9ACTN Unreviewed; 209 AA.
AC A0A6B3GBH8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE Flags: Fragment;
GN ORFNames=G3M53_31325 {ECO:0000313|EMBL:NEE29924.1};
OS Streptomyces sp. SID7982.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2706094 {ECO:0000313|EMBL:NEE29924.1, ECO:0000313|Proteomes:UP000482171};
RN [1] {ECO:0000313|EMBL:NEE29924.1, ECO:0000313|Proteomes:UP000482171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SID7982 {ECO:0000313|EMBL:NEE29924.1,
RC ECO:0000313|Proteomes:UP000482171};
RA Currrie C., Chevrette M., Carlson C., Stubbendieck R., Wendt-Pienkowski E.;
RT "Insect and environment-associated Actinomycetes.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|RuleBase:RU000504};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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:NEE29924.1}.
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DR EMBL; JAAGMV010003900; NEE29924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6B3GBH8; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000482171; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:NEE29924.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000482171};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:NEE29924.1}.
FT DOMAIN 2..55
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 89..201
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NEE29924.1"
SQ SEQUENCE 209 AA; 22191 MW; D887A5FB76D60211 CRC64;
AKPVIVATQM MESMITNSRP TRAEASDVAN AILDGADAVM LSAESSVGAY PIETVKTMSK
IVCAAEEELL SKGLQPLVQG KKPRTQGGSV ARAACEIADF LDGKALVAFT QSGDTARRLS
RYRTAQPILA FTTDENTRNQ LALSWGVESY VVPHVDNTDA MVDLVDAELL KLNRYSSGDT
MVITAGSPPG VPGTTNMVRV HHLGGGERD
//
