ID A0A4V2JSR0_9ACTN Unreviewed; 470 AA.
AC A0A4V2JSR0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00018587, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=pyk {ECO:0000313|EMBL:TBT87467.1};
GN ORFNames=ET989_02870 {ECO:0000313|EMBL:TBT87467.1};
OS Propioniciclava sinopodophylli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propioniciclava.
OX NCBI_TaxID=1837344 {ECO:0000313|EMBL:TBT87467.1, ECO:0000313|Proteomes:UP000292373};
RN [1] {ECO:0000313|EMBL:TBT87467.1, ECO:0000313|Proteomes:UP000292373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 33808 {ECO:0000313|EMBL:TBT87467.1,
RC ECO:0000313|Proteomes:UP000292373};
RA Huptas C., Wenning M., Breitenwieser F., Doll E., Von Neubeck M.,
RA Busse H.-J., Scherer S.;
RT "Lactibacter flavus gen. nov., sp. nov., a novel bacterium of the family
RT Propionibacteriaceae isolated from raw milk and dairy products.";
RL Submitted (JAN-2019) 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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:TBT87467.1}.
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DR EMBL; SDMQ01000002; TBT87467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V2JSR0; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000292373; 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; 2.40.33.10; PK beta-barrel domain-like; 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; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
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; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 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:TBT87467.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000292373};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:TBT87467.1}.
FT DOMAIN 4..324
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 356..466
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 470 AA; 50125 MW; 6A5286B590F66F46 CRC64;
MPARRAKIVC TLGPATDSYE SVMELVEAGM NVARLNMSHG DHETHLRRLN NVRQAAQAAG
RPIGVFADLQ GPKIRLGNFE NGSEMIEAGD GFTITTQDVP GTKERAGTTL HTLTNDVRPG
DQILINDGAI ELRALEVTDT DVVTEVVIGG RVSDHKGINL PGVAVSVPAL SEKDADDLRW
ALEHGVDMVA LSFVRNASDI DDVHAIMDEF GMRVPVIAKI EKPQAVAALD EIVRAFDAIM
VARGDLGVEL PLEDVPGVQK SIITAARLVA KPVIVATQML ESMITAPRPT RAEASDVANA
ILDGADAVML SGETAVGAWP IVTVETMGRI VRKIESLGLE RIAPIDWNPH TTSGIIAKAA
VEIAERIGAK YLVAFTKTGD TALRLTRLRS TIPVCTFSPY VETAQKMTLA WGIKAFTTPE
FYSIDSMVEA VQNALKGSGL VETGDTIVIV AGNPKHSAGK TNSVRVAVIP
//
