ID A0A0A0C4R2_9CELL Unreviewed; 474 AA.
AC A0A0A0C4R2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=N869_13875 {ECO:0000313|EMBL:KGM14339.1};
OS Cellulomonas bogoriensis 69B4 = DSM 16987.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM14339.1, ECO:0000313|Proteomes:UP000054314};
RN [1] {ECO:0000313|EMBL:KGM14339.1, ECO:0000313|Proteomes:UP000054314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69B4 {ECO:0000313|EMBL:KGM14339.1,
RC ECO:0000313|Proteomes:UP000054314};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL Submitted (AUG-2013) 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:KGM14339.1}.
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DR EMBL; AXCZ01000005; KGM14339.1; -; Genomic_DNA.
DR RefSeq; WP_035056679.1; NZ_AXCZ01000005.1.
DR AlphaFoldDB; A0A0A0C4R2; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000054314; 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:KGM14339.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054314};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:KGM14339.1}.
FT DOMAIN 1..322
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 353..465
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 474 AA; 50405 MW; 686BF1BFEBC355ED CRC64;
MRRAKIVCTI GPATESPEQI QALVDAGMDV ARINRSHGDA SEHEAVINRV RAAAKASGKA
VAVLVDLQGP KIRLGRFVEG KHELAVGDIF TITTEDVPGT KELVSTTYKG LPGDAKVGDR
ILIDDGRVAV RITAVEGERV VTRVEVPGPV SNNKGLNLPG VAVSVPAMSD KDETDLRWAL
RLGADLIALS FVRSAVDYDD VAAIMAEEGR TVPVIAKVEK PQAVDNLAEI VDAFDGVMVA
RGDLGVELPL EQVPLVQKRA IELCRRSAKP VIVATQVLES MISAPRPTRA EASDCANAVL
DGADAVMLSG ETSVGDYPIE AVRTMARIIE NTEEHGSDRI APLGWSPQTR GGAITRAAAE
VGETLGVKYL VTFTQTGDSA RRMSRLRASI PLIAFTPETA VRNTLALSWG VSTYEVPKVE
HTDAMVMQVD QMLRANGLAE EGDRVVIVCG APVGVPGTTN SLLVHKIGTE LSNR
//