ID A0A3P7P0M5_9FIRM Unreviewed; 476 AA.
AC A0A3P7P0M5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:VDN47020.1};
GN ORFNames=PATL70BA_1145 {ECO:0000313|EMBL:VDN47020.1};
OS Petrocella atlantisensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Vallitaleaceae; Petrocella.
OX NCBI_TaxID=2173034 {ECO:0000313|EMBL:VDN47020.1, ECO:0000313|Proteomes:UP000279029};
RN [1] {ECO:0000313|EMBL:VDN47020.1, ECO:0000313|Proteomes:UP000279029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70B-A {ECO:0000313|EMBL:VDN47020.1};
RA Postec A.;
RL Submitted (SEP-2018) 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 -!- 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}.
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DR EMBL; LR130778; VDN47020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P7P0M5; -.
DR KEGG; cbar:PATL70BA_1145; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000279029; Chromosome 1.
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:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 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:VDN47020.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000279029};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:VDN47020.1}.
FT DOMAIN 1..319
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 354..467
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 476 AA; 52256 MW; 72573AF36B76A178 CRC64;
MRKTKIICTM GPATEGIYED MILNGMDAAR FNFSHENHEV HGHRIKTMKV ARAKLNQPIP
LIVDTKGPEM RIGVLKNKVN LVNGEIIKLI SEEIEGDEKA VTISFKDLYK SVSIGQSIYI
DDGRINLEVV SIEGTDIVCK IIAGGVLSSR KGVNVPGCIT GLPFMTEKDR ADIEFAVDQD
VDFIALSFVS NAKDVESVRE IFKQKNREDI KIISKIENTE AIKNIDEIIA VSDSIMIARG
DLGIELPVKS VPIIQKKLIK KCYTSSKPVI VATQMLESMT DNPVPTRAEV SDVANAIYDG
TSVVMLSGET AAGKYPIETL RMMTTVILET ENDIDYKVKL DEGAWKVIDQ NVINAISEVT
VIAASKIDAK AIVVPTRSGN SVRMISSFRP ACPIIAITLE EGLQRQLNLS WGIKPMMSKF
IGDQKEFFEK VLDQAVATKL VEKGDLIILT AGIPTGYDGK TNMLKMHKVG DEVIGG
//
