ID A0A0A0K324_9MICO Unreviewed; 485 AA.
AC A0A0A0K324;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=N801_11150 {ECO:0000313|EMBL:KGN42717.1};
OS Knoellia aerolata DSM 18566.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385519 {ECO:0000313|EMBL:KGN42717.1, ECO:0000313|Proteomes:UP000030013};
RN [1] {ECO:0000313|EMBL:KGN42717.1, ECO:0000313|Proteomes:UP000030013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18566 {ECO:0000313|EMBL:KGN42717.1,
RC ECO:0000313|Proteomes:UP000030013};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia aerolata.";
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:KGN42717.1}.
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DR EMBL; AVPL01000002; KGN42717.1; -; Genomic_DNA.
DR RefSeq; WP_035932084.1; NZ_AVPL01000002.1.
DR AlphaFoldDB; A0A0A0K324; -.
DR STRING; 1385519.N801_11150; -.
DR eggNOG; COG0469; Bacteria.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000030013; 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:KGN42717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030013};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:KGN42717.1}.
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 485 AA; 51939 MW; 3762A669ACF86D10 CRC64;
MRRAKIVCTL GPATSSPEQL RELVDAGMDV ARFNLSHGDL VDHARVYMDV RRASDETGHA
VGILADLQGP KIRTGRFRDG SVMLDNGARF TITNRDIEGT VDAVGTTYAG LPSDVSTGDT
ILIDDGKLAL TVLESDGTDI LCEVVEGGVL SNNKGINVPG AAMSVPALSE KDEDDLRWAL
DMKVDMIALS FVRSAADIVP VHKIMDEKGY RIPVIAKIEK PQAVDNLDEI VRAFDGLMVA
RGDLGVEMPL ETVPLVQKRA CELGRRQAKP VIVATQVLES MITNSRPTRA EASDAANAVL
DGADALMLSG ETSVGAHPIE AVRTMARIIE NTEEHGLGRI LPLENKPRTK GGAVTAAAAE
IGELLGCKFL ITFTVGGDSS RRLARVRPRI PMLAFTPFQW TRSQLALTWG VETFLTAEPR
HTDDYAVQVD DELLACGRAE EGDVVVIVAG SPPGIPGSTN ALRVHRIGDA KNKVAPAYAE
VDNDA
//
