ID A0A2U9IBM4_9CREN Unreviewed; 444 AA.
AC A0A2U9IBM4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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};
GN Name=pyk {ECO:0000313|EMBL:AWR93410.1};
GN ORFNames=DFR85_01085 {ECO:0000313|EMBL:AWR93410.1};
OS Acidianus brierleyi.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=41673 {ECO:0000313|EMBL:AWR93410.1, ECO:0000313|Proteomes:UP000248044};
RN [1] {ECO:0000313|EMBL:AWR93410.1, ECO:0000313|Proteomes:UP000248044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1651 {ECO:0000313|EMBL:AWR93410.1,
RC ECO:0000313|Proteomes:UP000248044};
RA Counts J.A., Kelly R.M.;
RT "Complete Genome Sequences of Extremely Thermoacidophilic, Metal-Mobilizing
RT Type-Strain Members of the Archaeal Family Sulfolobaceae: Acidianus
RT brierleyi DSM-1651T, Acidianus sulfidivorans DSM-18786T, Metallosphaera
RT hakonensis DSM-7519T, and Metallosphaera prunae DSM-10039T.";
RL Submitted (MAY-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 -!- 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; CP029289; AWR93410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9IBM4; -.
DR KEGG; abri:DFR85_01085; -.
DR OrthoDB; 56298at2157; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000248044; Chromosome.
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:AWR93410.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248044};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 1..304
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 331..442
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 444 AA; 49023 MW; 614F383BCD735808 CRC64;
MRKTKIVATL GPSSENKVKE LSKYVNIFRL NFAHGDENSH KKYFDLIKDY AKDASILVDL
PGPKIRIGDI NGKLDLKSGD KIVFSEKEGI PVEDPLFYKA VKEGIYILLA DGNIKVKIDK
VDSDKVEATV IEGGILTSRK GINIPDIKLD SGITDNDLKL LNEALRLGAD FIGLSFVISY
KDVIKIKNMV KDKVWIISKI EKKSAVNDLH NIIRESDGIM VARGDLGVEI GLENLPFVQK
KIIKLSKLNG KPVILATQVL ESMVNSPMPT RAEVIDISNS ISQGVDAIML SDETAAGNFP
IEAVKYLDNI ITAVEKRVKT VRPPPKSSSD DAIAIAAVNV AEVSKSKIIA VHSRSGISAI
RISRLRPKVP IIALCPNENI VKKLKLCWGV YPFYVREVRS LDEITQLVEE YSKDYVKEGE
SIVIAGGDPK LEEGRTNFIK LHRA
//
