ID Q0EYB7_9PROT Unreviewed; 486 AA.
AC Q0EYB7;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 85.
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 ORFNames=SPV1_05924 {ECO:0000313|EMBL:EAU54275.1};
OS Mariprofundus ferrooxydans PV-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU54275.1, ECO:0000313|Proteomes:UP000005297};
RN [1] {ECO:0000313|EMBL:EAU54275.1, ECO:0000313|Proteomes:UP000005297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU54275.1,
RC ECO:0000313|Proteomes:UP000005297};
RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) 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:EAU54275.1}.
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DR EMBL; AATS01000010; EAU54275.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0EYB7; -.
DR STRING; 314344.AL013_06285; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_0; -.
DR InParanoid; Q0EYB7; -.
DR OrthoDB; 5288036at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000005297; 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:SF125; PYRUVATE KINASE II; 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:EAU54275.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005297};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EAU54275.1}.
FT DOMAIN 5..330
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 364..479
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 486 AA; 52032 MW; 7ED987A06BB7EC31 CRC64;
MSKIIRRTKI VATLGPASES PAVLDRLIKA GVNVVRLNFS HGTPEEHRQR AESVRAAAKN
NGVVVGILAD MQGPKIRVGK FITGKTELVP GQKFIIDAEM DLDAGNDERV GITYKELIDD
VKPGDRLLLN DGLIVMDADS VVGQEIHCTV ILGGELSNNK GINKAGGGLS AAALTEKDKE
DIITACSIGV DYIAISFPRH GADMDYARSL VRAAGGHAGL VAKVERAEAV EDENLKSIME
SSDAVMVARG DLGVEVGDAA VPPIQKKMLR MAPKYNCPVI VATQMMESMC SNPIPTRAEV
NDVANAVLDG TDAVMLSGES AAGKYPVEAV EAMHRTCIET EKQRVLPSSA TRDPRFPPHS
VDECIARQAM ETAHSMPIRA IAAFTDTGNT VLYMSRHLGD VPIYALTPKQ STLGRVTLFR
NVTPLCMPVD YGPTEAPQAT IDVKQMMLEK GIVNEEDLII MTFGTPMGHS GGTNALKIIR
IGDNLS
//
