ID B5JE82_9BACT Unreviewed; 485 AA.
AC B5JE82;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=VDG1235_3640 {ECO:0000313|EMBL:EDY84013.1};
OS Verrucomicrobiae bacterium DG1235.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY84013.1, ECO:0000313|Proteomes:UP000003839};
RN [1] {ECO:0000313|EMBL:EDY84013.1, ECO:0000313|Proteomes:UP000003839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG1235 {ECO:0000313|EMBL:EDY84013.1,
RC ECO:0000313|Proteomes:UP000003839};
RA Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; DS990592; EDY84013.1; -; Genomic_DNA.
DR AlphaFoldDB; B5JE82; -.
DR STRING; 382464.VDG1235_3640; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_3_0_0; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000003839; 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; 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.
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:EDY84013.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003839};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EDY84013.1}.
FT DOMAIN 10..338
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 369..468
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 485 AA; 53514 MW; CB2086F1E1445AA8 CRC64;
MFQDSHRIPR RTKIIFTVGP ATDSEEMLES LIGEHYVDIC RINMAHANHD YVRTVVRRIR
KVGERLNRHI PVMMDVKGPE IRTGDVDAPI ELKPGEIFDF TIKPGANEGE SGGEEIRSVD
VNYAELINDV DVGSIVLVDN GLIRLEVLEK INARIRCKVT IAGELTSRRH INLPGVKVNL
PALTEKDRGD TRVGIEEGVD FYALSFVRES SDLQLLRDFL DENGAHKSLI IAKIEDQSAI
SNLYSIIQDC DGLMVARGDL GIECPFETLP TIQRKAVKAC LTLGKPVIIA THMLESMISS
PMPTRAEVSD VANAVLEEAD CVMLSGETTI GKYPVQCVDA ITKIATEVDR NGQKTGYAKH
FSLESDKAKI QHSAVVMANE LNAVAIICFT RSGNMAKGVS ALRPERSPIF AFSNSHDTIK
QLRLHHGIIP FQMIFCTEPD ATVSRAMKHL KKRGYLIPGD KIVVVSDILA ANSIINSIQL
RTVTA
//
