ID A0A0H4VLG7_9BACT Unreviewed; 476 AA.
AC A0A0H4VLG7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=TH63_02530 {ECO:0000313|EMBL:AKQ44752.1};
OS Rufibacter radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1379910 {ECO:0000313|EMBL:AKQ44752.1, ECO:0000313|Proteomes:UP000036458};
RN [1] {ECO:0000313|EMBL:AKQ44752.1, ECO:0000313|Proteomes:UP000036458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG31D {ECO:0000313|EMBL:AKQ44752.1,
RC ECO:0000313|Proteomes:UP000036458};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Rufibacter sp./DG31D/ whole genome sequencing.";
RL Submitted (JAN-2015) 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; CP010777; AKQ44752.1; -; Genomic_DNA.
DR RefSeq; WP_048919544.1; NZ_CP010777.1.
DR AlphaFoldDB; A0A0H4VLG7; -.
DR STRING; 1379910.TH63_02530; -.
DR KEGG; ruf:TH63_02530; -.
DR PATRIC; fig|1379910.4.peg.544; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000036458; 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; 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:AKQ44752.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036458};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 6..327
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 360..471
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 476 AA; 52615 MW; A133B7903E68513D CRC64;
MAIHFNKTKI IATVGPASNT PERLRALIQE GVDVFRLNFS HGTHPEHLKV IEHVRAINAE
EGFNICLVQD LQGPKIRLND IENGAVEIVA GQQVTIVCDK SVGTSTRLST SYLRLAHDVR
PGDAILIDDG KLELTVISTD GDKEVLTEVV YGGVVKPRKG INLPDTVVTA PSLTEKDIQD
LHFGLDNDVE WVALSFVRKV EDIHEIKRII AERGKDTRVI AKVEKPEAIR NIDSIIEATD
AVMVARGDLG VEIGMEEVPM LQKMIVEKCQ AVGKPVIIAT QMMESMITNP RPTRAETNDI
ANAVMDGADT LMLSAETAAG AYPIETIRSM NRTIQSVESQ AEVFHRNFVY NPEGDTFMND
TVVASAVGLA RDTDARALIG LTKSGYTAFQ LAKHRPKSHI FIFTDNRALL TTLNLVWGIR
GFYYDRFVST DDTISDLKEI LLREGHLEKG DVFINIGSMP VMEKKRANMI KLSIVH
//
