ID A0A3A1XJH0_9BIFI Unreviewed; 479 AA.
AC A0A3A1XJH0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 Name=pyk {ECO:0000313|EMBL:RIY23514.1};
GN ORFNames=CJI50_06135 {ECO:0000313|EMBL:RIY23514.1};
OS Bifidobacteriaceae bacterium NR021.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae.
OX NCBI_TaxID=2026094 {ECO:0000313|EMBL:RIY23514.1, ECO:0000313|Proteomes:UP000266454};
RN [1] {ECO:0000313|EMBL:RIY23514.1, ECO:0000313|Proteomes:UP000266454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NR021 {ECO:0000313|EMBL:RIY23514.1,
RC ECO:0000313|Proteomes:UP000266454};
RA Vancuren S.J., Hill J.E.;
RT "A comparative genomics approach to explaining the enigmatic role of
RT Gardnerella vaginalis in the vaginal microbiome.";
RL Submitted (AUG-2017) 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:RIY23514.1}.
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DR EMBL; NQOP01000005; RIY23514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1XJH0; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000266454; 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:RIY23514.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000266454};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 1..327
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 357..473
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 479 AA; 52321 MW; C12CFEB47EA4D134 CRC64;
MRKAKIVDTI GPATESLEGI TKLVEAGMDV ARLNRSHGTP EDHLRVYNNV RAASKSTGRN
VAALVDLQGP KIRCGWFKKN AEGEDKVYLE EGQEFIITTD DVEGDEHRTS TTFKGLPGDC
HAGDPILIDD GKVRLEVTKV EGNDVHTKVI VAGPVSSHKG INLPGVAVSL PALTEKDEAD
LRWAIRTGAD IIAMSFVRFA TDIDRAHEIM DEEGRRIPIV AKIEKPQAVE NLEEIVKTFD
GIMVARGDMA VEMPLEEVPL VTKRCIELSR RYAKPVIVAT EVLGTMVNSP VPTRAEASDC
ANAVLDGADA TMTSNETAVG KYPDVTVKTM SRISQYATEH GYDRIPAVEL DMSSTGAVSS
AAVDLADKLN AKAIVAYTQT GRTVHRISRE RPTAPIYGLT NNEHTYRWLA LSWGTEGFLI
DEDYHDMNRH DLMIFTDKVL REAGKVSDGD QIVILSTAQG ERQAGRTDSI YVHTVGACD
//
