ID A0A136KJ01_9BACT Unreviewed; 479 AA.
AC A0A136KJ01;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:KXK09392.1};
GN ORFNames=UZ22_OP11002001074 {ECO:0000313|EMBL:KXK09392.1};
OS Microgenomates bacterium OLB23.
OC Bacteria; Candidatus Microgenomates.
OX NCBI_TaxID=1617429 {ECO:0000313|EMBL:KXK09392.1, ECO:0000313|Proteomes:UP000070280};
RN [1] {ECO:0000313|EMBL:KXK09392.1, ECO:0000313|Proteomes:UP000070280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB23 {ECO:0000313|EMBL:KXK09392.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-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}.
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:KXK09392.1}.
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DR EMBL; LMZU01000045; KXK09392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136KJ01; -.
DR STRING; 1617429.UZ22_OP11002001074; -.
DR PATRIC; fig|1617429.3.peg.1152; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000070280; 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:KXK09392.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:KXK09392.1}.
FT DOMAIN 3..320
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 376..475
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 479 AA; 53143 MW; C0B77B967EFA0814 CRC64;
MQLTKIIATV GPDILSPQAI TDLIAKGVSV FRFNFKHNTV EWHSEGIQMV NRVSEEIGKP
VATLIDLQGP SIRIHMPTDS LALKKNEKIY FGEVVFEKNV KGLSITYPNI ITSLNDGQLI
VADDGNFRFT VHKEGSQTYL VSHTAGVLLN KKSLNIPGGD FPFPALVARD FEGIQLAARE
EVDYIALSFV RSKADIDDLR AEMKKYKITA DVISKIETMK ALDNIDEIIA ASDGIMVARG
DLGVELPFEE VPYYQKLLIA KCLDASKPVI TATQMLNSMI EHPIPTRAEV SDVANAVYDF
TDAVMLSGET AFGNYPFKSV EAMQRITTFN EKKLTFDLRK RYKFVTADNE ARVCEMAYNL
FLSLAKDSPE ELGGFLVFTR SGRTARLLSR YRPRPAMPIF AFTDNETVRD KLALSFAVQP
ILFKEGEARS DVKKDQILSA IAHLTGAKLV KKGKLIIVLH GDKWAVTGGT STVKLLKAQ
//
