ID A0A0S8CGG4_9CHLR Unreviewed; 426 AA.
AC A0A0S8CGG4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
DE Flags: Fragment;
GN ORFNames=AMJ70_05280 {ECO:0000313|EMBL:KPK22705.1};
OS Dehalococcoidia bacterium SG8_51_3.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703394 {ECO:0000313|EMBL:KPK22705.1, ECO:0000313|Proteomes:UP000051285};
RN [1] {ECO:0000313|EMBL:KPK22705.1, ECO:0000313|Proteomes:UP000051285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_51_3 {ECO:0000313|EMBL:KPK22705.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK22705.1}.
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DR EMBL; LJTX01000089; KPK22705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CGG4; -.
DR PATRIC; fig|1703394.3.peg.343; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000051285; 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};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 2..277
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 311..422
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPK22705.1"
SQ SEQUENCE 426 AA; 46007 MW; 8FE77EBDA5406779 CRC64;
YIQIVRKLSH HLAIPIAVIM DLPGPKYRTG KLKDGRAELR KGAEVVLTTR SITGSNRVVP
VNLPTLPQDT KVGDTVLLDD GAMQLKVLER RGTEMRCRVV VGGILTERRG LAVPGMRDSA
PFITNALRKH ISFAVRHQPD YLAVSFVSGA DDVASVKAIL REDGIDIPVI AKIERGVAVD
GFGDILAISD GIMVARGDLG VDIPLEKVPL VQKEIIKKCN RAGKLVITAT QMLESMINTP
WPTRAEVTDV ANAIFDGTDA IMLSAETSIG KYPAQAVRMM GKIAREAEER LPYEQMLSER
ANWLEQTTSE LISYSACHTA QSLEANALVA FTQSGSTAGR VSRCRPRVPI VAITPDDAVA
RRLVLQWGVY PFQIAGASSV EELFATGMRL SRELGLAKSG DLIVITGGIP VGVTGSTNLL
KVSKIQ
//
