ID A0A1H7LLA2_9FIRM Unreviewed; 357 AA.
AC A0A1H7LLA2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=SAMN04487770_1052 {ECO:0000313|EMBL:SEK99255.1};
OS Butyrivibrio sp. ob235.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1761780 {ECO:0000313|EMBL:SEK99255.1, ECO:0000313|Proteomes:UP000199418};
RN [1] {ECO:0000313|EMBL:SEK99255.1, ECO:0000313|Proteomes:UP000199418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB235 {ECO:0000313|EMBL:SEK99255.1,
RC ECO:0000313|Proteomes:UP000199418};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; FOBE01000005; SEK99255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7LLA2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000199418; 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 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; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel 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:SEK99255.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199418};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 24..340
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
SQ SEQUENCE 357 AA; 39567 MW; 77B64BAB17189D87 CRC64;
MRYGEINGTD SIVGLENEIK FMVDIFGTLG PSCNDEATLK AMFMAGMTGV RINLSHVMLR
DNEELLNFVK RAAESVCIDP KILIDLQGPE LRIGNLQKEI NLCSGDEIPV RCEGYHGVIS
DVIPLDKRIF EEMEEGDEIL LDDGKILAGV EHRSNNEAIL KIIRGGILNS RKSILIKGKT
ILMPTLTSDD ISNISDAVKL GVTGVMQPFV RNRQDLQILR KTLDDAGGDK IEIYAKIENM
DGVGMLPDIM DECDEIVIAR GDLGNAMPLW ELPYVQKRIS KECRTRSKRF MVVTQMLASM
EHSPIPTRAE VSDIYNAVAD GASSVMVTGE TAIGEYPVEV IEFLSKTALQ YEKSKKI
//
