ID A0A2T0BF06_9CLOT Unreviewed; 472 AA.
AC A0A2T0BF06;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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_2 {ECO:0000313|EMBL:PRR82449.1};
GN ORFNames=CLVI_17890 {ECO:0000313|EMBL:PRR82449.1};
OS Clostridium vincentii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=52704 {ECO:0000313|EMBL:PRR82449.1, ECO:0000313|Proteomes:UP000239471};
RN [1] {ECO:0000313|EMBL:PRR82449.1, ECO:0000313|Proteomes:UP000239471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10228 {ECO:0000313|EMBL:PRR82449.1,
RC ECO:0000313|Proteomes:UP000239471};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium vincentii DSM 10228.";
RL Submitted (MAR-2018) 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 -!- 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}.
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:PRR82449.1}.
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DR EMBL; PVXQ01000016; PRR82449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0BF06; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000239471; 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:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 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:PRR82449.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239471};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:PRR82449.1}.
FT DOMAIN 1..323
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 357..469
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 472 AA; 51790 MW; 1AB7E94A274581BE CRC64;
MQKTKMIFTI GPASDTEEML RTFIKIGMSA ARLNFSHGTH ESHKEKIVLL KKIREDMDSP
TAIILDIKGP KIRTHNFIND GVEIEKGQDF SFICGEEILG DNTKCSITYD ILYRDVRPGG
SILVDDGLLK FEIVNVVGKE IKCKAIVSGL IQNHKGVNVP NVTIQLPSIT EKDIEDIAFG
CEMGVDFIAA SFIRKASDIL EVRRVLRKYN GEHIQIIAKI ENQEGVENID SIIEVTDCVM
VARGDMGVEI PIEKVPIIQK MIIKKCRKAG KTVITATQML DSMIRNSIPT RAEASDICNA
IFDGTDAIML SGESASGCFP TEAAQTMSRI ALEAEANLDY DHLNESLAES SLTEYADAIS
YSTCRTAVAL NAKVIVAATK SGSTARLLSK YRPRCIIVGI TPYENVRRGL TLNFGVLPTK
CDMFNTTDDI LVESKKVVYD LNLAGKGDDI IIAAGMPTTH TGGTNMMKIE KL
//
