ID A0A265Q7I7_9FIRM Unreviewed; 585 AA.
AC A0A265Q7I7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:OZV12238.1};
GN ORFNames=CIW83_10480 {ECO:0000313|EMBL:OZV12238.1};
OS Tissierella sp. P1.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC Tissierella.
OX NCBI_TaxID=1280483 {ECO:0000313|EMBL:OZV12238.1, ECO:0000313|Proteomes:UP000216906};
RN [1] {ECO:0000313|EMBL:OZV12238.1, ECO:0000313|Proteomes:UP000216906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:OZV12238.1,
RC ECO:0000313|Proteomes:UP000216906};
RA Bukhtiyarova P.A., Antsiferov D.V., Avakyan M.R., Frank Y.A., Ikkert O.P.,
RA Pimenov N.V., Brasseur G., Tuovinen O.H., Karnachuk O.V.;
RT "Isolation and Characterization of an Anaerobic Sulfidogenic Tissierella
RT from Cu-bearing Coins.";
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 -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing
CC enzyme family. {ECO:0000256|ARBA:ARBA00006237}.
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:OZV12238.1}.
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DR EMBL; NPMN01000012; OZV12238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A265Q7I7; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000216906; 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; 3.50.30.10; Phosphohistidine domain; 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; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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; PF00391; PEP-utilizers; 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; SSF52009; Phosphohistidine 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 Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:OZV12238.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216906};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 1..324
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 357..470
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 503..575
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 585 AA; 63194 MW; ADF31734D6847AD0 CRC64;
MKKTKIVCTI GPASESENVL KELFVNGLNV CRLNFSHGSH EEHKRRIDNI KKVREELNMP
IGIMLDTKGP EIRLGDFKDG TIEIEEGDIF TLTTRDIVGD KSIVSVSYVG LPNDIEKESR
ILIDDGLVEL KVLEIIDGTD IKCIALNNGT LKNHKGVNVP NVKINLPAIT KKDIDDILFG
IENGIDFIAA SFVRKASDVI EIRKILEENN ADFIEIISKI ENQEGVDNID EILAASDGIM
VARGDLGVEI QTEEMPLVQK ELIKKSNLVG KPVITATQML DSMMRNPRPT RAEVTDVANA
ILDGSSAIML SGETAAGKYP IESVKTMYNI AIRTEESLDY GEILKSKVAI TEVSTTNAIG
KATCTTAMDL GASAIITATS SGYTSKAISK FRPKSPIIAA TTTESVMRRL SLVWGVYPVL
SPYSNSTDDV IELSIQSAVD KGYIKEGDLV VITAGIPVGT SGSTNLIKVH TIGKVLLKGM
GIGKDSTLGR VCIANNGEEL MKKFRDGDVI VSKDTDREMV KFMEKASAII TEQGGLTSHA
AIVGLNLNKP TIVGAQDATT ILEDGEIITV DSTTGLIYKG EARVL
//
