ID A0A0U2YIB4_9BACL Unreviewed; 585 AA.
AC A0A0U2YIB4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=AUC31_03480 {ECO:0000313|EMBL:ALS74378.1};
OS Planococcus rifietoensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS74378.1, ECO:0000313|Proteomes:UP000067683};
RN [1] {ECO:0000313|EMBL:ALS74378.1, ECO:0000313|Proteomes:UP000067683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:ALS74378.1,
RC ECO:0000313|Proteomes:UP000067683};
RA See-Too W.S.;
RT "Complete genome of Planococcus rifietoensis type strain M8.";
RL Submitted (JAN-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 -!- 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}.
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DR EMBL; CP013659; ALS74378.1; -; Genomic_DNA.
DR RefSeq; WP_058381085.1; NZ_CP013659.2.
DR AlphaFoldDB; A0A0U2YIB4; -.
DR STRING; 200991.AUC31_03480; -.
DR KEGG; prt:AUC31_03480; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000067683; Chromosome.
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:ALS74378.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000067683};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 1..325
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 358..469
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 507..576
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 585 AA; 62760 MW; 0609D06AFF70D9F3 CRC64;
MRKTKIVCTI GPASESPEVL EQLMKAGMNV ARLNFSHGDH DEHALRIKRI REASEKTGIT
VGILLDTKGP EIRTHKMEND SIELETNQEI TISMTEVLGT KEMFSITYDK LIEDVHEGST
ILLDDGLIEL RVTSIDKERG QIHTIVENAG TLKTKKGVNV PGVSVQLPGI TEKDAADLLF
GIEQDVDFVA ASFVRRRSDV MEIRSLLEKN GGSHIQIIPK IENQEGVDNL DEIIMVSDGL
MVARGDLGVE IPAEEVPIVQ KSMINKCNSA GKPVITATQM LDSMQRNPRP TRAEASDVAN
AIFDGTDAIM LSGETAAGLY PVESVETMHR IAETTEAALD HKQIVSNRRK EKESNMTEAI
GQAVAYTALN LRVQAILAPT ESGHTAKMIS KYRPGSPVIA VTSTARTARK LTLIWGVQPI
VGTRVESTDE MLDVAVVEAL KHGLIKHGDL VIITAGVPVG EAGTTNLMKL RVIGDILAKG
QGIGKSVGFG EAVVVRNAEE ALAMDTEGKI IVTYGTDRDM MDAINNCAGI VTEEGGLTSH
AAVVGLSLGI PVIVGVKDAV TKVESGQDIT IDADAGVIYH GHASV
//
