ID A0A365KLT5_9BACL Unreviewed; 586 AA.
AC A0A365KLT5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:RAZ74089.1};
GN ORFNames=DP120_16040 {ECO:0000313|EMBL:RAZ74089.1};
OS Planococcus halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=2233542 {ECO:0000313|EMBL:RAZ74089.1, ECO:0000313|Proteomes:UP000251002};
RN [1] {ECO:0000313|EMBL:RAZ74089.1, ECO:0000313|Proteomes:UP000251002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCU63 {ECO:0000313|EMBL:RAZ74089.1,
RC ECO:0000313|Proteomes:UP000251002};
RA Gan L.;
RT "The draft genome sequences of strains SCU63 and S1.";
RL Submitted (JUN-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 -!- 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:RAZ74089.1}.
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DR EMBL; QLZR01000008; RAZ74089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365KLT5; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000251002; 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:RAZ74089.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000251002};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:RAZ74089.1}.
FT DOMAIN 1..325
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 358..471
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 586 AA; 62638 MW; 38BE4463A092F246 CRC64;
MRKTKIVCTI GPASESPEIL ESLIESGMNV ARLNFSHGNH EEHAERIKRI RQASEKTGKI
VGILLDTKGP EIRTHQMEND GIDLVTNQNI TISMTEVLGT AEKFSITYDH LIEDVQKGSI
ILLDDGLIEL RVDSIDKENG LIHTVVENAG TLKSKKGVNV PGVSVQLPGI TDKDAQDILF
GISQKVDFVA ASFVRRSSDV MEIRELLEKN GGSHIQIIPK IENQEGVDNI DDIIMVSDGL
MVARGDLGVE IPAEEVPLVQ KSLIEKCNSA GKPVITATQM LDSMQRNPRP TRAEASDVAN
AIFDGTDAIM LSGETAAGIY PVESVETMHR IAMTTESALN YKQLVSNRRK DKEANMTEAI
GQAVVYTALN LKVKAIIAPT ESGTTAKMIS KYRPESPIIA VTSSEIAAKK LTLVWGVQPI
VGTPVSSTDE VFAIAVEESL KHEYVDHGDL VVITAGVPVG KAGTTNLMKV HVIGDIAAKG
QGIGKTVAYG ESLVVKSAEE ANAVDTEGKI LVTIGSDREM MPAIEKCAGL ITEEGGLTSH
AAVVGLSLGI PVIVGVKNAT SIIKNNEDIT IDAETGVVYH GHASVL
//
