ID A0A1J7C5G3_9GAMM Unreviewed; 470 AA.
AC A0A1J7C5G3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN ORFNames=BK025_13630 {ECO:0000313|EMBL:OIV46182.1};
OS Sodalis sp. TME1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1912097 {ECO:0000313|EMBL:OIV46182.1, ECO:0000313|Proteomes:UP000181913};
RN [1] {ECO:0000313|EMBL:OIV46182.1, ECO:0000313|Proteomes:UP000181913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TME1 {ECO:0000313|EMBL:OIV46182.1,
RC ECO:0000313|Proteomes:UP000181913};
RA Rosas-Perez T., Vera-Ponce De Leon A., Rosenblueth M., Ramirez-Puebla S.T.,
RA Rincon-Rosales R., Martinez-Romero J., Dunn M.F., Martinez-Romero E.;
RT "The Symbiome of Llaveia Cochineals (Hemiptera: Coccoidea: Monophlebidae)
RT Includes a Gammaproteobacterial Co-symbiont Sodalis TME1 and the Known
RT Candidatus Walczuchella monophlebidarum.";
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 -!- 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:OIV46182.1}.
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DR EMBL; MNBX01000426; OIV46182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7C5G3; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000181913; 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 CDD; cd00288; Pyruvate_Kinase; 1.
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:OIV46182.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000181913};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 1..325
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 356..468
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 470 AA; 50762 MW; 9FE54FAD7C11A32A CRC64;
MKKTKIVCTI GPKTESEEVL SSLLDAGMNV MRLNFSHGDY EEHGQRIKNL RAVLKRTGQQ
AAILLDTKGP EIRTMKLVNG ADVSLRAGQT FTFTTDQSVV GNSERVAVTY PGFTQDLAVG
NTVLVDDGLL GMTVTSVTQD EVVCKVLNNG DLGENKGVNL PGVSIALPAL AEKDKRDLIF
GCEQGVDFIA ASFIRKRSDV LEIREHLQQH GGEHIQIISK IENQEGLNNF DEILEASDGI
MVARGDLGVE IPVEEVIFAQ KMMIEKCNRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN
AILDGTDAVM LSGESAKGKY PLEAVTIMAT ICQRTDRMLP SRIDGQHDSR KLRITEAVCR
GAVETAEKLE SPLIVVATEG GKSAKSVRKY FPKAEILALT TNPLTARQLL LSKAVACQLV
EEIASTDDFY RIGKAMALET GLAAKGDIIV MVSGALVPSG TTNTASVHML
//
