ID A0A5M6DB27_9BACT Unreviewed; 476 AA.
AC A0A5M6DB27;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=pyk {ECO:0000313|EMBL:KAA5544573.1};
GN ORFNames=FYK55_09650 {ECO:0000313|EMBL:KAA5544573.1};
OS Roseiconus nitratireducens.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Roseiconus.
OX NCBI_TaxID=2605748 {ECO:0000313|EMBL:KAA5544573.1, ECO:0000313|Proteomes:UP000324479};
RN [1] {ECO:0000313|EMBL:KAA5544573.1, ECO:0000313|Proteomes:UP000324479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC645 {ECO:0000313|EMBL:KAA5544573.1,
RC ECO:0000313|Proteomes:UP000324479};
RA Dhanesh K., Kumar G., Sasikala C., Venkata Ramana C.;
RL Submitted (AUG-2019) 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:KAA5544573.1}.
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DR EMBL; VWOX01000004; KAA5544573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5M6DB27; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000324479; 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; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 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:KAA5544573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000324479};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:KAA5544573.1}.
FT DOMAIN 11..329
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 362..473
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 476 AA; 51320 MW; E456B5C1D7878477 CRC64;
MPRPSLDQSC TKIVATVGPA CDTPEKLAEL IEAGADVFRI NTAHGKIPDH EQKLAAIREA
SAMTGVHVGV LLDLAGPKIR LGELVNEPLQ CDVGMQLTFI RRGEPKTDHE LTSTYGKLID
ELTVGNRVML ADGMVALEVE SVSADRAVCR VTAAGELRSR QGINLPGVKL SVSAMQRNDL
DNAIWAADHG IDFISLSFVR TAEDVRTLKN VLTAHDCEAL VIAKIEKPEA LANLEQIVDA
ADGIMVARGD LGVEIDVAET PMAQKRIIRV CKEKVKPVIV ATQMLESMHH SPRPTRAEAS
DVANAILDGA DACMLSGETA IGDFPVKTVQ MMSRIMQCTE QSLTHDMTER TVTNRVHPIT
TAVTFAATNI AEAIDASLIV IATKSGGTAW VKSKSRSLIP TLGASDCEET LRRMNLFWGI
KPIAIKKMGH PAEIRTEICR WGKKTGVLKV GDRIVFVSGS GVVEKAHNSV VVHTVD
//
