ID A0A562BTW6_9BURK Unreviewed; 497 AA.
AC A0A562BTW6;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ORFNames=L602_001400000880 {ECO:0000313|EMBL:TWG88173.1};
OS Cupriavidus gilardii J11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=936133 {ECO:0000313|EMBL:TWG88173.1, ECO:0000313|Proteomes:UP000318141};
RN [1] {ECO:0000313|EMBL:TWG88173.1, ECO:0000313|Proteomes:UP000318141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J11 {ECO:0000313|EMBL:TWG88173.1,
RC ECO:0000313|Proteomes:UP000318141};
RA Gladden J.;
RT "Genome sequencing of lignin-degrading bacterial isolates.";
RL Submitted (JUL-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 -!- 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:TWG88173.1}.
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DR EMBL; VLJN01000006; TWG88173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A562BTW6; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000318141; 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; 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.
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:TWG88173.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000318141};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 5..322
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 355..467
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 497 AA; 52759 MW; DC6904AA456FC9BD CRC64;
MRRQRKAKIV ATLGPASSDI ATIRQLFEAG ADVFRLNFSH GTHDDHRQRH EAVRRVEAEV
KRPIAVLADL QGPKLRIGTF AAGKVALAAG DRFVLDSDPT PGDGRRVHLP HPELFEVAAP
GQSLLIDDGK VRLHIESVSR GSIVTRAVNH GTLSDRKGVN VPDAVVPIPA LTAKDRRDLD
FALSLDVDWI ALSFVQRPAD IVAARELIGT RASVLSKIEK PAALQQLEEI VRVSDAVMVA
RGDLGVELPP ERVPGVQKRI LRVCRQLGKP VVIATQMLES MIDSPVPTRA EASDVASAIY
DGADAVMLSA ESANGRHPVG AVAMMDRIVT EVERDPLYRN LLDAQHETPL STRQDAICAA
LREVTQIIGA AATVAYTSSG ATALRAARER PRAPILSITP HLAIARRLAM AWGVHSTVSP
DVRSVDEMVD AATGAALAEG FAVPGDQITI AAGMPFGQGG TTNLLRVAEI AGTAKPMSVR
SGAGTAPADV VQQAVGA
//
