ID A0A327QP15_9BACT Unreviewed; 495 AA.
AC A0A327QP15;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, 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=LX64_02237 {ECO:0000313|EMBL:RAJ05083.1};
OS Chitinophaga skermanii.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=331697 {ECO:0000313|EMBL:RAJ05083.1, ECO:0000313|Proteomes:UP000249547};
RN [1] {ECO:0000313|EMBL:RAJ05083.1, ECO:0000313|Proteomes:UP000249547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23857 {ECO:0000313|EMBL:RAJ05083.1,
RC ECO:0000313|Proteomes:UP000249547};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
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 -!- 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:RAJ05083.1}.
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DR EMBL; QLLL01000004; RAJ05083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327QP15; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000249547; 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:RAJ05083.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249547};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 26..343
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 379..491
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 495 AA; 55693 MW; F3DC6906F8E0724C CRC64;
MSTKDLSKYY HKQMDNAAGR QHSAGKTKIV ATVGPACDTY EKLLELVQAG VNVFRLNFSH
GSHEDKSRII SYIRQINKTE PYNIAILADL QGPKLRVGEI ENNALPLVAG DLLTFVNEKV
VGTKERIYVS YHDLHKDVKV GQKILLDDGK IETIVREVTP QHEIKAEVLL GGILSSKKGF
NLPETKVNLP ALTEKDEIDL QFIIDNECDW VALSFVRSAK DLIYLRKKLK ERDSKIKVIS
KIEKPEAILN LKEIIWESDG VMIARGDLGV ELPVEQVPMI QKDIIRKCIH RAKPVIVATQ
MMESMIDRTR PNRSEITDVA NAVLEGADAV MLSGETATGQ HPTLVIQTMR KIIAEVEKEE
IIYNRNLIPH RHSPTFLSDA LCYNACKISE DLESDALIGM TQSGYTGFML SSYRPKSPLY
IFTKERTLVN QLSLSWGVRA FYYAEEESLD DIVTDQINIL KERGFLQAKD VVVNTGSTPV
KDHLPTNVIK ITRVD
//
