ID A0A0J1BS42_9MICC Unreviewed; 492 AA.
AC A0A0J1BS42;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=ABL57_13280 {ECO:0000313|EMBL:KLU09255.1};
OS Kocuria sp. SM24M-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1660349 {ECO:0000313|EMBL:KLU09255.1, ECO:0000313|Proteomes:UP000036489};
RN [1] {ECO:0000313|EMBL:KLU09255.1, ECO:0000313|Proteomes:UP000036489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM24M-10 {ECO:0000313|EMBL:KLU09255.1,
RC ECO:0000313|Proteomes:UP000036489};
RA Palermo B.R., Castro D.B., Cauz A.C., Magalhaes B.L., Carlos C.,
RA Costa F.L., Scagion G.P., Higac J.H., Pereira L.B., Almeida L.D.,
RA Neves M.S., Cordeiro M.A., Prado P.F., Silva T.M., Balsalobre T.W.,
RA Paulino L.C., Vicentini R., Ferraz L.F., Ottoboni L.M.;
RT "Draft genome sequence of Kocuria sp. SM24M-10 isolated from coral mucus.";
RL Submitted (MAY-2015) 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:KLU09255.1}.
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DR EMBL; LDNX01000118; KLU09255.1; -; Genomic_DNA.
DR RefSeq; WP_047803957.1; NZ_LDNX01000118.1.
DR AlphaFoldDB; A0A0J1BS42; -.
DR PATRIC; fig|1660349.3.peg.502; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000036489; 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:KLU09255.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:KLU09255.1}.
FT DOMAIN 1..322
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 353..465
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 492 AA; 53022 MW; 23A301F5BB867F4E CRC64;
MRRAKIVATI GPAISSYENL SQAIRSGMNV ARLNMSHGDH SVHDASYENL RRASEDLGQT
VAILADLQGP KIRLGRFADG PHELLPGDEF SITVEDVEGT AELCSTTHKG LPGDVNVGDP
LLIDDGRVAL RATAVSDTTV TAEVVVGGPV SNNKGINLPG VAVNVPALSD KDEDDLRWAL
RRGVDLIALS FVRDAKDIVR VHEIMDEEGR RLPVIAKIEK PQAVDSLHEI IDAFDGIMVA
RGDLGVELPL EQVPIVQKRA IELARRWAKP VIVATQVLES MIDSPRPTRA EASDCANAVL
DGADAVMLSG ETSVGKYPIE TIQTMARIIE ATESQALERV PALGTEPRTR GGAVTRAAVT
IARQLDVSYI CTFTQSGDSA RRLSRLRPPH PILAFTPEPL VTALMSLLWG VQPIQVAKVD
HTDDMTRQVD LHLQEQGLAG EDDLVVICAG SPPGVAGTTN LVKVHRVGDV KDAGELLSGQ
RRRERVGPWR ES
//
