ID M6YI77_9LEPT Unreviewed; 486 AA.
AC M6YI77;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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_1 {ECO:0000313|EMBL:EMO89329.1};
GN ORFNames=LEP1GSC024_2003 {ECO:0000313|EMBL:EMO89329.1};
OS Leptospira noguchii str. 2001034031.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193053 {ECO:0000313|EMBL:EMO89329.1, ECO:0000313|Proteomes:UP000012138};
RN [1] {ECO:0000313|EMBL:EMO89329.1, ECO:0000313|Proteomes:UP000012138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2001034031 {ECO:0000313|EMBL:EMO89329.1,
RC ECO:0000313|Proteomes:UP000012138};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Whelen A.C., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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:EMO89329.1}.
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DR EMBL; AKXB02000098; EMO89329.1; -; Genomic_DNA.
DR RefSeq; WP_004445967.1; NZ_AKXB02000098.1.
DR AlphaFoldDB; M6YI77; -.
DR GeneID; 23201870; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000012138; 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:EMO89329.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EMO89329.1}.
FT DOMAIN 9..331
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 360..471
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 486 AA; 54047 MW; 075B33127B65CED5 CRC64;
MKSESSVFRK TKIICTIGPA TSDKKMIQAL AEAGMNVARL NMSHGNHDFH RSIIRNIKSL
NKDVLKNPIA ILLDTQGPEI RTGDLQVDHL DLKVGETFTF HIIPGEESEE QSVFVNYKDI
VKDLKVGDPV TVDNGLINLV VEEINDSALK CKVLDGGRLG SRKHINLPGI RVNLPSITPK
DHKDILFGLE EDVDFIALSF VRSAEDINQL KQIIEENDGH AQIIAKIEDQ EAVRNMKEIV
EAADGVMVAR GDLGVEVPIE ELPILQRAII KECALKGKRV IVATHLLESM IHNPSPTRAE
VTDVANAIYE EADAIMLSGE TAAGKFPVRC VEMMDKIAQR VEKTGGVDYV KDKIPQDKKE
QMARAAAKLA DSLKCPAIIV ITRRGTTALN VAGFHPHYPL IYAFTNMTTV RRKLWLTRGV
IPHRIDFSKD PEKTIRLAIE TLKKTGRIED GDQVVILSDI IAGEDRVETI QIREVKTYFN
SEVEKL
//
