ID E4PTP0_MYCLG Unreviewed; 478 AA.
AC E4PTP0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:ADR23841.1};
GN OrderedLocusNames=MSB_A0269 {ECO:0000313|EMBL:ADR23841.1};
OS Mycoplasma leachii (strain DSM 21131 / NCTC 10133 / N29 / PG50).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=880447 {ECO:0000313|EMBL:ADR23841.1, ECO:0000313|Proteomes:UP000008712};
RN [1] {ECO:0000313|Proteomes:UP000008712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21131 / NCTC 10133 / N29 / PG50
RC {ECO:0000313|Proteomes:UP000008712};
RA Wise K., Calcutt M.J., Foecking M.F., Madupu R., DeBoy R.T., Roske K.,
RA Martin T.R., Hvinden M.L., Durkin A.S., Glass J., Methe B.A.;
RT "Genome sequence of Mycoplasma leachii PG50 MU clone A8.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADR23841.1, ECO:0000313|Proteomes:UP000008712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21131 / NCTC 10133 / N29 / PG50
RC {ECO:0000313|Proteomes:UP000008712};
RX PubMed=22843585; DOI=10.1128/JB.00761-12;
RA Wise K.S., Calcutt M.J., Foecking M.F., Madupu R., Deboy R.T., Roske K.,
RA Hvinden M.L., Martin T.R., Durkin A.S., Glass J.I., Methe B.A.;
RT "Complete Genome Sequences of Mycoplasma leachii Strain PG50T and the
RT Pathogenic Mycoplasma mycoides subsp. mycoides Small Colony Biotype Strain
RT Gladysdale.";
RL J. Bacteriol. 194:4448-4449(2012).
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}.
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DR EMBL; CP002108; ADR23841.1; -; Genomic_DNA.
DR RefSeq; WP_013447580.1; NC_014751.1.
DR AlphaFoldDB; E4PTP0; -.
DR KEGG; mlc:MSB_A0269; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_1_14; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000008712; Chromosome.
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:ADR23841.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:ADR23841.1}.
FT DOMAIN 10..336
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 374..472
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 478 AA; 53573 MW; D49B6ED6CB08A0C2 CRC64;
MTKETLQKRM KRTKVITTIG PSTHSAEAIK ELFSNGMTTI RLNFSHGSYE EHGYRIKAAK
KISKALNKPI SIMLDTKGPE IRLGKFKDNK QEVVKGQAIT IYTDSYSYLN KECVQGEMTV
AYDMSVDLKP GDMILIDDGK LELTVDSVEP QIIKATAFNH HIVKTNKRVN LPGIDFSLPF
LSEKDEKDIL FGCEQGVDYI AASFVNTAEN VRQIKEILTK ANANHIQIIS KIESQVGLDN
IDEIIEESDG IMIARGDLGL EIPYYDVPYW EKIIIRKCRE KGKIVIVATQ MLETMTENPS
PTRAEVTDVY YATELGADAT MLSGESAAGD YPFLTVHTMS TINKRAEVEF YNKIYYQVQL
DNARNSTSGP RAEIADLLAT KTKDGEYKYA IVLSKTGELL KTISKFRPNV TILGVSPDKK
LWTSFGVWHS IFMNKVDTLD NLDNNVEKLS EIAKSWGAKL GEKVLVVRST AIKEIEVI
//
