ID I3EIL4_NEMP3 Unreviewed; 409 AA.
AC I3EIL4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=NEQG_00880 {ECO:0000313|EMBL:EIJ89061.1};
OS Nematocida parisii (strain ERTm3) (Nematode killer fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX NCBI_TaxID=935791 {ECO:0000313|EMBL:EIJ89061.1, ECO:0000313|Proteomes:UP000002872};
RN [1] {ECO:0000313|EMBL:EIJ89061.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ERTm3 {ECO:0000313|EMBL:EIJ89061.1};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C., Troemel E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Nematocida parisii strain ERTm3.";
RL Submitted (JAN-2011) 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|ARBA:ARBA00001174,
CC ECO:0000256|RuleBase:RU000504};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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; GL870877; EIJ89061.1; -; Genomic_DNA.
DR AlphaFoldDB; I3EIL4; -.
DR STRING; 935791.I3EIL4; -.
DR EnsemblFungi; EIJ89061; EIJ89061; NEQG_00880.
DR VEuPathDB; MicrosporidiaDB:NEQG_00880; -.
DR HOGENOM; CLU_015439_1_1_1; -.
DR InParanoid; I3EIL4; -.
DR OMA; MVRVHHL; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002872; 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 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; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel 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:EIJ89061.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002872};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 7..331
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
SQ SEQUENCE 409 AA; 45114 MW; BDA404F26BB1527A CRC64;
MKKILPTKII CTLGPASSTE EKIRQMFDEG MAIARINLSH ATGEGNSSLI ETINKIRKEP
KYSSLSIAMD TKGPEIRLGE MEEAEVNIAV GDTVILTTDT KYAKCCTKDR MYIDHRNIYN
DLTEDTKCIF IDDGKIELEI VDIFKEKEII STKAKSTGVV SSKKGVNIPG IKLTLPNLTE
NDIKSIQYGI KNGIDLIFAS FIQSAKDIRD IKKILNGNTE IKIIAKIEST QGLANIAEII
DESDGIMIAR GDLGIETDYS NLFYAQCKIS HECRIKNKPF IVATEILESM KKSLKPTRAE
VTDLSFAVIS GAACVMLSGE SAVGVDPVNT VRVMHQIIER SSEAAIFTDV FNDCLVLRNN
TIKVSITNSN AILREKNILF GWSAIDSNIS TDDISAPNGY LIEKITEDE
//
