ID A0A0R3SGD8_HYMDI Unreviewed; 595 AA.
AC A0A0R3SGD8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 39.
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=HDID_LOCUS3959 {ECO:0000313|EMBL:VDL41616.1},
GN WMSIL1_LOCUS1743 {ECO:0000313|EMBL:VUZ40742.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000396101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0000396101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL41616.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VUZ40742.1, ECO:0000313|Proteomes:UP000321570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS-il1 {ECO:0000313|EMBL:VUZ40742.1,
RC ECO:0000313|Proteomes:UP000321570};
RA Jastrzebski P J., Paukszto L., Jastrzebski P J.;
RL Submitted (JUL-2019) 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; UYSG01001346; VDL41616.1; -; Genomic_DNA.
DR EMBL; CABIJS010000044; VUZ40742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3SGD8; -.
DR STRING; 6216.A0A0R3SGD8; -.
DR WBParaSite; HDID_0000396101-mRNA-1; HDID_0000396101-mRNA-1; HDID_0000396101.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; Unassembled WGS sequence.
DR Proteomes; UP000321570; 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:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 46..374
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 416..530
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT REGION 544..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 65250 MW; C8CC03EDD951C427 CRC64;
MPTLIPLVTA SNQNKDVCAG RFMSKSSSHL SFMSQLDIDQ VANNARRTSI GCTLGKSWSG
SEDLEKMIKV GMNILVINPA ILPVDTYKDV VKSIREIEED SDYGFIVAVA VDMIGAHVRT
GSFSKGLSHE VNLEEGTRVT LTLDENYRNN CTKDMIFIDT ESFPKLIHCL RKGDRIFLDE
GQISLYIRDI GFDCINCIVE EGGLLGSFKR VCPPKNRLNQ ETVQASFMTE LKFASDIKAD
FVLVNLIENA AMIQEARMHL PKNTKVFAKL ENQESIKNLR EIIEASDGVV ICRSSLAMYY
NPEKIFKLQK HIIGHCNVAE KPVFLTGQLI ESMTSKPMPT RAEASDIANA VLDGADGLIL
TIETSWGSFP SETVDVVDNI CREAERAIWY DISRSELNDM RIMRGLVNNS IKNVTGASAV
EAAGSCGASA IFIVTSTGLS AMSLAMSRPP CIVIGIMADI NVARYCLAFR GLHPYLFTGE
KAAEWSEDID NRINAGIEYA RKTGLVKTGD RIVVVTGSVA TSGSTNTIHI FTLEDDRGKL
RIVGSPNESA STDKPGEGPQ DNLPPTEPSR RHKYSVMLVR SHSAFGSVTD ILSPV
//
