ID A0A158R7X0_TAEAS Unreviewed; 1111 AA.
AC A0A158R7X0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=TASK_LOCUS4526 {ECO:0000313|EMBL:VDK33570.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000452501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000452501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK33570.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYRS01018353; VDK33570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158R7X0; -.
DR STRING; 60517.A0A158R7X0; -.
DR WBParaSite; TASK_0000452501-mRNA-1; TASK_0000452501-mRNA-1; TASK_0000452501.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; 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; 3.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 2.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 2.
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 PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 3.
DR Pfam; PF02887; PK_C; 2.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 2.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 2.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 2.
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:UP000282613};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 1..308
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 350..483
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 568..763
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 768..866
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 909..1022
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 1111 AA; 122628 MW; 00E94C2B0A2DD3FD CRC64;
MVDAGMNILV INPNMVTRDV CKDVVKCIRE LEESYDRERL IAIAFDVAGA PVRTGTFKEG
MSYEAKLVEG NRVTLTLDEE YKFGCTEELI FIDTQFFPKL IHYLRKGDRI YLDEGQVTLL
VRDVGFDCIN CIVEEGGLLG SFKCLTLSRN RLNQEILRST YVKDLDFAAE CGADFVFTNF
AGSISMIEET RRILPKTTKV FAKIETQESV KNLRELIAVC DGILVCRSGL AMYYTPEKIF
KIQKYIVGHC NVADIPVFVT GQLAESMISK PRPTRAEASD IANAVLDGVD GLLLTIETSW
GMYPFDTVNV VDNICREAER AICHEISRAE LNYCRLLRGQ VNDSIKNVTG ASAVEAADSC
SASAIFVITT TGASAISIAM SRPSCIVIAI TVDIAVARYC LAYRGLHPYL YVGEGVFCCL
LDIAWRHRHV GCERVTEWCE DVDNRINAAI EHTRHTGLVK GGDRIIVVTG SVSTSGSTNT
IHIFTLEGEH SKLRIVGSSH ELSQVGSPWS MENTAVAFPF PSAVGASRTR QAHGAGPRYS
VMLSRARPLS HLQHTCNLDV DQVADNVRQT TIVCTLGKSW KTKEGILKMM DAGMNIMLIN
LSMTPRDICK EVIKYAREIE KESNYSRPLG IAMDMTAAPV RTGIFEGGPS YEANLKEGSR
VTLTLDDNYK FKCTPEIIFI NTKYFPQLIQ CLRKGDRVYL DDGQVSLIVK DVELDCVNCM
VEEGGIIGSY KRVTLPRDRL YQESVQLNYI KDLKFAAECG VGFDPFTICS LHDLIAASDG
LVIRRSDLAM QYTPEKIFKL QKYIVAHCNI AEKPVFIIEQ LLESMVSKPR PTRAESSDIA
NAVLDGADGL VLTMETSWGM YALDSVRVVD NICREAERAV FHFETRGELK QCRMQMEQNS
FDIRSVTGAS AAEAAASCNA TAIFVITTTG LSATSIAMLR PPCSVIAITL DVSVARHCLA
YRGLHGFVFT GKSEGDWAVD IDNRINAAIE HARSTGLVKG GDRIIVVTGS VATSGSTNTM
QIFTLEEEHS KLRIVGSANE VAAATAHKGL LNLADSSMGQ QQHQQKDEEV IDELEEIRLI
QGARSRRPRF SVMLSSNKRG FGGINDIRVP L
//
