ID A0A090L2B4_STRRB Unreviewed; 536 AA.
AC A0A090L2B4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=SRAE_1000222200 {ECO:0000313|EMBL:CEF63966.1,
GN ECO:0000313|WBParaSite:SRAE_1000222200.1,
GN ECO:0000313|WormBase:SRAE_1000222200};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF63966.1};
RN [1] {ECO:0000313|EMBL:CEF63966.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000222200.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF63966.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000222200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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; LN609528; CEF63966.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090L2B4; -.
DR STRING; 34506.A0A090L2B4; -.
DR EnsemblMetazoa; SRAE_1000222200.1; SRAE_1000222200.1; WBGene00258836.
DR WBParaSite; SRAE_1000222200.1; SRAE_1000222200.1; WBGene00258836.
DR WormBase; SRAE_1000222200; SRP03391; WBGene00258836; -.
DR OMA; ESANGHY; -.
DR OrthoDB; 312683at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000035682; Chromosome X.
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 CDD; cd00288; Pyruvate_Kinase; 1.
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; IPR018209; Pyrv_Knase_AS.
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.
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:CEF63966.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 51..379
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 414..532
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 536 AA; 58234 MW; CDCD4044E4E54FEF CRC64;
MVSVEATAAF LKELETVSYY AKDEKQAVLS KGTFLEHLSS LDITEPPHAV RKTAIICTIG
PKCNNVETLA LMIKNGMNVA RLNFSHGDHE YHAMTIKNVR EAARLVKHES IVAIALDTKG
PEIRTGMIMN SSTAEVELIK GHSIRLTTNP SFEKSGNAVN LYVDYENITR VLSPGKIIYI
DDGLISLIVD EVGDDYVICT IENGGMLGSK KGVNLPGTSV DLPAVSEKDI ADLLFGVEQG
VDIIFASFIR NGSAVSKIRE ILGEKGKNIK IISKIENQEG VLNADEIIKA SDGIMVARGD
LGIEIPAEKV FLAQKLLIAK CNEAGKPVIC ATQMLESMIS KPRPTRAETS DVANAVLDGA
DCVMLSGETA KGSYPIETIK IMHYICKEAE AAVYHSKFFE EILKRVQKPT SHVETIGIAA
VSASKSCQAS AIVLCTTTGN TAAMISKFKP SVPIIAITKN PQTARQLWLY RGVFPIYYSG
VEKHTDWTKD VDMRIREGIN FGKEKGFIEN GDNIIVITGW TSGAGKTNTL RLIIAD
//
