ID Q9U016_GIAIN Unreviewed; 517 AA.
AC Q9U016;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 92.
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};
DE Flags: Fragment;
GN Name=pk {ECO:0000313|EMBL:AAF19604.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:AAF19604.1};
RN [1] {ECO:0000313|EMBL:AAF19604.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB/ATCC30957 {ECO:0000313|EMBL:AAF19604.1};
RA Henze K., Muller M.;
RT "Glycolytic kinases in the amitochondriate protist, Giardia lamblia.";
RL Submitted (MAY-1999) 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; AF150875; AAF19604.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9U016; -.
DR VEuPathDB; GiardiaDB:DHA2_3206; -.
DR VEuPathDB; GiardiaDB:GL50581_2643; -.
DR VEuPathDB; GiardiaDB:GL50803_003206; -.
DR VEuPathDB; GiardiaDB:QR46_2469; -.
DR UniPathway; UPA00109; UER00188.
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 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, ECO:0000313|EMBL:AAF19604.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AAF19604.1}.
FT DOMAIN 38..372
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 416..493
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT NON_TER 517
FT /evidence="ECO:0000313|EMBL:AAF19604.1"
SQ SEQUENCE 517 AA; 57407 MW; 0B90DCF48B0D2F65 CRC64;
MFSDAVQRRQ ASGIVANLVA DDLIRSPMTP KPGDSRYRRA KVIASLGPSC NTEGSIAQMI
RHGADAFRIV MAKASNEENI RLYNLVRKCA ADQKKHISII ASLQGPKFRV TRFRNTTNSI
TLQEGSELNI MFNKAMECDA PNTVFVNESE IFTVIEVGDE VVFKNGPLIA KVTSVSPDKT
NVKAVVTTRG STKLYGGSSL RIPSKLSSIA PLTSLEYEHL HLLAEKMPVD WICYSHINTE
SDIKHIENYT DFLSKKYPDF RPMLMTKVET PLAVLNLKQI VTHVDGIMIA RGALGDEMDF
SYLPSIQKSI IQIARDSGKM CYIATNVCES MSENVIPTRA EVSDVTNCLG DGCDGFVLCA
ETSTGHHSVA TVKYLVEIIV AVENDPLDVS YRSKVLFSGT TRKQPLKTDS QHRLPDSISV
SAISLASILD AKCICIFSIH GGGLIRLMRQ RPTVPVVVMT AAESTARWMN LLWGVTVNVC
HRFTDIEDAT KVCDEYVQER HCSLWRRHRR HLRVVPS
//
