ID C6LV41_GIAIB Unreviewed; 652 AA.
AC C6LV41;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
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=GL50581_2643 {ECO:0000313|EMBL:EET00128.1};
OS Giardia intestinalis (strain ATCC 50581 / GS clone H7) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=598745 {ECO:0000313|EMBL:EET00128.1, ECO:0000313|Proteomes:UP000002488};
RN [1] {ECO:0000313|EMBL:EET00128.1, ECO:0000313|Proteomes:UP000002488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50581 / GS clone H7 {ECO:0000313|Proteomes:UP000002488};
RX PubMed=19696920; DOI=10.1371/journal.ppat.1000560;
RA Franzen O., Jerlstrom-Hultqvist J., Castro E., Sherwood E., Ankarklev J.,
RA Reiner D.S., Palm D., Andersson J.O., Andersson B., Svard S.G.;
RT "Draft genome sequencing of giardia intestinalis assemblage B isolate GS:
RT is human giardiasis caused by two different species?";
RL PLoS Pathog. 5:E1000560-E1000560(2009).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EET00128.1}.
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DR EMBL; ACGJ01002351; EET00128.1; -; Genomic_DNA.
DR AlphaFoldDB; C6LV41; -.
DR EnsemblProtists; EET00128; EET00128; GL50581_2643.
DR VEuPathDB; GiardiaDB:GL50581_2643; -.
DR OMA; MACFEVI; -.
DR OrthoDB; 5473234at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002488; 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 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:EET00128.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 38..372
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 416..517
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT REGION 560..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 70489 MW; 54DA39E7FD9B9370 CRC64;
MFSDAVQRRQ ASGIVATLVA DDLIRSPMTP KPGDSRYRRA KVIASLGPSC NTEGSIAQMI
RHGADAFRIV MAKASSEENI RLYNLVRKCA ADQRKHVSII ASLQGPKFRV TRFRNSTNSI
TVQEGSEISI MFSRAAECDV PNAVFVNESE IFTVIEIGDE VVFKNGPLIA KVTHVSPDKT
NVKAVVTTRG STKLYGGSSL RIPSKLSSIA PLTSLEYEHL HLLAEKMPVD WICYSHINTE
ADIKHIENYT DFLSKKYPDF RPMLMTKVET PLAVLNLKQI VTHVDGIMIA RGALGDEMDF
SYLPSIQKSI IQISRDSGKM CYVATNVCES MSENVIPTRA EVSDVTNCLG DGCDGFVLCA
ETSTGHHSVA AVKYLVEIIV AVENDPLDVS YKSKVLFSGT TRKQPLKTDS QHRLPDSISV
SAISLASILD AKCICIFSIH GGGLIRLMRQ RPTVPVIVMT AAESTARWMN LLWGVTANVC
HRFTDIEDAT KVCDEYVIKN GIAASGDDIV VIFGSFLISS TDHSVNTIGT VRRGSNHVMA
HVVKGADGMK KATVAPVVAP PIPTGQVESA ASPKTDRQDR SLHSRELPQQ PAKSSPTSQT
AVPPYARQVG GLDQPKTAGA SVHQPPGTSP GAILRTNRIS VPPGSSSPAV TN
//
