ID A8B498_GIAIC Unreviewed; 553 AA.
AC A8B498;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 24-JAN-2024, entry version 97.
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=GL50803_0017143 {ECO:0000313|EMBL:KAE8303640.1},
GN GL50803_17143 {ECO:0000313|EMBL:EDO81855.1};
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922 {ECO:0000313|EMBL:EDO81855.1};
RN [1] {ECO:0000313|EMBL:EDO81855.1, ECO:0000313|Proteomes:UP000001548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000313|Proteomes:UP000001548},
RC and WB C6 {ECO:0000313|EMBL:EDO81855.1};
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
RN [2] {ECO:0000313|EMBL:KAE8303640.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB C6 {ECO:0000313|EMBL:KAE8303640.1};
RA Xu F., Jex A., Svard S.G.;
RT "New Giardia intestinalis WB genome in near-complete chromosomes.";
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}.
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:EDO81855.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACB02000002; EDO81855.1; -; Genomic_DNA.
DR EMBL; AACB03000002; KAE8303640.1; -; Genomic_DNA.
DR RefSeq; XP_001709529.1; XM_001709477.1.
DR AlphaFoldDB; A8B498; -.
DR SMR; A8B498; -.
DR STRING; 184922.A8B498; -.
DR EnsemblProtists; EDO81855; EDO81855; GL50803_17143.
DR GeneID; 5702453; -.
DR KEGG; gla:GL50803_0017143; -.
DR VEuPathDB; GiardiaDB:GL50803_17143; -.
DR HOGENOM; CLU_015439_8_2_1; -.
DR InParanoid; A8B498; -.
DR OMA; MAVTRCE; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001548; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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, ECO:0000313|EMBL:EDO81855.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001548};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EDO81855.1}.
FT DOMAIN 38..368
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 406..509
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 553 AA; 60525 MW; 6997CB75C898443A CRC64;
MLNNKFTANQ ITEYNLTNLK KLVEQGLKGV DKNHPHFNRV KICCTLGPSS FNVEVIAGMI
RAGADIIRIN FSHGNTDDHT QIFHKVQQAM QLTGKTVAIM GDIQGPKLRI AGFSNPDNCI
ELKEGQEFTL DHNNVNGDES RVYLPHKEFF AVCEPNDDII LNDGYIRLVA TSVDRQAMRI
VTRVKTGGKL GARKGITIPT RILPLSGLSP KDLGDIRNAC RLGMDWIALS FVQTKADVIE
ARDYIAKLHA ENPASFCPRV CSKIEKPTAV LDIDDIALLS DMLMVARGDL AIETCLSKVC
SIQKYICERA RYHGCQAMVA TQMVESLIEN TVPTRAEVTD VASVCFDGAN SVLVTAETAA
GHDPVNVVKV LRSILTTTEQ SEAFIKQVLT DNYINQRTSK EHKRPDSIAL GACLLARELG
AKLIIVFSKS GNSTGRVLRQ LPHCPVLCIT SEQRSYQWLH MCWGCRPVLH PGNIDSMKTL
ISVADTHALE SGQAERGDAV VLVFGTPFSD VNRKGCNNIM AHVVGGGSFN NSTDVEYGVT
PQLAELTPVV GDS
//
