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Database: UniProt
Entry: A8B498_GIAIC
LinkDB: A8B498_GIAIC
Original site: A8B498_GIAIC 
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}.
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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
//
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