ID V6U352_GIAIN Unreviewed; 555 AA.
AC V6U352;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=GSB_17143 {ECO:0000313|EMBL:ESU45628.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU45628.1, ECO:0000313|Proteomes:UP000018040};
RN [1] {ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GS {ECO:0000313|Proteomes:UP000018040};
RA Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA Nash T.;
RT "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT Pig).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESU45628.1, ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS {ECO:0000313|EMBL:ESU45628.1,
RC ECO:0000313|Proteomes:UP000018040};
RX PubMed=24307482; DOI=10.1093/gbe/evt197;
RA Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA Nash T.E.;
RT "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT Pig).";
RL Genome Biol. Evol. 5:2498-2511(2013).
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:ESU45628.1}.
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DR EMBL; AHHH01000003; ESU45628.1; -; Genomic_DNA.
DR AlphaFoldDB; V6U352; -.
DR EnsemblProtists; ESU45628; ESU45628; GSB_17143.
DR VEuPathDB; GiardiaDB:DHA2_17143; -.
DR VEuPathDB; GiardiaDB:GL50581_3239; -.
DR VEuPathDB; GiardiaDB:GL50803_0017143; -.
DR VEuPathDB; GiardiaDB:QR46_0195; -.
DR eggNOG; KOG2323; Eukaryota.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000018040; 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 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:ESU45628.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 40..370
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 408..511
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 555 AA; 60729 MW; 09F08A192A960909 CRC64;
MATLNNKFTA NQITEYNLTN LKKLVEQGIK STDKNHPHFN RVKICCTLGP SSFNVEVIAG
MIRAGADIIR INFSHGNTDD HTQIFYKVQQ AMQLTGKTVA IMGDIQGPKL RIAGFSNPDN
CIELKEGQEF TLDHNNTNGD ESRVYLPHKE FFAVCEPNDD IILNDGYIRL VATSVDRQAM
KIVTKVKTGG KLGARKGITI PTRILPLSGL SPKDLGDIKN ACRLGMDWIA LSFVQTKADV
IEARDYIAKL HAENPASFCP RVCSKIEKPT AVLDIDDIAL LSDMLMVARG DLAIETCLSK
VCSIQKYICE RARYHGCQAM VATQMVESLI ENTVPTRAEV TDVASVCFDG ANSVLVTAET
AAGHDPVNVV KVLRSILTTT EQSEAFIKQV LTDNYINQRT SKEHKRPDSI ALGACLLARE
LGAKLIIVFS KSGNSTGRVL RQLPHCPVLC ITSEQRSYQW LHMCWGCRPV LHPGNIDSMK
TLISVADTHA LESGQAERGD AVVLVFGTPF SDVNRKGCNN IMAHIVGGGS FNNSADVEYG
VTPQLTELTP IVGDN
//
