ID A8BW44_GIAIC Unreviewed; 654 AA.
AC A8BW44;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-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};
GN ORFNames=GL50803_003206 {ECO:0000313|EMBL:KAE8302816.1}, GL50803_3206
GN {ECO:0000313|EMBL:EDO76844.1};
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:EDO76844.1};
RN [1] {ECO:0000313|EMBL:EDO76844.1, 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:EDO76844.1};
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:KAE8302816.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB C6 {ECO:0000313|EMBL:KAE8302816.1};
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:EDO76844.1}.
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DR EMBL; AACB02000054; EDO76844.1; -; Genomic_DNA.
DR EMBL; AACB03000003; KAE8302816.1; -; Genomic_DNA.
DR RefSeq; XP_001704518.1; XM_001704466.1.
DR AlphaFoldDB; A8BW44; -.
DR STRING; 184922.A8BW44; -.
DR EnsemblProtists; EDO76844; EDO76844; GL50803_3206.
DR GeneID; 5697391; -.
DR KEGG; gla:GL50803_003206; -.
DR VEuPathDB; GiardiaDB:GL50803_3206; -.
DR HOGENOM; CLU_015439_8_2_1; -.
DR InParanoid; A8BW44; -.
DR OMA; ESANGHY; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001548; Chromosome 3.
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 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:EDO76844.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001548};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EDO76844.1}.
FT DOMAIN 38..372
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 416..516
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT REGION 557..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 70738 MW; 56F2BDE89FD834A0 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 KVCDEYVIKN GIAASGDDIV VIFGSFLVSS TEHPVNTIGT VRRGSNHVMA
HVVKGVDGLK KAVPTPAPII APPIPTGPVE SATSPKADRQ DRSSRSREAS QPQVRSSPPS
QTVASPHARQ VGGSEQPKSG GPSAHLPSGT SPGAILRTNR IAVPPGSSSP AVTN
//
