ID A0A182H1Q2_AEDAL Unreviewed; 960 AA.
AC A0A182H1Q2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=RP20_CCG019953 {ECO:0000313|EMBL:KXJ81422.1};
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160 {ECO:0000313|EnsemblMetazoa:AALF019953-PA.1, ECO:0000313|Proteomes:UP000069940};
RN [1] {ECO:0000313|EMBL:KXJ81422.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ81422.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ81422.1};
RX PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA Yan G., Tu Z.J., Fang X., James A.A.;
RT "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT insights into its biology, genetics, and evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN [2] {ECO:0000313|EMBL:KXJ81422.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ81422.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ81422.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:AALF019953-PA.1}
RP IDENTIFICATION.
RC STRAIN=Foshan {ECO:0000313|EnsemblMetazoa:AALF019953-PA.1};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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 class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01026}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01026}.
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DR EMBL; JXUM01023189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JXUM01023190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KQ560654; KXJ81422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182H1Q2; -.
DR STRING; 7160.A0A182H1Q2; -.
DR EnsemblMetazoa; AALF019953-RA; AALF019953-PA; AALF019953.
DR VEuPathDB; VectorBase:AALC636_015359; -.
DR VEuPathDB; VectorBase:AALC636_030964; -.
DR VEuPathDB; VectorBase:AALF019953; -.
DR VEuPathDB; VectorBase:AALFPA_065890; -.
DR VEuPathDB; VectorBase:AALFPA_075429; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000069940; Unplaced.
DR Proteomes; UP000249989; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00288; Pyruvate_Kinase; 1.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001737; KsgA/Erm.
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; IPR018209; Pyrv_Knase_AS.
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 InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR029063; SAM-dependent_MTases_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 Pfam; PF00398; RrnaAD; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SMART; SM00650; rADc; 1.
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.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000249989};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01026};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01026};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01026}.
FT DOMAIN 550..750
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT REGION 829..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 545
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 593
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 618
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 960 AA; 107187 MW; F7D6304C8D83283C CRC64;
MNPESVSHLE HMCSLDIDSQ TAFVRLSGII CTIGPASVAP EMLEKMMATG MNIARLNFSH
GSHEYHANTI KNIREAVDNY SKKQGKPFPL AIALDTKGPE IRTGLIEGSG TGEVELKKGE
QIQLTTDKDH LEKGSKEKIY VDYVNIVKVV KKGDHVFVDD GLISLVVDSI SGDTLTCTVE
NGGMLGSRKG VNLPGVPVDL PAVSEKDKSD LQFGVEQGVD VIFASFIRNA AALKEIRSIL
GDKGKNIKII SKIENQQGMQ NLDAIIAASD GIMVARGDLG IEIPAEKVFL AQKSMIARCN
RAGKPVICAT QMLESMIKKP RPTRAEISDV ANAIIDGADC VMLSGETAKG EYPLECVLTM
AKTCKEAEAA LWHRNLFNDL VNTTPNPLDT ACSIAIAASE AASKSRAAAV IVITTSGRSA
HLISKYRPRC PIIAVTRFAQ TARQCHLYRG ILPVVYEQQA LEDWLKDVDA RVQYGMDFGK
ERGFLKPGNP VVVVTGWKQG SGFTNTIRIV YVYEEKMIPV CLVRRDACTR ASTVHRTQTT
DRFYVASPER AKEIAKLLTD DLEPDGLLVE VNPGMGLLTK ELLEKTDNLF LYEADERFEP
ELNKLVVPKP KVELRFVDFN GYWRHCYQDS LDQGSRIDKL LAGLPRRSRW KDEEVNFRLF
SVIGSLNFFK SLIHSVATQK GLYGLGRCEM ILAVPPLFFA HLTCRSEFGY KLYRSTSVLF
QIFFEHELIG KIPRKDFLPW PKNPSAKSRI LTQYRRLGLV ENDELFLMRV VPRRNLFDHC
LPDNLKLLSF FVSQNMVSRK NRIIPALERW IPFCGARLIL NQNYVDPSAA PSSPKKHSDS
PSFQYTSSPL RERDFPERMT IFTEFGELTP SQILTLFNEF ISWPEFQQSP FLQTMEQHYN
KHVYGGRRDS AAAEATVATK SGTSPKVVID GEEALEDEEE QLLVEGSDET EPEGTSRSRT
//
