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Database: UniProt
Entry: A0A0T6BBN4_9SCAR
LinkDB: A0A0T6BBN4_9SCAR
Original site: A0A0T6BBN4_9SCAR 
ID   A0A0T6BBN4_9SCAR        Unreviewed;       522 AA.
AC   A0A0T6BBN4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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};
DE   Flags: Fragment;
GN   ORFNames=AMK59_2610 {ECO:0000313|EMBL:KRT84760.1};
OS   Oryctes borbonicus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC   Scarabaeidae; Dynastinae; Oryctes.
OX   NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT84760.1, ECO:0000313|Proteomes:UP000051574};
RN   [1] {ECO:0000313|EMBL:KRT84760.1, ECO:0000313|Proteomes:UP000051574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB123 {ECO:0000313|EMBL:KRT84760.1};
RC   TISSUE=Whole animal {ECO:0000313|EMBL:KRT84760.1};
RA   Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA   Roedelsperger C.;
RT   "Draft genome of the scarab beetle Oryctes borbonicus.";
RL   Submitted (SEP-2015) 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:KRT84760.1}.
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DR   EMBL; LJIG01002180; KRT84760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6BBN4; -.
DR   OrthoDB; 312683at2759; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000051574; 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; 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   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.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051574};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          30..359
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          393..495
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRT84760.1"
SQ   SEQUENCE   522 AA;  57186 MW;  E68F06549334EF94 CRC64;
     RMEFGDSSNH LRQQANLNIH LEKNKLCLSG IVCTIGPAST NANILLDMMK SGMSVARLNF
     SHGSQSEHTD RIKVIRKALE LYKTASNETY PLAIGLDTKG PEIRTGNIMQ GSQSKVEIQA
     GTYVRLTTDP RYKTMSTNRI IYVDYQRLPQ VIKVGDTVYI DDGKIILNCT QIQTDIIECK
     VINGGMLGSK KGVNLPGFKL GLPAVSEQDK EDLSWGIRNN IDMVFASFIH TAGDVRDIRN
     ALGPLGKDIW VIAKIETQEA VDNIEQIIEA SDGIMIARGD LALQIPIEKV FLAQKSIIAK
     CNLRGKPVIC ATQMLESMLD NQRPSRPDVS DISNAILDGA DCVMLSGETA VGKYPVECVK
     TMTKICKEAE AAVWNGRLLQ EMLANSSSLD ERNAISAASV VTATLCKASA IILSSGSSVE
     LSELISKYKP RCPILAVTKD INFAEKIGLF RGVHPIISET GTFSTGLEAQ QLLQNVLGYV
     KSKGFVNNGD RVLFLRKGIK VSKSYKDRFL LEVLTVTDLN EK
//
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