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Database: UniProt
Entry: A0A2I0WBX0_9ASPA
LinkDB: A0A2I0WBX0_9ASPA
Original site: A0A2I0WBX0_9ASPA 
ID   A0A2I0WBX0_9ASPA        Unreviewed;       750 AA.
AC   A0A2I0WBX0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE            EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN   Name=PKP4 {ECO:0000313|EMBL:PKU73149.1};
GN   ORFNames=MA16_Dca026942 {ECO:0000313|EMBL:PKU73149.1};
OS   Dendrobium catenatum.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX   NCBI_TaxID=906689 {ECO:0000313|EMBL:PKU73149.1, ECO:0000313|Proteomes:UP000233837};
RN   [1] {ECO:0000313|EMBL:PKU73149.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU73149.1};
RX   PubMed=26754549; DOI=10.1038/srep19029;
RA   Zhang G.Q., Xu Q., Bian C., Tsai W.C., Yeh C.M., Liu K.W., Yoshida K.,
RA   Zhang L.S., Chang S.B., Chen F., Shi Y., Su Y.Y., Zhang Y.Q., Chen L.J.,
RA   Yin Y., Lin M., Huang H., Deng H., Wang Z.W., Zhu S.L., Zhao X., Deng C.,
RA   Niu S.C., Huang J., Wang M., Liu G.H., Yang H.J., Xiao X.J., Hsiao Y.Y.,
RA   Wu W.L., Chen Y.Y., Mitsuda N., Ohme-Takagi M., Luo Y.B., Van de Peer Y.,
RA   Liu Z.J.;
RT   "The Dendrobium catenatum Lindl. genome sequence provides insights into
RT   polysaccharide synthase, floral development and adaptive evolution.";
RL   Sci. Rep. 6:19029-19029(2016).
RN   [2] {ECO:0000313|EMBL:PKU73149.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU73149.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
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   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663}.
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DR   EMBL; KZ502775; PKU73149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0WBX0; -.
DR   STRING; 906689.A0A2I0WBX0; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000233837; 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; 2.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 2.
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; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   PANTHER; PTHR11817:SF76; PLASTIDIAL PYRUVATE KINASE 4, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 2.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PKU73149.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:PKU73149.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233837};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          281..366
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          507..726
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
SQ   SEQUENCE   750 AA;  83663 MW;  EDA5C22F4024E643 CRC64;
     MHHEQGTLWG FLDIGIKMAT FTMSKLLSLL LILQKNGEEM LLCDRKECRQ RSHVQFPIKS
     IKKYPILLAK LPEEDDPECN SWKMYAFHDT LNAVNRTLAM NLNEGNAYAQ PDKSGRGSVE
     VSELIPSYGH CLPELPTNRL LSLLEKLKAV HLHLLAAEHW NASHLRLCHR NYVVSATNLT
     HYLALKCLHL QQLQEDLSSI GLLTLEFINS HVLASIGTSI QLLHHLLSNS LESKDSATYL
     DRNGYSPTER SENAVNFAIS TMKKRVSVHN TALFGECLDK RTGQIMVTIG KEVVKDEILV
     KNLLKAGTNV IRINCAHDDP NVWREIIRIV KHNSHLLEKP CRILMDLAGP KLRTVLLRTH
     SNMVKLSPKK DSSGNVVFPA QVWLCFDGSN PPAGLSTNAI IWIQKSFFNK LKMGDYVSFV
     DVRGRKRVLK VLKKSILSTE YGCIAECLQT AYIKVDTELS VKKKKGEFVG RVIKVLANQH
     FVRLKVGDLL TIFRSSSSYL NELSSTTLGS TKITCSSDHI FESVEQGEPI LFDDGKILGK
     VREVNANWAT VVVTHARPKG SKLGSGKSIN IPKSRVQLKG LTPKDLLDLD FVGSNADMVG
     ISFIRNVDDI VIVQHELEKR NLTKLGIVLK IETKDSLQRL PSLLFQAMQT SNPLGVMIAR
     GDLMVECGWD QLGEIQEEIL SICSAAHIPV IWATQVLESL VKFGFPTRAE ITDVFKAMGA
     SCIMLNKGDN IVQAVTALNS LLSNRSSSER
//
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