PPDK2_MAIZE
ID PPDK2_MAIZE Reviewed; 883 AA.
AC Q42368; K7UZT6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pyruvate, phosphate dikinase 2 {ECO:0000303|PubMed:1668653};
DE EC=2.7.9.1;
DE AltName: Full=Pyruvate, orthophosphate dikinase 2;
GN Name=PPDK2 {ECO:0000303|PubMed:1668653};
GN Synonyms=CYPPDKZM2 {ECO:0000303|PubMed:1668653};
GN ORFNames=ZEAMMB73_872355 {ECO:0000312|EMBL:AFW81976.1}, Zm.19608;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Maize Genome Sequencing Project;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-90, AND TISSUE SPECIFICITY.
RX PubMed=1668653; DOI=10.2307/3869364;
RA Sheen J.;
RT "Molecular mechanisms underlying the differential expression of maize
RT pyruvate, orthophosphate dikinase genes.";
RL Plant Cell 3:225-245(1991).
RN [4]
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=24710069; DOI=10.1104/pp.113.231993;
RA Chen Y.B., Lu T.C., Wang H.X., Shen J., Bu T.T., Chao Q., Gao Z.F.,
RA Zhu X.G., Wang Y.F., Wang B.C.;
RT "Posttranslational modification of maize chloroplast pyruvate
RT orthophosphate dikinase reveals the precise regulatory mechanism of its
RT enzymatic activity.";
RL Plant Physiol. 165:534-549(2014).
CC -!- FUNCTION: Formation of phosphoenolpyruvate, which is the primary
CC acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P11155};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots and stems.
CC {ECO:0000269|PubMed:1668653}.
CC -!- MISCELLANEOUS: PubMed:1668653 shows the existence of a second gene
CC coding for both cytoplasmic and chloroplastic isoforms of PPDK.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; FJ935750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ935778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000784; AFW81976.1; -; Genomic_DNA.
DR EMBL; S46967; AAB23732.1; -; Genomic_DNA.
DR PIR; PQ0191; PQ0191.
DR RefSeq; XP_008656296.1; XM_008658074.1.
DR AlphaFoldDB; Q42368; -.
DR SMR; Q42368; -.
DR STRING; 4577.GRMZM2G097457_P01; -.
DR PaxDb; Q42368; -.
DR PRIDE; Q42368; -.
DR EnsemblPlants; Zm00001eb349810_T002; Zm00001eb349810_P002; Zm00001eb349810.
DR Gramene; Zm00001eb349810_T002; Zm00001eb349810_P002; Zm00001eb349810.
DR eggNOG; ENOG502QREJ; Eukaryota.
DR HOGENOM; CLU_015345_0_2_1; -.
DR BRENDA; 2.7.9.1; 6752.
DR Proteomes; UP000007305; Chromosome 8.
DR ExpressionAtlas; Q42368; baseline and differential.
DR Genevisible; Q42368; ZM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR22931; PTHR22931; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 3.
DR PIRSF; PIRSF000853; PPDK; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01828; pyru_phos_dikin; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Photosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:24710069"
FT CHAIN 2..883
FT /note="Pyruvate, phosphate dikinase 2"
FT /id="PRO_0000343516"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT ACT_SITE 843
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 571
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 628
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 757
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 757
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 778
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 779
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 780
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 781
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 781
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
SQ SEQUENCE 883 AA; 96076 MW; 43FBA34A30B31649 CRC64;
MAPAPCGRSS QRVFHFGKGK SEGNKNMKEL LGGKGANLAE MASIGLSVPP GFTVSTEACQ
QYQEAGRALP PGLWAEVLDG LRWVEEYMGA ALGDPRRPLL LSVRSGAAVS MPGMMDTVLN
LGLNDQVAAG LAAKSGDRFA YDSFRRFLDM FGNVVMDIPH ALFEEKLEAM KKAKGLKNDT
DLTATDLKEL VSQYKNVYVE AKGEPFPSDP KRQLELAVLA VFDSWESPRA KKYRSINQIT
GLRGTAVNVQ CMVFGNMGNT SGTGVLFTRN PNTGEKKLYG EFLVNAQGED VVAGIRTPED
LDAMKDVMPQ AYKELVENCR ILESHYKEMQ DIEFTVQESR LWMLQCRTGK RTGKSAVKIA
VDMVNEGLVE RRAAIKMVEP GHLDQLLHPQ FENPSAYKDQ VIATGLPASP GAAVGQVVFT
AEDAETWHSQ GKSVILVRAE TSPEDVGGMH AAAGILTERG GMTSHAAVVA RGWGKCCVSG
CSGIRVNDAE KVVKIGGNVL REGEWLSLNG STGEVILGKQ PLSPPALSGD LGTFMSWVDD
VRKLKVLANA DTPEDALAAR NNGAEGIGLC RTEHMFFASD ERIKAVRQMI MAPTVELRQQ
ALDRLLPYQR SDFEGIFRAM DGLSVTIRLL DPPLHEFLPE GNVEEIVREL CSETGANQED
ALARIEKLSE VNPMLGFRGC RLGISYPELT EMQARAIFEA AIAMTNQGVQ VFPEIMVPLV
GTPQELGHQV ALIRQVANKV FTSMGKTIGY KIGTMIEIPR AALVADEIAE QAEFFSFGTN
DLTQMTFGYS RDDVGKFIPI YLAQGILQHD PFEVLDQRGV GELVKLATER GRKARPNLKV
GICGEHGGEP SSVAFFAKTG LDYVSCSPFR VPIARLAAAQ VLV
