ID A0A1Q9EYC9_SYMMI Unreviewed; 2131 AA.
AC A0A1Q9EYC9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
GN Name=ppdK {ECO:0000313|EMBL:OLQ12401.1};
GN ORFNames=AK812_SmicGene3691 {ECO:0000313|EMBL:OLQ12401.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ12401.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ12401.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ12401.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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:OLQ12401.1}.
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DR EMBL; LSRX01000044; OLQ12401.1; -; Genomic_DNA.
DR OrthoDB; 1219344at2759; -.
DR Proteomes; UP000186817; 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: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:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR CDD; cd22744; OTU; 1.
DR Gene3D; 1.20.80.30; -; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
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 NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:OLQ12401.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:OLQ12401.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1566..1688
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 952..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1853..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2131 AA; 231908 MW; 41C5C2A9D767CDEA CRC64;
MGASTCGFHP TGFVKCRLLR NCQRHVHPRR YQALSFEDLS SKPALINPIK LKAMAMKMRH
RLHNVEFKRP TSVPERGPRS LAVAAVESEP QPARAPKTPG LCTTTTAATC QFVQHGNVEF
RFWLNFLALV PLAKILGDAT EGLRTNIVSV GLPDDGVLLG SGTLLDMTKS YGTPLMMSLS
LALGTAFLLG GLTREAGTIP FTLSVRYTPK LDSPYPFWLQ AFSFQLHPSL CSFLRLFVMT
WVYNFGSGNA DGRAEMKNLL GGKGANLAEM ASIGLPVPPG FTLTTEICTY YYQNDCQYPA
DLKEQVTNAL ALVETRTGRK FGDATNPLLV SVRSGARASM PGMMDTVLNL GLNDATAEAL
AKQSGDRRFA FDSYRRFVQM YSDVVLGIEL HNFEKLLERS KKKRGVTQDH ELQPKDLEQL
VKDYKACVYL QLGEEFPEDP QQQLWGAVGA VFGSWMNQRA KTYRKLHDIP EEWGTAVNVQ
AMVFGNMGND CATGVAFTRN PSNGAKDFYG EFLVNAQGED VVAGIRTPQE LTIKARKSHG
SDLPSLEEVM PGIFRELENV RHQLENHYRD MQDIEFTIQQ GKLYMLQTRT GKRTAHAALQ
IAVDMATEGL ISKSQALMRL KPDLIDQLLH PTLDPKAKKT VIAKGLPASP GAAAGKVVFS
ADEAVTRSEN GDKVILVRIE TSPDDIHGLH AAEGVLTTRG GMTSHAAVVA RGMGRPCVAG
AGEVKVNYSS ASFEVGDVVV REGQLVTIDG VTGEVMLGEV PTVPPQLSGA FGTVMSWADE
FRTMQVRANA ETPADARQAK EFGCEGIGLV RTEHMFFEGG RIVAMRQMIL ASDKTDRQAA
LDKLLAMQRE DISIHEDAPC AFARLADADH VHGAKFLLVM GGSWYDSGQH NQLLGVRIGE
ASNPGPRSVC GYGSWRSRDF GALGFQQQVM KMMQSMMEAM MGKMMESFFG GGSQWSSGAT
PMDNPKGKGK HGQMKGPGGG SMGEPPGAAP ASGGPGKGVK GKDAGNPKGK PKGKDGHGDV
TGQDADYAKG KPKGQGKYGG GAEGAKPFRK GTKDDSGTGM KDGGQGPFGA NNSKGKGKGK
IDRPGGESRE WRQDGGWETI EWHAKPSAFG ASRLVTTIAA LEDALDQADK FVAQFKGADF
EEAATMLEGG CPKGTVLIKD GEACESMDAL QKQWPVIKKH VPGLVNGATR LRCVWVCTFG
ADSADLAPAV GFVKAAAPKT RRHHDTVVVR CCAWQGFADE KEFKQLLKRP GQFARSWFTK
VAPLHIQEFI DSWGWQSYGE DQARGLVRLT KEAASVALRS SGCWALGAAL FFTPLDWAAI
DASEAPSLLW VDRQEEENAK TYLERVRKEA DVFGLHCGGD RLAVRLDPLD ARIMPQRGTW
HLRGARFEWL PEDVESVLTA VGFTEVSIEA KLLRRGLPVW EFRAVRVDFR DFVPIELEPG
EDLAAEGEVD IVLEASRVAR RRKQGEARTL PAERVAKFGA INVEELVKQV AAPKRKSRFD
KPRTSVAPAA PLEDMVVDTD GADEGDEVGQ KRRRPEQGGR DGDEGEDSAG SASQPSSKCV
LLPPGAKVHA NPGGGDCLFY CLADVLSGVQ NKTRGHRQVR AGVVAWMEKH TELLEQHWDH
LGPDGKHMEG SFRDYLKAVR RSGAWAGWLE LYAAGVAEDL NILILSPDGV VRFAARNEVG
HFAVLKYECG HYEVLTMDQK RIAELWLAAS DAKPVGGRGG GRSKASSLHL SQFDAASEGT
SWAHSSLHLS AAAVQEQNAI AELDGGPAGM DGGAQPLPEG PVGGLALSEF ASGGTATPHD
GSARSRRAWP TPADLRSLSS AHTERPVVVP PRRRLRSKSQ QWMPLSALAS AGAGVTASLD
DQEPGSPVAA SPPKPQVPRP RKSKYRVDDV ARWPCPLCPM VIESKSVSIL CKLRYSHCHR
HHEGQGLPGA RRVCLDAFRA LGPEEPDDWR CPLCDWGLPQ GTRGQISEVA LATAKDQHRQ
AKHPGVSRKE YDGKLKVRGK RKAVHVMQMR VRRLNAFAAK RQRDGVASFV GWKSFTWPSI
RNSKSKERRA LCLQQAWCCV HCGFCTRVAV CRKSHVKLCS TWDRSKLVGQ RARLWKSYAE
AKKLEHGVDP VMLLQVFENA DLVMGGAGQP S
//
