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Database: UniProt
Entry: A0A194QV09_PAPMA
LinkDB: A0A194QV09_PAPMA
Original site: A0A194QV09_PAPMA 
ID   A0A194QV09_PAPMA        Unreviewed;      1314 AA.
AC   A0A194QV09;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   SubName: Full=Putative phosphoenolpyruvate synthase {ECO:0000313|EMBL:KPJ09368.1};
GN   ORFNames=RR48_08819 {ECO:0000313|EMBL:KPJ09368.1};
OS   Papilio machaon (Old World swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ09368.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ09368.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ09368.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ09368.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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DR   EMBL; KQ461103; KPJ09368.1; -; Genomic_DNA.
DR   RefSeq; XP_014366099.1; XM_014510613.1.
DR   STRING; 76193.A0A194QV09; -.
DR   GeneID; 106716936; -.
DR   KEGG; pmac:106716936; -.
DR   InParanoid; A0A194QV09; -.
DR   OrthoDB; 3092388at2759; -.
DR   Proteomes; UP000053240; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
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; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; Pyruvate {ECO:0000313|EMBL:KPJ09368.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          433..751
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          1227..1298
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   1314 AA;  146280 MW;  0CE97171A4C23E22 CRC64;
     MDLYDILLQA GLITSALVLY LIYIRRPTNK SGPYREKEWN YIIKYIFARI AVRRWKTKFP
     SKFVVSEKSK EGLTEGWDGI SIRTSATDGT TVLLGIRKIC GRKPMAEVNL YVKLVDGTSY
     KLPSYPETLV VQWETIEDGW SAGGLKVQIL EPEQRLRILY NGLLRNSVDN TIQHVRLNLI
     WCSATSVVRH PADWSEQLAA HALALETWRD GSWAQILSKF DHNSWLQFGA AQGTLQTFDE
     EGALQKRERL RMRGVRERGW SRDVCPRRAL TLTAVAKDGT AIMLRGLSYK NIFNELISGC
     VRFPDYTIKP LTATDLIMSE FCETPDGIPK VYTITAVANG RSLKVVLRIN DDGVKVISLT
     PQKQDIVYRT LAVEINGEHG TGILELTYES SDKTPIPQQA SQTHFLKWLN EDKAGSVGNC
     LSFEDSAAAC PAYVGGKGAS LALLASVQND EGYKVPPGFC LTTKALERQL EVYPELIQAI
     KGIEAANEDY DEDIFKQKCE ITVELFMKTD ISEDIKEEIL KYLNDLRMKI KEQNFSIEER
     FAVRSSGVGE DSEATSAAGQ NETVLGCVGD ADVLRAVRRC WASMFAFNSS YYRRQNGQPC
     SCGGGVVVQA LASARVAGVL FTRHPLGDPS RLLITANYGL GESVVSGSVE PDSIIVKRET
     NGLRISKIDL GSKKERVKPD GDGVSVETVS DEEQKVPCLT VSEILKLAKL GVSQEELWGA
     GRDIEWAIND DVIYLLQARP ITSLERWTEE ELLHELDFPI MSDDELLTFA NTGEVLPKPL
     TPMTYDLVVT PLQKGIDGVI GCNGDHYDRS IAVTHNRCAL VLYNSVYRRM PPKIDIGIRM
     VEMAVHGHKV ADDNIVSTAL HRRRPHFLDR VLTMASMFKS VLFAKSTMND TIKRVNEMNL
     EIETNDPLEY LNRLVAGLSE RMQVYSANHS HTSSASTFTQ FIAMSILLEG KEDFTPEHCS
     EIGVLLSSGD VLSAQVPLAL ADITRELEDS GKAQEFRVLE PSDAMTWLRK NLPHVHMDIC
     QFLEQHGHRA IMEFDLATKP WALVPEEFIK VLQTMPATKD ASKIIKSNAE IIASLKTPQK
     PSTRKALRWV LPLCHRSVRH REGTKAHLIL AIHKLRLSIL NLAKLLVRQW YLPHPDLIFF
     FRVNELRAYI EKRNPAILRK AIQRQQLYPG WCKLKFAEVN TGWFDPLPTA GPAVTAGDVT
     IHATSVCGGE VVGRACVVKD LSEISELQSG DILITHSTDI GWSPYFPLLS GIVTELGGLI
     SHGAVIAREY GLPCIVGATN ATSAFATGDT VRLCATTGTV QRVHLHTADT VADE
//
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