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Database: UniProt
Entry: A0A139WGR7_TRICA
LinkDB: A0A139WGR7_TRICA
Original site: A0A139WGR7_TRICA 
ID   A0A139WGR7_TRICA        Unreviewed;      2257 AA.
AC   A0A139WGR7;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0008006|Google:ProtNLM};
GN   Name=AUGUSTUS-3.0.2_34713 {ECO:0000313|EMBL:KYB27089.1};
GN   ORFNames=TcasGA2_TC034713 {ECO:0000313|EMBL:KYB27089.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB27089.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB27089.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB27089.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:KYB27089.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB27089.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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DR   EMBL; KQ971344; KYB27089.1; -; Genomic_DNA.
DR   STRING; 7070.A0A139WGR7; -.
DR   EnsemblMetazoa; TC034713_001; TC034713_001; TC034713.
DR   eggNOG; ENOG502QS3J; Eukaryota.
DR   InParanoid; A0A139WGR7; -.
DR   Proteomes; UP000007266; Linkage group 6.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          414..719
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          1210..1281
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   2257 AA;  255932 MW;  B73834CFF197F0FE CRC64;
     MELLLNFCYY VTLFLIPISL YVLVFQHRTK NRFYTNRDWF YIIKFLIAKS AVKKHQNKFK
     TKINITESPI EIRTENYCDN YFIYGADQKG NSLSLRFIIG SGLVGEVFLC LRLSTGAIYT
     FPGEKKTKQY NLSDWHWKTK DLHLEILEPF KRHRVTFNGL LSNATNDIEH VRFNLTWIAT
     NAPRFHPQDA ATDLLTNALA QHPWRDGDWL SLLGDECGYE QFGALHGFIR GDSFKDDFFV
     NLPSCRTRFW GTAEKLAVSK CLHLFVAGHD GTLISIWVKS LKHGCHGLQY GNVVMTNGTI
     QPITASDIRF DCLGQNSQLP ETFLIHIYAL KQTFRIVFHT NTIKTIVDGH DLSNIPADCD
     LNTQQGKSLV ELWQGVKNTS RDKPLKPLLI ENKSKTLPTC YVISLDDESA KIVNLSGGKG
     CSLAMLTCLK SDDFIVPNGF IITVNAFNKQ LEMNFNMKKA VSILDDICCG RSLGDLEHAC
     AQTIKTFESE KIIPEVASVI LQAFRNLKPR PTDRFAVRSS AIGEDSEDLS AAGQNSTFLG
     CSTFASILQS VSACWASLYT NQSVRYRHKH GIAIPSQMAV VVQKMVQADC AGVLFTCHPS
     TGNPAHIVIT ANHGLGESVV SGRSEPDTII LERTFDNDVT IQSKTLGLKN KIVKMTTDGE
     GVVECDGLQG FSLTDNQALV LGRVGVALEE KMGGARDIEW AFSQGRLYLL QARPITTLNL
     WTDYELLHEF DVATLSDDVV YTVANTGEIL PGAISTLTLS TVVKAIDKSI QISVEGHSNE
     YSLKCLGTFQ GHLFVDVITG IHRRVKNKIE LISKIVDLAI FGHPIINEKI HYLSLNRFGP
     IGSLEQFKEL YTMIKLAWCN EKNAKMSKTI NETYQVGIDT TRDTLKDIYN KIDKSLNKMA
     EVLLLHCYTT RTSVSYQIFA MTVLAENAQD FTIDHYNDIA MLLASCDEVI SAEIPNTLAN
     ITRILNENHQ NMKFAEIDPN LGRKWLKDNS PEASKIFEQF IKNHGHRALR EFDIFNETWG
     TNPVEVIKMI QTNCRSKSPK QEKTIKPIDE VIAGLVSPTK TSTRKFLKFL MNKSRRAVGL
     REQTKSESIR FVDKLRQSYR ILGQKMAFQG LIPEPDLIFH LSHYEIGQIL DKSDRNPIII
     TKALRRQKLY PKWDRLKFPE ISYGIPLPET RDFIPRSGSG TVKCEGTPVC FGIIQARACV
     ITDLKEIDQL HEGDVLITYC TDIGWSPYFP MLGGIVTELG GLVSHGAVIA REYGLPCIVG
     AKGATKMFKT GDLVILSGEN GTVERCATNI PPIFDHFTPK CVFTLPKCSH NLTVTKSRFF
     HIRPPNRAKL YTDGENAYAY IILPKIVKFT TCYNAPKQIK TSEQFDEFLN RNWRDSCASD
     IVEAFECIKD YCVVKDINVG DVRFDKLVDG LMDHCEKLTD EELLRLLTLL TEYPQCESST
     THNYHDIWSC LDDICCWKMS NWNFQKLFTF AEIWYRLNLG RLSDFVYEVI DKAVKKSHRL
     PNEFLVYICF YLNVARKKEV PFDFEHTLAE RIDEFNVEEL TIVAMAYFKT KSKVKLLPIL
     NAMIRAINAN CDSINEISLT AMLKTIRLSQ HIQTADQIPP LLDNLMPQIP RLSKLAILHI
     ALLGTSLQIK HEKSLTRCAQ SILEDIENVR LKDLERILLA CSMFNIDTNP SIFDLVSNEL
     KKSNRQQESI QYNRSLGSTI HYLTFRQVYP FELINKVLDT EYINDVYGNS SRNFPRELFS
     LDCSLEIECP NYSGNRLDPV KKTKSAKWLT DYTPSHTQFK RLTLADKFYL DVAEHVSIAI
     GQNCVRHYHV LPHFSKSDIV ICRDLSDGNF VVPKLLDRYV LGDIMRPFGD FDWFAFIVMT
     TNLTVRGRNE PLGSMVMKER QLRRIGFKPI FVYWSEFGEL GTEKEKVKNL FQKIMNKLYK
     PKVTFSDSLT KISKNVRREI RPRSRSVYTT SSYISDDLGT PRDLKYENPS SWSPYVPKPI
     VVKNYYPDDL NSETWADDGG YMGGTTITPH GVISLRLHDR IRVDISLDRA IRIINMKNYI
     VLALNASGSS SALIHPNGRV LQYGSRVEIL AHDGQGNNKY AKMWYKGVSF TSDQCALVYL
     VDSAGTRTTT DTFTDLTGDI TLDVFYNRPN CGLDFACVTP GTHLVNEAVS VLQSANYWLT
     EDRTDNWIIN NVRISQTADG LVRVGRNSNK FSLRTSPTNG SASVSSPYLH CTGSMGQTRH
     LFVRRGERRM HYDGTTFIVR NAGHSAGFDE RHQLKVY
//
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