GenomeNet

Database: UniProt
Entry: D2A4M7_TRICA
LinkDB: D2A4M7_TRICA
Original site: D2A4M7_TRICA 
ID   D2A4M7_TRICA            Unreviewed;      2165 AA.
AC   D2A4M7;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=oleoyl-[acyl-carrier-protein] hydrolase {ECO:0000256|ARBA:ARBA00012480};
DE            EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
GN   Name=AUGUSTUS-3.0.2_15337 {ECO:0000313|EMBL:EFA05201.1};
GN   ORFNames=TcasGA2_TC015337 {ECO:0000313|EMBL:EFA05201.1};
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:EFA05201.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA05201.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA05201.1,
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:EFA05201.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA05201.1,
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ971344; EFA05201.1; -; Genomic_DNA.
DR   STRING; 7070.D2A4M7; -.
DR   EnsemblMetazoa; TC015337_001; TC015337_001; TC015337.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_7_1; -.
DR   InParanoid; D2A4M7; -.
DR   OMA; MFIEDID; -.
DR   PhylomeDB; D2A4M7; -.
DR   Proteomes; UP000007266; Linkage group 6.
DR   GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR049391; FAS_pseudo-KR.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF23; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF21149; FAS_pseudo-KR; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          18..425
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   COILED          33..60
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2165 AA;  242344 MW;  F4F3615F967380CE CRC64;
     MNRYDFEYGK WLSSAPPDEQ VVISGISGKF PKCENVTEFL ENLEEKKDML TESKERFKVD
     HPELPLKAGL LQGIDKFDAG FFGIHHRQIQ TLYLGLRKLL EITTEAIMDA GIHPEELKGS
     KTGVFVGYSW NDSEVEVLAK VTEPQQFAMT GLLRSMVAHR LSYFFKLKGP SHICETACSS
     SLVALDHALK ALRSDQCENA IVATCHLTFH PAVTVQFFRL GVLSPDSKCK VFDQEANGYV
     RSEAMSCLFL QKSKNARRIY AKILHSKENS DGFKSGGITF PSSPIQGQLL KEMYAESGIN
     PNELSYFEAH GTATRVGDVE EVNAIDTILA QNRTEPLYIG SVKSNIGHSE PGSGLSSLIK
     VILCMHSGYL LPNINYNRVK QNITGIVDGR LKVVTEKTPL HSPNAIAGVS SFGFGGSNCH
     VIVQRWGEDV AQTDGMPRLV CVSGRTEMAV WGFLNELKSK HFDVEFVALV HHVFKHEFSE
     HPFRGFVVLG EKGPLSESVR PCPLEKVPLF VKFGPMDKSY QTVGRYFLKF PVFEQTIRRI
     GTLLGNDQII ETLKGYKNQV KDPTLLSSYV QLGIIDVLKV LKIDAKLILD GSKAKLISQY
     YQNSSLETIL ERIKSQETSN GFERLDVVPK HSLVCDFTDS GPFGTNPEQF LEFLGRLYLN
     NYNPQIWQLY PQVKFPVRRT TPFLSPLIKW NHETKWPIPE CKIQAEKLTV SVVFNLEEEA
     DKYIEGHVID GRNLFPATGY LYLIWVIYAE NHLTRSAKLA PVVFTNCKFI RATIVPKIGF
     LNLVVSIQRE SGFFEIMEND TIVVTGRIQA PQDLKPFKST FKVVENQSEV VLDQYDIYKE
     LHLRGYDYTG LFKNLVKCNT EATCGVLKWD NNWVAFMDTM LQIKILQMDT RDLYVPVGIN
     KLVIDPIEHL RIIDQVGQVV PINAYKNNNL IKSGGIEISG LYASPISKRK QILEPVLEKY
     VFVPNSGTMD LSTITRVNTQ IILENTMEEL FKAVEIVDEV VPETLLMPLI YNALEDVPVV
     HPNLIISTKH VLEEVPGVKI ENYSLTNESN LSLIVGTKIL SRSTVLQKVL TSLSKTGYIL
     SREDVNFSPI TNVVTVTTYS TTSGEKLVLC KKLEPVKSHN FVKISSDNFN WVQEIQKLPH
     DNLVLYSEYP CDGTLGLINC LRREPGGGRI ICVFMMDKAP VFDSLDPIYS QQIAKNLAVS
     VYKNGTWGTY RHLRLEDSLE VLREHSFVTC GSRGDLSTLR WVQGPLTVNS DLDLVISNYC
     AINFKDIMTA SARITVTLDR INQENIEGIE FSGRKNSQNV MGIISNGALS TLIASDPNLT
     WVVPPHWSLE DAATVPVVYA TVIYALLMRS SLNAGTSILI HSGTGGVGLA AINVALAHKC
     TVFVTVGTKE KRDFLKKNFP EINERHIGNS RDVSFKEMIL KETRGRGVDV VLNSLSEEKL
     KTSVQCLARG GKFMEIGKFD LVNNNSLQLL LLEKEASYHG IMLDTLFKET KERKTGLWLK
     VDEGLKKGYI KPLPRTVFES NKVETAFRYM MSGTHIGKVL LKVRDESTDK PKLIKAYPKF
     YCDPKKCYIV IGGLGGFGLE LTDWLVLRGA RNLVLTSRTG VQTGYQTQRI KIWQSYGARV
     NISTITISSK DDCVKLIQEA TKLAPVDAIF NLAVVLKDEL FENQTEENFR ISLTPKAFAT
     KYLDQVSRDL CPNLRFFVVF SSVSCGRGNI GQSNYGMANS IMERVCEKRK SEGFPALAIQ
     WGAIGDVGLV AKMQKDNKEL VIGGTLQQKI SSCLNVMDRF LNQDNPVVSS MVVAEKRDKR
     LGSGSAVDVV ATILGIKDLK TISHHSTLAE LGMDSMMSTE VMQILEKDFE IFISAKEIRN
     LTFTRLKEMG KNSPNQDQNK QKLSQGTKTL IKFIPENCDE TLVTIPSLGT TTSKSLIFVF
     PGIEGVLKLL DPLTTNLKSR LLGVQYSYKN PESTIRETAI KILPLIERQL TAKNFNFVGY
     SFGALVALEL AQLLEEKGFV GKIVALDGSP HYTKQSIQHY APGESEAETE TMLLYNILGT
     VLPLDLLEKS KTDLIKCSNF DERINRAVSL IPEDLAEKHK LEKQAAVTLH QRFKAVRCYT
     FGGEKIKSFV KLYKAEVPLV GGMDDDYKLA QLCDNKVEVM TVGGDHTTML EQGELANDLN
     KIFEE
//
DBGET integrated database retrieval system