ID A0A0P8ZDR5_DROAN Unreviewed; 1748 AA.
AC A0A0P8ZDR5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=oleoyl-[acyl-carrier-protein] hydrolase {ECO:0000256|ARBA:ARBA00012480};
DE EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
GN Name=Dana\GF27091 {ECO:0000313|EMBL:KPU72694.1};
GN ORFNames=GF27091 {ECO:0000313|EMBL:KPU72694.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:KPU72694.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:KPU72694.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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; CH902623; KPU72694.1; -; Genomic_DNA.
DR RefSeq; XP_014760922.1; XM_014905436.1.
DR SMR; A0A0P8ZDR5; -.
DR STRING; 7217.A0A0P8ZDR5; -.
DR EnsemblMetazoa; FBtr0391944; FBpp0351358; FBgn0274314.
DR InParanoid; A0A0P8ZDR5; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0032787; P:monocarboxylic acid metabolic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR Gene3D; 1.10.287.1960; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR049391; FAS_pseudo-KR.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF23; FATTY ACID SYNTHASE 3; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF21149; FAS_pseudo-KR; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1348..1425
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPU72694.1"
SQ SEQUENCE 1748 AA; 195876 MW; 316972E494690AFF CRC64;
VGIGYKTILH MLPESIEVAC HNSPDSCTIS GPIDDVSNFV ADLKAKGIFA KEVPCSNIAY
HSKYIAKMGP PLLQYMKEII PNPKKRSSKW LSTSVPKLEW EHPTRKLCSA EYHTNNLLNS
VLFEETFSLL PENSMTIEVA PHGLLGAILK RSMANGVHIP LTNRGNKNNA LFFMSALGKI
YQNGVLVPVA KLYSPIDFPV SRNTPKISSL IRWDHSEDWF VTKYENMKTK SSGERVFTVN
LASDNEEFMS GHVIDGKILV PATCYLQYVW ETFSLMYHGP SYMDVPVEFE DVRFVRATNM
PTSGEVELNV MIHYGTGRFE ITEAGSLVVT GNIREIYNPT IPEVYHFQKE SNFPMISKKD
FYKELRLRGY HYNGAFKEVF SARSDGLFGQ VEWHYNWVTF MDAMLQIQIL GTDSRTLLLP
TKIRKLRING VHHFDLMTKM DPDNRIFDVY VDQKYDRIIA GGIELIGLHA SPVQRRRPPG
IPVLEKYLFI PYASSALSIE NATRVCVQLA LENNPTLKMK IVEVDTNGKK SLINTFVESI
EDLPVITGEY MLLTSQNIDE IPGVHIENGR LCTQSNCHFV ICSGFEGDNN RDVIETSKKA
LVDNGYLLVR ETSLFNMDTT EISDQFRQIT IIPIDENDET FVLLQKVPQK LQIQPILVEV
SENDKAFEWI SHIQTALTTK TPVIVYSFNE IFSGVLGFVN CLRKEPDGNL VRCVFINDIN
APAFDLSHPL YATQLSLGMA FNVFHNGRWG SYRHLLLPKC DKRISRLDHI YGNVIQRGDL
STLQWLEGPL NPQNCIIKIA YSSLNFRDVM LATGRLAVEL YGSSRIDQNC VLGFEYSGIN
MVTGRRIMSM VVKGGVASYV EKPSKLMWDI PSHWSLKEAA TVPVVYVTVY YAFFMIGDIR
KAKTILIHAG SGGIGLAAIR VALAYNLEVF TTCSTQKKKK FLLDTFPKLK ESNIGNSRDT
SFEFMIHRET DGKGVDYVLN SLSEDKLLAS VRCLGKSGHF LEIGKFDMAN DSKLGMGCFL
KEITFHAVLA DNLLTASDQD IWHLKNMIDS DISQGIIVPL PVTVFPAHEI EQAFRHLIGG
KHIGKVVIQV REDPEDAATL PVCAINQIYF KPSLSYIIPG GLGGFGMELA DWMAIRGARK
IVLSSSRGIT KDYQSYRIAL WNTYGCEVLI STDDITTKEG CQQLLSRAAN LGPVGGIFNL
AVTLRDGIFS NQSAKQFLDC FSPKAIATKY LDELSRVSCP DLEYFTIFSS VSCGRGNAGQ
TNYGMANSIM ERIIERRHKD GLPAKGIQWG AVGEVGLVAD MADDKIDMEI GGTLQQRISS
CLQELDRLLS SEDPIVSSMV VAEKRSGRSG NENIIDAVMN IMGIRDLKSV SLGTTLSEMG
MDSLMAVEIK QTLERDFELI LTPQDLRLLT FQKLQEFVDA KKKENTDGLP MIFASESKLL
GMDLLIRNLG DEAHCDKIVV PLATRATLSK QSLPPNIIIP GLEGTAGRAW YQLGSALHSR
AIVLQLHQFS NLLTVNDISE KSIEHIKQIL MPTEPYYIIG YSYGTLVALK IAQLLETAGF
RGHITLLDGA PHFLKRLTNL HLGEHFSEND VYNLLFSSIV NQIFPDETKE SAAQIFQKID
NIDDKMALFM EYVEKQNVYT KEYSKTMVTA MFNRVKMTSN LDLESFGNLK ADITLVRPAE
VSLQDVEEDY CVSLLTSGKV TLKVIEGNHT TMLDNPILSQ IINDFDPSLL DDKNFEEYIR
NDKPVSVV
//
