ID A0A182X139_ANOQN Unreviewed; 1285 AA.
AC A0A182X139;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA003506-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA003506-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA003506-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|RuleBase:RU003694}.
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DR STRING; 34691.A0A182X139; -.
DR EnsemblMetazoa; AQUA003506-RA; AQUA003506-PA; AQUA003506.
DR VEuPathDB; VectorBase:AQUA003506; -.
DR Proteomes; UP000076407; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF23; FATTY ACID SYNTHASE 3; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 219..625
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1285 AA; 143749 MW; AD9ECC4130FF0CE0 CRC64;
MFETVFAKAE QFLVIGYSFG SLLALEVVKR LEARSLRGKL MLIDGSPLYL QRFASHHLSG
FDDEHLQMAI LTLVLRFSLP SVSNEILSSI MGEATYENRV TKMLDIGRES NPFSEDYTRK
MMRVLLFRLK AAMNMSTEVK EKLASPLVLV RSGTIGDIEE DYGLTEFTSS SMIVKIIDGT
HQTMLANMEL LEIINKDTFI HLPFTMKTVT NCSEPIDSEN SIVISGISGK YPRSDNVQEF
ANNLYSKVDL VDDKEERWRH THPDIPKRLG KLNHLEKFDA DFFGYSPKEA HTMDPQHRLL
LEHCYEAVMD AGLHLDDLRG SKTGVFIGIS MSETETYWTY KKTQMPYRRV MLGFTRSMTA
LKIAYALDLK GPAMTVDTAC SSSMYALDWA CKAIRQGQCD AAIVAGTNLT LHPYITLQFA
LLGVLAADGY CRPFDKNASG YSRSEANAVI LLQKAKDAKR IYAHVVNTKT NCDGYKLEGI
TFPSNKIQKQ LLDELYSEVP YDPKDISYVE AHSTGTVVGD PEECDAIEKV FCPNRTSPLL
VGSVKSNIGH SEPAAGLCSL TKCIIAMQTG LIPPNIHYTE PRKDVPSLLN GHLKVVDEAT
PLGGPLVAVN SFGFGGANAH ALLHAHTRKK GHDIRPHDDL PRLVVWSGRT IEAVDQFLEG
IAKHSFDPEL YALTHNIQRK ELAKMTSRGY AVLARGSDGS TTILQKNISK ANKTLPPFAI
VFGQMDYEWQ ATLQAFEKFP PFKASVEQCL ALLKEPEHDC IFSKDDYATI LQRAVWTLII
QIGVYQVLKS IGVKVDQYGG YSIGQITCAY IDGVLSLADA IRVAFTHGVL LSSYQNPETV
NYRDIITNKE LNTKLTSILE SFLFAKATDR WKTATSVLSF RIYDPKSATQ MFNRIDSNAI
VLQPLPSIQS TDSLVNSFLA SIGRAFIHGQ HCQLLDLYPT VTFPVSLETP MIGPLIRWNH
SVDWHVANFQ TKKMVDQGSN QHSVTLAEQE YIAGHCIDGR VLIPATEYLY LVWDSFTSKT
GTIPNEVAVQ FTEVEFLRAT TIAAGQVITL FVEINDISGH FEVSEGSTLV VKGCIQRLDH
FQRQPIEQRN QPAITLPTKD FYKELRLRGY HYGGFFKSVM ESAADGSHAK IEWKGNWTAL
LDCMLQVAII ALDTRSLMIP TRIESIKIDP DVIKPVMDQP TYSDRVEKLM TVARDSNPFS
DQYARKMMRV LFYRLKVAMN MSTEVKEKIA SPLVLVRSAT IVDVEEDYGL SEFTVASLIV
KIIDGTHQTM LANPELIEII NKDTL
//