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Database: UniProt
Entry: A0A136HQE4_9GAMM
LinkDB: A0A136HQE4_9GAMM
Original site: A0A136HQE4_9GAMM 
ID   A0A136HQE4_9GAMM        Unreviewed;      2720 AA.
AC   A0A136HQE4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KXJ57589.1};
GN   ORFNames=AXW15_06060 {ECO:0000313|EMBL:KXJ57589.1};
OS   Neptuniibacter sp. Phe_28.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Neptuniibacter.
OX   NCBI_TaxID=1795871 {ECO:0000313|EMBL:KXJ57589.1, ECO:0000313|Proteomes:UP000070472};
RN   [1] {ECO:0000313|Proteomes:UP000070472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXJ57589.1}.
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DR   EMBL; LSMR01000009; KXJ57589.1; -; Genomic_DNA.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000070472; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR004136; NMO.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR   PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00698; Acyl_transf_1; 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; PF03060; NMO; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 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   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          681..1123
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   2720 AA;  292349 MW;  67AFFB4B574C13C7 CRC64;
     MNEFKKFVYT PAGYNDASLA IAACRAGGIG ILNAELSADS DKLLEQFALL SVHARNPFGI
     KVDTPQKALL SAAAASVDQG FSYLIVDELV LASLAIEIKR LRKLGVTVLV EVTNAHTDAA
     TLEKQVDGLM VKGYEAGGFV GEGSSFILLQ KWSAKTGLPL FVRGGITPHV AAACSAVGAK
     GGVLESQVLL LKDSPLSERL SSFIGNLSGN ETIAVGDEEL GAYFRVLVRP GYREAQVFNN
     NVSGRLVNPE DVLGKIDWDA PQKGLLPLGQ DVCFAKAWRE KYGYLSNVFA AIDQTIHDSM
     QAAIQYKPLA ENAPLAEALG VRFPLVQGPM SRVSDSAEFA GAVADGGALP MLAFALLKGA
     ALDKLLAETD KRLGDKPWGI GLLGFAPQSL LDEQIELAQK YKPQYAIIAG GRPDQAVKLE
     QEGIQSFLHV PSANLIPLFL QEGARRFIFE GRECGGHIGP LSSFVLWSSM VDRLLEELES
     GKTKGEGIQL LFAGGIHDAA SAAMVQVLAA PLLDKGVQVG ALMGSSYLFT KEIVESGAIV
     PAFQKEVVEC EHTVSLESGP GHASRCAYTP FAKMFFDKRR EMIEQGVPVD EARATLDDLI
     MGRLRIASKG CARLGENAKL TALDEATQHA DGMYMLGQVA TLRTELIDVE TLHAQVTEDS
     HALLVANSMD SAQEDEADSS PVDIAIVGIS GLFPGANSTE EYWSNILDKV DAITEIPSHR
     WDWRLYFDED RYSKDKIYSR WGGFIDDLAF DPTKYGMPPK SVEAVDPMQL MALEVASRTL
     ADAGYDKRDF DRENASVIIG ASGGAGDVGM QYGLRAEMPR FKGDLPDHIA DILPEWTEDS
     FAGILINVMA GRIANRLNFG GVNFTTDAAC ASSLAAIYQG ISELSAGRSN MVLAGGVDTV
     QGPFGYLCFS KTQALSPRGR CSTFDVSGDG IVISEGIAMV AMKRLADAER DGDQVYAVIK
     GVGGSSDGKA KGLTAPLPQG QLRAMRRAYK QAGFGPETVG LFEAHGTGTV AGDTAELEST
     ISLLKEAGAG THQAVVGSVK TMIGHTKAAA GVAGLIKACL ALKHQTLPPH YGVTQPNNVL
     MGEDCPLYLV DEAQPWIKKE QPRRAACSAF GFGGTNFHVV MEEYQGEYRP WMKKAVRTQG
     PAELLIWSED TTEALIATLS NVAKELTSVA ALDLKKLSFN LINKHKSGLE TVTLVVRDQA
     DFAEKVVATL GYLKDEISAL PEGAYYGNGQ KADGKVAAIF PGQGAQYPQM GRELAYTYST
     VGNALSDADK LLKAPFEKRF AGCSLSDFIY PRGAYTPEQK TAATQALTST DVTQPALGAV
     ETGLWRMLKT LGFKADMFAG HSYGEFVALH AAGAFDYETL VSLSEARGRF IVDEAKRAGD
     ELGTMAAVQA TRDKVETAIK QIDGVIVANH NAPTQCIISG SKAGIAQAIE ALSQTDIMAT
     PIPVAAAFHS SFVKPAQSHL AKLIESTKWI SPELPVYSNS TGDVHDASVA KLKSSMAAHL
     VNPVEFVAEI EAMYRDGARI FVEVGPKSIL SRLTKQILGD RPHTTITLDN DQEGVYGLLS
     ALANLVCEGV ELDLQPLLAG IQSELVSSNG LENYDSAAPI SKQTWMLNGS GARRATEAVR
     QIGVTLEQVL AQNSVAAEAS SAGSVMTTVP SPQINENISY DRHHFKHNKE RKMDGRRQAP
     NAGGPAVMAE YFDMMRQFLE SQESVMSMYL SGTPVPRSGE TRPQRLPKTA PQMAELSMEV
     PVVAAPVAAP VVAPVAAPAP APVAVAPVAA PAPAPVAAPV AEAKPATDDA FDREKITQML
     LEIVEDKTGY PSDMVGLDQK LEADLGIDSI KRIEIVGSLL KALPAAYGDA LGENRGQLNT
     QENLTGMLDL LCDLPVGAAT SPFKVAGVRA EVSSTLSDSS FRHVVVPSPA PIEVNAKRAL
     NIGHYVITRD AADIAGKLAA LLTDRGCTVQ IVEPSVLEDE EQILKFSAAV CAEKADLAGV
     IHLAEIGSPA LMSESSVVDF KAVLNSNEKS FFLLLKGLSP AFSDAAHIVA ASGLGGAFGR
     TNAVFNGLSL QSGFVGCLKS VSEERPALRV KAIDLDAEQS VGDLANILLE EMMLCGGRQE
     VGYPAGKRTI FKTVAEVAPQ PAENATLDGL TVLATGGLRG ITAEVLREVA LPGNTLLLTG
     RSPLPEPETA ETAALKTEAE LRQFFIAQVR DGILSLTPAE VMKKVAGVIG AREMLSNLQD
     FQQRGAKVEY FAVDVTDESS MKGLLDAIYD KYGALHGVVH GAGIIEDKLL QDKTSESWSR
     VVETKVLGLF HIQKYVRPES LRFLTVFSSV AGRYGNSGQL DYATANELLN RLCSQLNQLW
     KNKVVVRSLC WGPWGPTQFG EGMVTAETEA KFAEKGVALV TAKAGRDVFR EEILQQPSEN
     IEVICGIGPW EKHEATIGRV EFDESIPRIT GALLDNARVT AMPKGDQVVE FYLSDRHEYL
     QQHRIDNIPV LPAAVALEIM SETVTALWPG WHVVEARDSR LLKGLQLDDL NQKLKVVVNP
     PPYGSSDGFD VTVSLQSEKR MHYKAVLRLE QTYPESFTYE PEKHSDKQLS VETAYNEWLF
     HGPCFQVIKK IAGLSQQGSV SDVETSTPAG WLSTVMVDDG WVFDPAMTDA AAQMALLWGR
     TFNDQSALPA RFGKVMKFQE KLPEKLRMCF ARKESEQPNT IVSDVYFVDE KNNVALLIED
     LECISSMELN RLGGTEKLAL
//
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