ID A0A0D0KE92_RHIRD Unreviewed; 2487 AA.
AC A0A0D0KE92;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KIP97611.1};
GN ORFNames=RU07_23640 {ECO:0000313|EMBL:KIP97611.1};
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358 {ECO:0000313|EMBL:KIP97611.1, ECO:0000313|Proteomes:UP000035017};
RN [1] {ECO:0000313|EMBL:KIP97611.1, ECO:0000313|Proteomes:UP000035017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEJ076 {ECO:0000313|EMBL:KIP97611.1,
RC ECO:0000313|Proteomes:UP000035017};
RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT draft genome assemblies.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:KIP97611.1}.
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DR EMBL; JXQV01000054; KIP97611.1; -; Genomic_DNA.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000035017; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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; 3.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; 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; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 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 SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..422
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2374..2448
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2487 AA; 265151 MW; 56A1780CEDDC3130 CRC64;
MTVEILGRAC VAPSAQNVEQ LFELLRQEIC AVSIIPDERW AKARFWHPMR GMPGKAYTFS
AGVLADVYDF DPTMFGISAR EASYMDPQQR ILLQTVWRAL EDASVSLAEL QRERVGVYIG
ASSLDNGNLQ IEDPASGGPH FMTGNTLSIV SNRISHILGL NGPSMTIDTA CSSSLVALHQ
AERALRDGEI DTAIVGGVNL LLHPFSFIGF SQARMLSPEG LCRAYSNDGE GYVRAEAAGA
VVLRRTDRAL SEGSRSRATL VASGMNSAGR TNGISLPSRE AQAQLLRSIY NDNGIDPESL
AFIEGHGTGT KVGDPAELWA IGSVLGRARS QPLPIGSIKS NIGHAEPASG VLGLIKAILS
FENNYLPASL HAETLNDNVD FAGLNVEVNR AGRVLAQGSE RRLAGVNSFG FGGTNVHVVI
SDPASAAKDG VEDKGGVFTL TAHTQSALHA LLEEYDARFA ASSDTQKAAL ISATRNRSML
KHRFVAAGKS ALDIANAVSS YLNDGHNADS QIGEVPGRTI QTAFFYAGNG SQWAGMGIDA
YRENSEFKTR FDHFSQLFSS RAGIEITELL FADDLDQQLR DTRIAQPLLF AVQAALTDCL
ISYGVKPDLV FGHSVGEVAA AYAAGILSAE DATTIVSIRS KHQHALAGMG TMAAVAMSET
ASVAFAQRYG LDNIKVAGTN SHNSVTISGP VDEIKAFKEA AQATRNAVHI LDINYPFHHP
LIDGERDAFL AEIPSVTPKR GHTTFISTVT GAEIHGERLD AEYWWRNVRE PIAFESAVNV
ALEFGCNLFM EISPRSILSS YVTETAKQLS ASAVVLPTLT RPGVGEGVDP VKRSALRAIS
HGAKIEDVEG RARGITGIDL PPLPFENATY RPHPTSDGIN VFGRDGADGP YTLLGWRTDP
NASVWKNHID ALLFPDLAGH VVDGKSIIPG SAFIEIAVQA ARGYYGTEEV EINNLEIFRP
LELRDSRMSE LLTRISPETG VIEIASREYM SEDGWTIHAT ARSRISVGLS RKAELNIGDF
GKAYAISAAE AYETARRFGL DYAPCFQLLE RAEVFGDRHI VVSLLPAASP AHPYLSYGMD
PVSTDAAFHG LVALFGSLTG EIDGAPYIPV RFGAVRTASS GQPIASAVIQ IERFSANSLK
ARIELLAEDG SLVAALDDCR FRRTWLRQHS TLDTVAFHYE AVARRQLAPN PSSAMTATSL
AGIFPSIPQA QADEATLLLD ASVQRACHDI ALVLTGQNGT VSVSSLPGDP AFQCFLSSCL
YTLEDAGIAQ FTDAGWTIPP DSELPPLGEL LNEIYRRFPE RVAETVLINN AYRETLERVA
AKFMVAPQPS SFLSDATLDH VRHHTAIGRR REEFVISAVK SALADVVPGD GVTIVELGAV
SMAFSSRLAD MAALKGARLV VIEPSDHLRR TLEIGFERNP SVDCLAPDAA GTLDTADFVV
SASGSLYGQF RQHSGLKDVL RIAASSGGRV AIAEAPSSAL SDFVFGFTEN WFADSATPEF
PTGQFASAIH WEDLLKECGF DAPNVDQPEL AEGGLLLVQA KSTMCNRSDK VIAPGSASIF
ELLQSEGDIP LLPLGFSKTL LCPPDEPRAA FDSLFAESLA YPLAFMCTLP KEPSDSAGLQ
DIIATLSAFA ETARAQARAQ NVARIRLLIV AAGGSPAASD QADPTASGLW TFARVLQNEY
DEFDVFLLDA DTQGPTISNA VLSLLAYDGL EREWVSSSRT GVLSVVRAVP GHVSEAGRKV
TTFEAATIHQ HTSGRVDSIV WTQDKVPVPN DGEVVVKVAA TGLNFRDVMW SMGLLPEEAL
EDGFAGATIG MEMAGTVVAI GSSVTDLSVG DAVMGIGPKA FSTHMVVARD GVTKVPQGID
PAAAATVPVA FLTAYYAMVE LGRIREGETI LIHGAAGGVG LAALQIAKLK GAKVIATAGT
VEKRRFLTLL GADHVFDSRS LAFVGDVLRV TDGEGVDLVL NSLFAEAMER SFELVKPFGR
FLELGKRDYY SDRKLALRPF RRNISYFGID ADQLLVRAPD LTRRIFADIG TLFSDGKLTP
LPYRAFNYDE TGAAFRLMQN AGHIGKIVVR PPVQGQDHVQ VFSDALLTLQ PGVYLVIGGI
GGFGLETAKW LVSRGATHIA LSTRGGVADH ETLDAIAAWK ASGVEVTLHA CDVTIEASLE
ALLVELRSYG PIKGVVHAAM VLNDGLISNL DREKNRAVID VKAVGASNLD RLTRADDLEL
FLLFSSATTM IGNPGQANYV AANGYLEGLA RARRRAGLPA LAIGFGAIGD VGFLARNTNV
SDILSRRLGK AVLKARAALS FVERVIVNDA GTVDQAAIMI AELDWASASA LPITAQPLFS
AIPRNAAGGA SGGDGDQIDL AALVAGKSHE EAHAILHGFL AGEIAAILKV AEDSVKADKV
LKDIGLDSLM AMELGVGFQQ KTGIDIPLSG MGDGATVGDI VQKLYEKVTA DVNADDTGDD
ANSASLVEQL TDKHTATVTD KKLGNNG
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