ID A0A260X644_9NOCA Unreviewed; 1580 AA.
AC A0A260X644;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:OZF56641.1};
GN ORFNames=CH292_03140 {ECO:0000313|EMBL:OZF56641.1};
OS Rhodococcus sp. 14-2470-1a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2023150 {ECO:0000313|EMBL:OZF56641.1, ECO:0000313|Proteomes:UP000215821};
RN [1] {ECO:0000313|Proteomes:UP000215821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14-2470-1a {ECO:0000313|Proteomes:UP000215821};
RA Savory E.A., Fuller S.J., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA Grunwald N.J., Chang J.H.;
RT "Evolutionary transitions between beneficial and phytopathogenic
RT Rhodococcus challenge disease management.";
RL Submitted (JUL-2017) 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:OZF56641.1}.
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DR EMBL; NPFZ01000005; OZF56641.1; -; Genomic_DNA.
DR Proteomes; UP000215821; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08952; KR_1_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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; IPR041618; PKS_DE.
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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 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; PF18369; PKS_DE; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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; 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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 43..455
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1427..1502
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1580 AA; 166162 MW; 55ECA9B5FFFFE801 CRC64;
MADSTPTTEV TNRDSKLREY LERATNELER TRLQVRELQD REHEPIAIVS MACRYPGGIR
TPEDLWRIVD EGIDVVSEFP VDRGWDVESL YHPEPGRTGK SYVRHGGFLH DAADFDAAFF
GISPKDAPGT DPQQRLLLEV CWEAFERAGL DPTAMKGSPT GVFMGLMHHD YVGGTISGSI
VSGRIAYTLG LEGPAVTMDT ACSSSLVALH SAVQALRRGD CSLALVGGVA VMASPEMFVE
FSERRALSSD GRCKSFSADA SGAAWAEGAG VLLVEKLSDA RRNGHEVLGL VRGSAVNQDG
ASNGMTAPSG PAQVRVIRQA LADGQLAPNQ VDIVEAHGTG TTLGDPIEAQ AVLTAYGQDR
PADRPMWLGS IKSNMGHPQA AAGVAAIIKM VMAMRHETMP RSLHAHNPSP AVDWTRGNVE
LLAEPQPWPS EGRPRRAGVS SFGISGTNSH IIVEEAPPVP VADTSEVVGA VPVVPWVLSG
RSPEVVRIAA RRLREQLQDS ISRGDNVDAL DVGFSLATTR AAFPYRAAVV GRDVPTLLDD
LDEIVTGQRE ASAVTDSTRT AFLFSGQGSQ RAGMGKVLRQ GFPVFAAALD RICAEFDPHL
PEPLQDVMFA ENPDTLARTR FTQPALFAFE VALAEQLAHW GIRPDIVAGH SIGEIAAAHV
AGVFSLTDAV TLVAARGRLM DGLPSGGAMI AIAASEAEVH PLLVPGLDIA AVNGPRSVVV
SGDEDKATAL AAQFDKTNRL RVSHAFHSHL MDPMLDEFRS TAASLHYYEP RIPVISDVTG
DVAEGLSDPE YWVRHVREAV RFADGIDSVV REGADTLIEV GPDAILTGMA ADTAPQMVAT
QRRDQDEDQA LVATIAALHS AGHRIDWPAV LAGGRRVGLP TYPFQRTRYW ENVTSMLVPA
PRDESETFWE LVREQDVSAM AATLGIDDQE SLATLVPALS RWHDRRSSAA ASDDLCYRIG
WSQIATEHNE SGAWRVAILA LGGSVADGEL AAALRRRGAD VVTHLVNGST RAEFAAELSA
VASIDEIVVD SGPSATVPVV SALVQSLEDI GAAARVRIVT HDAVAHEISA RVEGYVAGAL
WGLGRVIGVE LPDRWAGLID LPSDASPRVF DRAAELVTAG GDEDQVAVRE SGAFGRRLER
AGARTGPAWT PTGTVLVTGA SGALGENLAR WLAAQGAPRI VLASRRGASA PGTSALIAEL
DGTDVSAVEC DVTDRAALAD VVNDIGDPHP LTAVFHLAGV LDDGVFDALT PDRFEKVIAP
KATAAQHLHE LTADLNLTAF VLFSSFSAVV GGAGQANYAA ANAALDSLAE HRRGAGLPAT
SVSFGPWGGD GMADSHVVRD TGRALGIDPI VPAHALTALK RAIETGETLL TVVDVAWNTF
VPAFSALRPS PLVAGLADVA APGGAAAAEV PSIAGELSRM SGPERDRALL DLVRSEVAAV
LGYGGPGDVE PGLAFKDLGF DSLTSVDLRN RISSACGVQL PATLVFDYAS PAALADHLAG
ELGEPASGAD VVLAELDRLE AMIGSLGAED LEQARVTARL QSILSGATAA LAGTTASTTT
LDDASADDVL AFIDNELGAS
//
