ID A0A1X0USF6_9NOCA Unreviewed; 1661 AA.
AC A0A1X0USF6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:ORI25140.1};
GN ORFNames=BJI47_05955 {ECO:0000313|EMBL:ORI25140.1};
OS Rhodococcus sp. 1168.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2018041 {ECO:0000313|EMBL:ORI25140.1, ECO:0000313|Proteomes:UP000192546};
RN [1] {ECO:0000313|EMBL:ORI25140.1, ECO:0000313|Proteomes:UP000192546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1168 {ECO:0000313|EMBL:ORI25140.1,
RC ECO:0000313|Proteomes:UP000192546};
RA Nahar A.;
RT "Metabolic and lipid synthesis pathways analysis of sub-Antarctic
RT Rhodococcus luteus.";
RL Submitted (OCT-2016) 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:ORI25140.1}.
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DR EMBL; MKKY01000031; ORI25140.1; -; Genomic_DNA.
DR Proteomes; UP000192546; 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; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; NF040607; mycolic_Pks13; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000192546};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..96
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 118..541
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1169..1243
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 548..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1661 AA; 176582 MW; 6E7E427788491CCA CRC64;
MANHEIDAER VTDSSGAEMT VSQLREWLRN WVAEATGQPV AQISDDRPME EFGLASRDAV
ALSGDIEELM GVTLTATVAY QHPTIASLAT RIIEGEPDVP DEAADDAYYL QAKGPGSSHD
IAIVGVSTRF PGAGHTPEEM WTMLSEGRDG ITDLPEGRWQ EFTSDPVIKA AVDATVTKGG
YLDDVKTFDA EFFAMSPNEV VNVDPQQRLA LELTWEALEH ARIPASSVKG SQVGVFIGSS
SNDYQLLAVS DPAVHPYALT GTSTAIVANR VSYFYDFRGP SIAVDTACSS ALVAVHQAVR
SLRDGESDLA VAGGVNMLLA PPITVGFGQT GVLAPDGKIK AFSSDANGMI RSEGGGLVVL
KRVEDAERDG DDILAVIAGS AINSDGRSNG LLAPSPDAQA DALRFAYRDA GINPSGVDYI
EAHGTGTILG DPIEADALGR VVGRGRSEDK PALLGSAKTN FGHLESAAGA AGLIKVVLAL
QHNRLPASLN YAGPNPYIDF DKAHLKVVSE GAEWPRYTGK AVAGISGFGF GGTNAHVVVT
EYVKAVPEAD GTEDAPAEAD THPPVSNVET TDPVAEAEQI LEESVPQTVV LAVSAALPSR
RKRTASELAD WLETEAGSIT PLADVGRALA KRNHGRSRAV VLASTHAEAI TGLRAIASGK
PGQGVFSADS PASNGAVWVF SGFGSQHRKM ANALYRNNAT FAAAVDDVDE LLLDEAGYSI
KEIILDDSQN YEFENSQVAI FVIQVALAAT LRAHGAEPSA VIGHSMGEVA AAYVVGGLNL
EDAVRIIYAR SRLLAEGQEG LGAASQGAMA LVEYTPEEVT ALTDQFPDVE PCVYAAPTHT
TVGGPRGQVE ALVEMAEAAG KMARILDVKG AGHTAAVDPL LGELAAELAG IEPGKLRAGV
YSSVDKQTHY RAGHEPIHGV EYWTKGMRNP VYFTQAVNVA VGDGHTTFVE LAPNPVALMS
IAATAWAAGV ADSTLIPTLK RKEDESETFL AALAQLYVHG HSLDLTTLFD DGDYAAIPRT
SYLRKEFWLD SRVNSSGNSH VPGSRVALPD GRHVWEVQAS ALGSFDELVK AAASQVLSSV
ELGYSVSHAA VPKIGTVVTA VTSHLGGASV QVHAHQGSAF TLLHEAVVTS GDPLPEPVVA
VAQSSTSPME ELPEVVETFG DRWDANGNQK LEDRLAIIVA ESMGYAPEDL PPEVPLIELG
LDSLSAVRIK NRVEYEFDIP TVQLQAVRDA NLLEVEKYLR YALENREEVA ALAEQQAAEK
EAEARDSVSP AAPVEAAPDT TPAVAQTDSM SDLGGKEGFA EAAGSDVPPR DNAERMTFAT
WAVVTKESAK GIFNTLPILD DEVAEKLAAR LSERAGGEVT FDDVLDSETI EQLAEKVRPH
LEGGEIDGVV RNLRARPEGS TATPVFAFHS AGSSTVAYEP LLRKLPAGTP MYGLERVEGP
ISVRAAEYVP LIRAIQPEGP YVFVGWSLGG ILAYEVARQM EEQGIEVAYI GLLDTVMPGT
EIPDTRDEVR KRWERYAAFA KKTYDVDYPI PYDKLVEADD EGQIRIITDL VKLSGAKIPG
GIIEHQRTSW LDNRAIQTAE LKPYGGPVTL YMADKYHDDA IALEPAYATR EAHGGWGPVV
KNLEIVEIGG DHLAIVDEPY IGRIAAHMTK KLEEIESGAK P
//
