ID A0A0K2YRT5_9NOCA Unreviewed; 1660 AA.
AC A0A0K2YRT5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:CRK54364.1};
GN ORFNames=RHCRD62_90043 {ECO:0000313|EMBL:CRK54364.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK54364.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK54364.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK54364.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CVQP01000012; CRK54364.1; -; Genomic_DNA.
DR RefSeq; WP_050067295.1; NZ_CVQP01000012.1.
DR STRING; 260936.RHCRD62_90043; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000044872; 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; 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 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:UP000044872};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..78
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 98..522
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1171..1245
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1660 AA; 176578 MW; DC2734AF80BF5AA8 CRC64;
MTVAQLREWL RNWVAGVTGQ PVEQISDDRP MEEFGLSSRD AVALSGEIED LLGITLNATI
AYQHPTIASL ATRIIEGEPE LPAGSDDAYY AVKDTSQSHD IAIVGMASRF PGSGHTPDEM
WRLLIEGRDA VTDLPEGRWS EFAADPQIAA AIEKANTKGG YLDDVKGFDA EFFAMSPLEV
RNVDPQQRLA LELAWEALEH AHIPANELKG EQVGVFIGTS ANDYQLLAIS DPLQAHPYAL
TGTSTSIVAG RVSYYFDFRG PSIALDTACS SSLVAVHQAV RSLRSGESDI ALAGGVNMLV
APAATLGFNE TGVLTDDGKI KAFSSDANGI VRAEGGGLVA LKRLEDAERD GDTILAVIAG
SAVNQDGRSN GIVAPNPDAQ ADVLRAAYRD AGIVPSGVDY IEAHGTGTIL GDPIEADALG
RVVGRGRDAD KPALLGSAKT NFGHLESAAG AAGLIKVVLA MQEDKLPPSL NYAGPNPYID
FDGTHLRVIP EATDWPRYTG RAVAGISGFG FGGTNAHVVV REYNGAVAPE ASANESPSEA
TESLDAEHVD VETEAEAVLA DAAASMGVEP LVTPQREEPL PVLLPVSASM PSRRRRAASD
LADWLETEAG STTALADLAR TLAGRNHGRS RAVVLARTHA EAITGLRAVA AGKPGQGVFS
ADSPAGKGPV WVFSGFGSQH RKMAKQLYTN NAVFRAAIDQ VDELIEFESG YKMAEKFLDD
SLDYDVETSQ VGIFAIQIGL AALLRHHGAE PEAAVGHSMG EAAAAYVTGG LSLEDAVRVI
TARSRLMGEA EATLSGDDIR LMALVEYTAA EIEAVLGDFP HLEVCVYAAP THTVIGGPQP
EVEAIVARAE AEEKMGRILQ TKGASHTSQV DPILGELAAE LAGIEPHTLT VGLFSSVDKE
TYYRAGHAPI HPVDYWTKGM RHSVYFTNAV RMAVDAGHTT FVELAPNPAT LMSVAATAFD
AGLHDAQLIP TLKRKEDEEV GVLTALAQLY VHGQPVNLAS LLPAGGYANA PRTAFQRKEF
WLDVQVSASG SGRAPGSHVS LPDGRHVWEV AASAVSNLNE LVTSAAAQVL SDVTLTAAVP
RGDVPASGTL TTTLSPHPGG GSLQVHAKSN GAFTLLLDAV VSSGEALPEL VVAAPEPRTG
AASPQRSSSP MEELPEVVES FGDKWDPNGT QALEDRLALI VAESMGYAVE DLPAEIPLIE
LGLDSLMAVR IKNRVEYEFD IPQLQLQAVK DANLREVEKY LRYAVENREE VEALAAAQQA
EKDAPALDSV LDDETTSPVA EAEQIVADAA PTVGDASDEE VNVPPRDAAE RLTFATWAVV
TGKSAKGIFN ILPVLDDVTA EKLAARLTER AGGEVSFDDV LDSETVEQLA EKVRPHLEDE
GKIEGLVRVL RARPEGSTAV PVFVFHPAGG STVAYEPLLK RLPADTPMYG FERTEGPLDV
RAREYLPLIT EIQGDGPYVL YGWSLGGALS YAVATLLREQ GKDVRIVGLI DTVMAGEEIE
DTPDEIKKRW QRYAAFAKKT YNVDAPLPFD MLAAAETDEE QIEILMNLLK VSGAKIPGGI
IEHQRTSWLD NRALQTVKPG KYDGPVVLYM ADKYHDDAIA LEPAFGTRTP DGGWAKVASD
LEIVHVGGDH IQIVDEPYIG KVGADLTKKL AAIEAEKRSN
//
