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Database: UniProt
Entry: A0A366D5P5_9NOCA
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ID   A0A366D5P5_9NOCA        Unreviewed;      2065 AA.
AC   A0A366D5P5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Thioester reductase-like protein {ECO:0000313|EMBL:RBO85350.1};
GN   ORFNames=DFR74_115199 {ECO:0000313|EMBL:RBO85350.1};
OS   Nocardia puris.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=208602 {ECO:0000313|EMBL:RBO85350.1, ECO:0000313|Proteomes:UP000252586};
RN   [1] {ECO:0000313|EMBL:RBO85350.1, ECO:0000313|Proteomes:UP000252586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44599 {ECO:0000313|EMBL:RBO85350.1,
RC   ECO:0000313|Proteomes:UP000252586};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) 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:RBO85350.1}.
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DR   EMBL; QNRE01000015; RBO85350.1; -; Genomic_DNA.
DR   RefSeq; WP_067514186.1; NZ_QNRE01000015.1.
DR   STRING; 1210090.GCA_001613185_06620; -.
DR   OrthoDB; 4516163at2; -.
DR   Proteomes; UP000252586; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR   CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   CDD; cd05235; SDR_e1; 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; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
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; IPR013120; Far_NAD-bd.
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; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08990; Docking; 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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 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; 3.
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.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252586};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..457
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1589..1664
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2065 AA;  216511 MW;  CF13A47390E8ED5F CRC64;
     MSEDKKLVDY LRWTTAELSK ARQRIAELES DAPESIAVVA TACRYPGGVN SAAALWDLVE
     NGVDAISEWP ADRGWDVDAL YDPDPEHVGT STTRHGGFID HATDFDAALF GISPREALGM
     DPQQRVLLET AWELFEAAGL DPAALRGSRT GVFVGAGEQT YLDLAAPPEL EGYSMTGKLS
     SVVSGRLAYT FGLEGPAITV DTACSSSLVA LHLAAQSLRR GECDRAVAGG VTVYGHPGGY
     IEFSRQRGLS PDGRCHSYGA GASGTGWSEG VGLVVLERLS DAVAAGREVL GVLRGSAVNQ
     DGASNGLTAP SGRAQEGVVR AALVDARLSG GGVDVVEGHG TGTRLGDPIE VGALQATYGR
     ERPEGRPLYL GSLKSNIGHS VAAAGIGGVI KMIEALRRGV LPKTLHAEAP NPHIDWSSGS
     IELLTEAREW PRTGEPRRAA VSSFGVSGTN AHVILEQAPE PAPAPPDPVT VTLPAVPWLV
     SGKTRDAARA QAERLREFAA SAPDLRPLDI AYSLATTRAA LDHRVAVVGT DHAELLAALA
     ESEPVTTTAG KTAFLFTGQG AQRAGMGIEL YRRFPVYAAA FDEAHEHLAP LLDRPLRDTI
     ESGDRLDDTA ITQPALFAVE IALARLLESW GVRPDFVAGH SVGEIVAAQV AGVLTLPDAA
     ALVAARARLM STLPRGGMLA VRADEEEVRA DLPDGVNVAA VNAPGAIVLS GGIEELDTLA
     GVLNARGLRT RRLAVSHAFH SHHMDPILDN FRSVAGRIDL KRARIPLVSN VTGAVAAPDA
     HADPGYWVRH IRDTVRFADG VRALADAGVT KFVEIGPDAI LSALTDDTLQ DRAHVSIPVL
     RRTAGDAATV VSSVAAMHNH GITVAWDKVF EGAGARRITL PTYAFQRSRH WAGDSVTTVS
     GLGPSVGHPV LDVAVDLADG AGVVVTGRLT RRHRGLVTGT AVAPGVLVEL AIRAGDELGC
     TELSVLTVLA PLTLPARADL HIQARVGAAS ETGEREVSIH SRPGGSAGPW TLHARGSVRL
     RIGEPGFDLT QWPPPGGQFA EVELPEDISA DSPAYRLHPA LLDVALAAAG EGTPTEFREV
     RLLSTGAAAL RVLVERDDDG RTTLFLADRA GAPVATIGGV TFGAPVAINA PRPSLADMVF
     RVDWVPAGIA DRPVRWGVLR GAGAVPEIGE PTLFTDLAEA ATADKPVDAI LAPLDAERAD
     PAADARDLTT RALLLLQQWG AVEERTAAPL VVLTRRAAGP DAANVAAGAV WGLVRSAQSE
     RPDRIVLADL DDEPASLEAL SAVVGAGEPQ VVVRAGRVFV PRLTRAALPT PRDAGPEECV
     LITGGTGSLG AALARHLVGE RGVRRLVLVS RRGTDSPGAA ALRAELSATG ARVDIAAADV
     ADRDSLAEVL AAHPITGIVH TAGVTDDGLI ADLDPDRLAA VLRPKADAAW LLHDLTRDRD
     LTSFVLFSSV AATIGGPGQG NYAAANAFLD ALAGHRAGLG LPATSIAWGL WEQEGGISGH
     LDAADKERIA RGGFPPLAAD DGLALFDALA AGGEAAVVAT PLDVSAIRAR PTTLLSGLLP
     TQRASAGNAA APAALADLLA DRTPDEQHAL VLETVLREAA SVLGHRGDDA LDPARPFSES
     GFDSLATVEF RNRLQRALAV RLSASVAFDH PTPQALAAHV LDQWRDGRSG AATTVDYRAE
     VLLADDIRPA DTVVQVAAGP EHILLTGASG FLGAFLLRDL IRTTSATVHC LVRGADEADA
     TRRLLANLDF YRVTDEVDRD RVRVVAGDLA APRIGLSDTE FDELARRIDV VYHAGATVHW
     LRPYESLRDA NVAGTEEILR LAARHRTVPV HYVSTVGVFA GAPEDGRALA VDDPTGPAEA
     LPSGYLRTKW VAEQRIEAAR DRGLPVSVYR VDVISGDQRH GACQTRDFVW LTLKGIVQAQ
     AAPAVPGGFF HLAPVDFVSA AIVEMAGRPE AAGRTFHLHN PSRVALPELV DRLRALGYSI
     ADREHAEWAE AIGASGDNAL VPLLDAFQAM IADTGAFYPA IDVSDTLAAI EGSGIECPPI
     TPELFATYVR FFIESGHFPA PAAAL
//
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