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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//