ID A0A136PQ13_9ACTN Unreviewed; 1565 AA.
AC A0A136PQ13;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Thioester reductase {ECO:0000313|EMBL:KXK60532.1};
GN ORFNames=AWW66_18415 {ECO:0000313|EMBL:KXK60532.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK60532.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK60532.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK60532.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-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:KXK60532.1}.
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DR EMBL; LRQV01000068; KXK60532.1; -; Genomic_DNA.
DR RefSeq; WP_067367785.1; NZ_LRQV01000068.1.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000070620; 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; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
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:SF37; FATTY ACID SYNTHASE; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 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 SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000070620};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..473
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1441..1516
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1565 AA; 169541 MW; F0A8BF64C1337201 CRC64;
MSSVKDFILE QFVNKQIDRD RTKRLLLELS EANLHEDIAV IGLAGRFAEA TNVDQFWEFL
KVSRDCIRDY PQSRKEDMYD ILRNPYYAEV MLGRPVDEAD LDRLYSVSGY LDRIDHFDSR
FFGIPPLEAD YMDPNQRIAL EVAYEALENA GYGGESAIGS RTGVFLGRDQ SNYSYYRMFS
ERHPMQLSGS WEGMVASRIS YLLDLKGPCI MTDTACSAGS VSVHQAIQSL LLGECDMALA
GGINLSSGGE PKTSFLSGAT MDNVVSGDDI VRTFDAQANG TLWGEGAGIV LLKPLKKALA
DRDHVRAVIK ASAVNNDGTS NSITAPNALM QERVILDAWA KADVPAETIT YVEAHGTGTV
LGDPIEVKGL TNAFRRHTDR RQFCGIGSLK TTMGHMVAAS GSASLAKVVK SLESGLLAPS
ANFDVPNPYI DFTDSPLYVN DRLMPWDTNG EPRRAGISSF GFIRTNCHMV LEEAPRYRAG
QQLRERYCFT VSAKTEAALM ALLDGYAAVL ADSPWSLADI CYTSNVGRGH HEHRVMVIAA
TKEQLAESVD RLRRRGLGTD ERQGIHHGVH AVVSDKRTDL GPGDITAQTG KRLSDSANAT
LAEYRSRGDA AALTALADAY VRGARVDFAA FYADEPRQRV PLPTYPFEKI RHWAKPMRTS
VRSFGGAETN PLLGAEISRS DTAIVFENTL SVDRHWVLSD HRIEHRPVVP GTTYLEMARA
ALAAVENTGS MRFDNVFFLV PLAVEEGEEA TVRTRLDRLE KGYSFQVSSS QDGEWVTHVE
GRISPLGDAG PAAPVDLDAQ KRAAIEVTDP YPTETDTGVF QFGARWDNVR AVWKHETGAL
TLLRLPQGVS SETFGLHPAK LDNAVNLISQ NSGETFLPYM YKSFVLHRPM PETFYSLIRT
VRDDSHEGET ITYDVDLVDV DGEPFARITD YTVKKVDWQR FSLAGPRRFL QVDWLAVPRV
AAEATGGAVW APVVRDNPAG RRLVAAVEAQ GHRVVPCYVG ERTDPGRDVF ALDEAGAGLL
AQRLRQEGVD GVLFATDVTA PAATGEAALT PGQRRAAGVD ALFELYRAFV TSRVKLTRGL
KVLGSQAWQV GPDDGATDPF SAATESLAQV IGQEHRHLLV DVLDAGTDVD LDFLLREALA
GSGGVLRAVR GSQTYLRRLR YVETADATGE SPYRGGTFLV TGGAGGLGLS VAEEMAHEGA
ERIILLGRRP LTEETARRVE KIAGAEYVEC DVSREADVRG LAARLREEAV TLGGIVHAAG
VAGDGFLANK PRPVFDAVLA PKVDGSLALV ELAKEHPGAF LVFFSSITAI TGGQGQGDYC
SANAFMDSLA VRARAEGVRA LSINWPTWSE VGMAVQYGIG DGDSPFRALT VKDGLAWLSH
FLRDPADGVI PTRFDLGVLH DRLDEMPFLL DDDVADAVAR AGAGGSSSDG ETTEVRVVGL
SDPNQTQLRI GAVYGAVLGM AEVDAHASFQ DLGGNSLMTA QLLQRVEEVY PGRIDIADLY
SYASVASLAG YIDERIAAES GPAEPDPADV GDIDQSLQDV LAEIGDAELT TMFAADADGA
GRNQA
//