ID C6WK75_ACTMD Unreviewed; 3670 AA.
AC C6WK75;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Acyl transferase {ECO:0000313|EMBL:ACU38288.1};
GN OrderedLocusNames=Amir_4442 {ECO:0000313|EMBL:ACU38288.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU38288.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU38288.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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DR EMBL; CP001630; ACU38288.1; -; Genomic_DNA.
DR RefSeq; WP_015803175.1; NC_013093.1.
DR STRING; 446462.Amir_4442; -.
DR KEGG; ami:Amir_4442; -.
DR eggNOG; COG0300; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_000022_35_8_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000002213; Chromosome.
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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08956; KR_3_FAS_SDR_x; 2.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; 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; 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:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 2.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACU38288.1}.
FT DOMAIN 33..460
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1778..1853
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1875..2288
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3526..3601
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1006..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2868..2904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3147..3190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3216..3257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3234..3252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3670 AA; 376787 MW; 3E8E88E4BA6490A5 CRC64;
MAEADKLREY LNKVTVQLKQ AKGRVRELDA AASEPIAVVG MSCRYPGGAH DPDGLWELVA
SGTDAVTGFP TNRGWDLEAL YDPDPDRPGT SYLRESGFLH DADEFDADFF GVSPREAQAM
DPQQRLLLES AYSALEDAGL APGALRGSDT GVFVGVMAQE YGPSLLTPSV AEADGYLVTG
NQLSVASGRI SYTLGLEGPA VTVDTACSSS LVAMHLAAQS LRNRECDLAL AGGVAVLSTP
GFFVDFSRQR GLAPDGRCKS FAAAADGTSW SEGVGVIVLA RLSHARRLGY PVLALIRGSA
INQDGRSSQL SAPNGPAQQR VIRAALAAAR LGPSEVDAVE AHGTGTPLGD PIEAQALLAT
YGRGRPGDRP LWLGSLKSNI GHTQAAAGVG GVIKMVQAMR RGVLPATLHV DEPTPEVDWS
SGGVELLRES RPWPEVDRPR RAAVSSFGIS GTNAHLILEQ APEPEPAPRE LPEVVPWALS
GHTEAAVRAQ AARLAEHAAR PDADHPADVG HTLALGRDLL DHRAVVAGDR AGLAEALADL
AAGRADVHRA RPVRTALVFP GQGAQWEGMA EGLLETAPAF RAALDECDAA LSRHVDWSVV
DVLRSAPGAP GLERVDVVQP VSFAVMVALA ALWRSVGVTP SAVVGHSQGE IAAAVVAGAL
SLEDGARVVA LRSALIAREL SGRGGMLSLA VSREEAEELA GGLVEVAVVN GPASVVLAGD
PEALAVVAAR CAERGVRHRV LPVDYASHSA HVERIADALR AELAGITPAV ADVPFYSTVT
AAPLDTGGLT ADYWYRNLRL PVLFADTARA VAADLGNAAF VEVSTHPVLV SSLEDVLAGE
PVAALGTLRR GQGDLARFLT AAGHAHSLGV EVDWGAAHGA DPRRVRLPGY PFQRSRFWLA
ADRSSGDPGG LGLTATGHPL LTAALPAATG GDVLLTGRIG VATHPWLADH AVRGAMILPG
TALLELALHA GGHAGLPVVE ELVIEAPLDL AEPRQLQVVV RAGADGTDGA GGTDGAGGAG
GSDGAGGSGG ARVVTIHSRA GDGPWTTHAT GVLGPERAGE PDGLDRWPPE GADPVDVTGA
YPELAERGLG YGPAFRGLTA AWRRGGELWA EVELTADPAG FGVHPALLDA ALHLHAHQGA
TDEVRLPFSW RGARLHAVGA TRLRVRLTPL GDGAIAVLAV DPAGSPVLTA ESLTTRPARR
VDATGDGRGL LLEELWLPVD PPRPDAAPDR ADGVSEVDDD APGAVVLWRS PDVDGDDLPA
AVRRSVGRAL DVVGRFLAEE RFAGSTLVVA TRAAVAARPG DRVEPAAAAV WGLLRSAQSE
HPGRLVLVDD PDEPDAARWA VAGLPQLAVR GSAALTPRLT GVTPSSTPTG VPTGVPTGIA
SGTVPGIASG IASGTAPGTV PGIASGTSTG AAPGEAAGIA PGTAPATSTG AVPGIAPGAV
PGEAAGTPTG IAPGASTGTA PGTAPGDAPS TVPGVAPGAP TSVVPGEATA PAAPAAPDPW
SPDTTVLITG GTGALGALLA RRLVAARGVR HLLLTSRRGP DAPGAAELVA ELTDLGAHVR
VVACDTADRE AVRALLAGLD RPLGAVVHTA GVLDDATFDA LTPERVDRVL RAKVDGAWHL
HELAAGVGAF VLYSSLAGLI GTPGQANYAA ANAALDALAR HRRDRGLPAT SLAWGLWAPA
GGMTGHLGDA DRARLARSGL LPITAEAGLA AFDAALAADR PVLALTPLDR SALRAADPDT
LPVPLRGLVP RAPRKAAPGD ATGFAERLRA LTDRGRRAAL LDLVRGHVAN ILGHADPAAV
PEEQAFRDLG FDSLTSVELR NRLTRATGAR LPATLVFDHP TPAALALFLG SALGVDDPAR
ATGAGDRAVR AAAPDEPVAI VGMACRFPGG ADTPDLLWDL LVDGREGLSA FPADRGWPDR
VGAGLGGFLP GAADFDPAFF GISPREALAI DPQQRLLLET AWEAMESAGI DPTTLRGTGT
GVFAGAMYRD YSGRFTGADG YEDVLGAANA GGVLSGRVSY ALGLEGPSVS IDTACSSSLV
AMHLAAQALR GGECGLALAG GVTVMATPDT FAEFSRQGNL APDGRCKSFA EGADGTGLSE
GVGLLLLERL SDAQRNGHRV LAVLRGSAVN QDGASNGLTA PNGPAQERVI RAALATARLE
PSEVDLVEAH GTGTTLGDPI EAQALLATYG QGRDADRPLW LGSVKSNLGH TQAAAGVAGV
IKVVQAMRHG VLPATLHVDE PTSEVDWSSG GVELLRHNRS WPEAGRPRRA AVSSFGISGT
NAHVVLEQAP EAAGPEPDRD LPDTAPLVLS ARTTGALRAQ ADRVAALLDA RPDLPVADVA
LSLATTRTAF ALHASVTGAD RADLVGGLRE FAGAGTGSTA SAGGLALLFS GQGAQRVGMG
LGLRAAHPVF ARAWDEAMAA VEAEQPGPVP LREVLEGRPD LVDRTDYAQT GLFVLQTALF
RLYESWGLRP DRVIGHSVGE IAAAHVAGVL SLADAARLVA ARGRLMAGLP PGGAMIAVEA
TEDRLRPLLE GEPLLGLAAV NGPTSLVVSG DRARAEAVAA RVAELGGRTR PLRVSHAFHS
PLMAPVLDDF RAVLDDLAYR RPDTTIVSTV TGAPVADDMS GPDYWLRHVL ATVRFHDALT
APGERPLSAH LELGPDGVLA AQAGRVLDGQ VVTHALRAGQ DEARTATAAL GELRRAGHEP
DWSRVLPGAR TAPLPTYPFQ RERYWLAGAR PAATPSAVGQ QPAHHPLLGA AVPLAGDGTL
VLTGRLDPDA PGWQADHRVL GRVVLPGTAL LDLVLHAAGL VGAGVVRAGV VDAGPVGATV
LDELLVETPL ELDGPRQVQV VANGAAGWIR VHSRPEEPDA EWVQHATATT TTAERSAPPE
PGGQRPGEQR PGEQWPPTGA TPLDPAALRA DLADRGLDLG PAFLGLRAAW RRGDELFAEV
AADDRAGEDR AGDGRAGHTV HPALLDAALH PAAHAGTGLR LPFSWNGVRS HATGARALRV
RLTELGEGAV SVRAEDPSGR PVLTVDRLTT RPVDAAGLTG RPRTTGAVHV LAWRPLATPV
GAHPEPAVVA APETGDGGPA AVREALRVVL TGVARALAEP TGTAVVLTRG AVAVDDGESP
DLAGAAVWGL VRSAQAEHPG RLVLVDADPA PAAGRPPAGS TPAGSTPVES SGGPGADHDP
GPTGGLPSGL DLAALVATGE PQIAVRSGRA HVPELVPAPA GHARQGDSPT EDAPPTEHPT
PTEHPTPAGH PTPTAPWTER SRVLVTGAAG ALGSATARHL VLAHGVRDLV LVGRRGVPEE
LVAELTGHGA TVTALALDVS DRDRVAALVA EHPVTAVVHA AGVLDDGVLT ALTEERFDSV
LRPKVDAAWH LHELAGPVEQ FVLFSSVAGL LGGAGQANYA AANAALDAIA THRARLGLPA
RSLVWGPWTG GGMADRLAAA DRDRLRDRGL LPITEVAGAA LFDAALRCPA PVVVLAPLDR
AATRSGPVPP VLRALLPAAP RRAAEPADHT DLADRLRALG ERERDHLLLG VVRSHVASVL
GHRDPSAIDR DEAFTDLGFD SLTAVELRNR LADGTGLRLP ASLVFDHPTP AVLVKFLRAR
LTPDAADVVR LKVAEVEALL SGAELDARAK DEAASRLELI ARRWRGSAQP DLDGASDEEL
FRLVDATGKD
//
