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Database: UniProt
Entry: A0A1C4IGY4_9ACTN
LinkDB: A0A1C4IGY4_9ACTN
Original site: A0A1C4IGY4_9ACTN 
ID   A0A1C4IGY4_9ACTN        Unreviewed;      2219 AA.
AC   A0A1C4IGY4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SCD36106.1};
GN   ORFNames=GA0115242_103923 {ECO:0000313|EMBL:SCD36106.1};
OS   Streptomyces sp. SolWspMP-5a-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCD36106.1, ECO:0000313|Proteomes:UP000199131};
RN   [1] {ECO:0000313|EMBL:SCD36106.1, ECO:0000313|Proteomes:UP000199131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCD36106.1,
RC   ECO:0000313|Proteomes:UP000199131};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMCI01000035; SCD36106.1; -; Genomic_DNA.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000199131; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion 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; cd05195; enoyl_red; 1.
DR   CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.11460; -; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR036299; Polyketide_synth_docking_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   InterPro; IPR016039; Thiolase-like.
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; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 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; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCD36106.1}.
FT   DOMAIN          33..458
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2058..2133
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   COILED          4..31
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2219 AA;  233979 MW;  CC0BAD5F92C391EA CRC64;
     MSNEEKLRDY LRRSMAELRQ AQKRLREYEE GKQEPIAVVG MACRLPGDVS SPEDLWELVA
     SGTDAIVDFP SDRGWDLEGI YDPDPEVPWK STVRHGGFMR DVSGFDTEFF GISPREALAM
     DPQQRLMLEC AWETCERTGI DPASLRGTRT GVFAGVVQSY APQISRPPEE LEGFLLTGST
     ASVASGRVSY VLGLEGPAVT IDTACSSSLV TIHLAAQALR NGECDLALAG GVAVLSHPDG
     FAEFSRQRGL AADGRCKPFA AAADGTGFSE GVGLVMLERL SDARRNGHTV LALVRGSAVN
     QDGASNGLTA PNGPSQERVI RQALDAAGLT PDQVDAVEAH GTGTKLGDPI EAQALLATYG
     QDRSAEQPLH LGSIKSNIGH TAAAAGVAGV IKMILAMRHG VLPQSLHIDE PTPHVDWSSG
     AVSLLTERTP WPVTDHPRRA AVSSFGISGT NAHLILEQPP TTPGDTDVPA DADAETETDA
     EADTVVGGPH VWLVSGKSAD ALTEQAARLH AFAAARPEVG TGDIAHALAA TRTAFEHRAA
     VIAHDRAELL DGLSALQEGR PSPHLVTGPS DHRSRTASKV AFVFPGQGSQ WPGMGRELLD
     TSSVFRTHLH ACADALAPHV DWSLLDVIQE HPDAPSLDRI DVVQPVLFAT MVSLAALWKS
     HGVQPHAVIG HSQGEIAAAH IAGILTLDDA ARIVALRSQA LRQISGQGGM VSLPLPADQA
     EALIAPWSDR ISIAAHNGPH TTIVSGDTPS LEHLLATCAA QKIDARTVPS DVPGHSAHLE
     SVRDRLLDDL RDITPQPGHT PFYSTVTGAL VEDTLTLDTD YWYRNLRQTV RFSDTARTLV
     ADGHHHLIEI STHPVLTTSV QDILDTTDHH DTPTLTTGTL RRHKGDWNQF LSSAALVHAH
     GTTIDWTRHT VPVTGDLVDL PTYPFQHQPF WLTHTPAGAG DASAFGLEAA EHPFLTASLE
     LPDESRVFTG TLSLQSHPWL ADHAITGTPL LPGTAFVDLA LHTGHHTGHP HLEELTLHAP
     LLLSGPALDL QATLAPALDG RRALTVRSRP RSAAPDDTIP WTVHATATLT TTAPARETPD
     LTVWPPAGAT PVAVDSAYPF LAEHGYTYGP AFQGLTAAWR DDQHTYAEIA LPETGTVTGD
     AGTGAFDIHP ALLDAALHAL GLDALENGGD RSEGMRLPFS WSGVELYSTG ARHLRVRLTP
     TGDDTVGLVL ADAGGAPVAT VDAFTTRPLP PEQLAALGSR RSPSLPLFVV DWTAVPVAAG
     AAAPSVTWAT LTGRVVGTDS GFGQVPVAEL GATAYPDLAA LGAAIEEGAA VPEVVLLPHA
     SATDADSPVG GAHAAVRAVL PVLQEWLATE AFTASRLVVV TRNAAWGQSG ADTAISLADT
     PLWGLLRSAQ SEHPGRFTLL DIDDATSSLG TLTAALATDE PQLALRNGAV YAARLNRLDA
     QRVLSAPEGA AAWRMELEGA GTLDHLTLAA MSTGDVPLAA GEVRLAVRAT GMNFRDALIA
     LGMYPGEAAH LGSEAAGVVT GVGPGVAELA PGDRVMGLVP HSMASEAVTD HRMLVRMPDD
     WSFVQGAAVP VVFMTAYYGL GDLGRLGAGE KVLVHAAAGG VGMAAVQLAR HWGAEVFATA
     SPGKWDALRE MGFDDAHIAS SRTCDFEEAF LTATGGQGVD VVLNSLAREF VDASLRLLPR
     GGRFVDMGKT DVRDPAAVAA AHPGAVYTNF DLFEAGPDRI QEILTELLGL FEAGALRPLP
     VTAWDIRQAP EAFRFLSQAR HVGKMVLTVP RALDPDGTVL ITGGTGTLGS LLARHLVGQG
     VRRLLLVSRS GPRAEGAGAL REELTGLGAE VTVAACDTAD AGQLAALLAE VPAAHPLTAV
     VHTAGAVEDA TVEKLTLDSL DTVLLPKADA AWNLHTQSRH LDLAAFVLYS SAAGSLGSPG
     QANYAAANTF LDALAHHRQA LGLPAASMAW GFWEQASSLT QHLNTTDLSR INRNGIAPMS
     SAEGLALFDA ALASGRAGLV TARLNHAALR GSADRLPPFF QNLVKGGRRA LAGAAAESEG
     RGGLTERLAP MSDRQRDQVL VNLIRDQLAA TLGHTDPSAI ETDSAFKELG IDSLTAVELR
     NKLSASTGVR LPATLVFDHP TPSALARYLR EQLAPDLPEA EPPMLAELAG LESALAGLTE
     EPDEETHARI ALRLETVMTK WRQLRTVETA PVQDVARRME SASASEILDF INKELREKR
//
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