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
//