ID A0A1M7QZC3_9ACTN Unreviewed; 1667 AA.
AC A0A1M7QZC3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Polyketide synthase 12 {ECO:0000313|EMBL:SHN37286.1};
DE Flags: Fragment;
GN ORFNames=SAMN05216499_1513 {ECO:0000313|EMBL:SHN37286.1};
OS Actinacidiphila paucisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310782 {ECO:0000313|EMBL:SHN37286.1, ECO:0000313|Proteomes:UP000184111};
RN [1] {ECO:0000313|EMBL:SHN37286.1, ECO:0000313|Proteomes:UP000184111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2025 {ECO:0000313|EMBL:SHN37286.1,
RC ECO:0000313|Proteomes:UP000184111};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FRBI01000051; SHN37286.1; -; Genomic_DNA.
DR STRING; 310782.SAMN05216499_1513; -.
DR Proteomes; UP000184111; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd05195; enoyl_red; 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; 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; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_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; 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; IPR020843; PKS_ER.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF21089; PKS_DH_N; 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; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000184111}.
FT DOMAIN 33..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 462..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1667
FT /evidence="ECO:0000313|EMBL:SHN37286.1"
SQ SEQUENCE 1667 AA; 174025 MW; 6F2DC1543B335FFE CRC64;
MANENRLRDY VNRLAVELDD AREQLRKAVD REHEPVAVIG MACRYPGGVR TPEDLWAVLR
EGTDAVGPFP ADRGWDVERL YDPSPDAVGH SYVREGGFLH DAADFDPAFF GMSPREAAAT
DPQQRLLLET AWEAFEHARL RPADLRGTDT GVFTGVMYDD YGSRLNPAPA GFEGYLVSGS
AGSVASGRIA YALGLEGPAV TVDTACSSSL VSAHLACRAL RDRECSLALA GGVTVMATPA
TFVEFSRQRG LAPDGRCKPF AAAADGTGWA EGAGLLLLER LSDARRNGHR VLAVIRGSAV
NQDGASNGLT APNGPSQERV IRAALAHARL APHDVDAVEA HGTGTELGDP IEAQALVNTY
GRNRPAERPL RLGSVKSNLG HTQAAAGVAG IIKIILSLEH GTLPRTLHVD APSPHVDWAG
GAVSLLTEPV PWPRTDRPRR AAVSSFGISG TNAHVIIEEA PGQAAASSPA EDAAATPSAG
AAGAAAGPVV PWVLSGRTEG ALRAQAERLL GHVDRTAPAS PADVGLTLAT ARTAFDHRAV
VLAADRDGLL DGLRAAAAGR PAPGLVTGTA RRGTRTAFLF TGQGSQRPGM GRDLYEAFPA
YAAAFDEVCA HLDPLLELPL KQVVFAAEDD PRAALVDRTD LTQAALFALE VASYRLVTSW
GVRPDVLLGH SIGELAAAHV AGVLDLSDAA QLVAARGRLM AATRKDGAMA ALEATEEELR
PVLDAEPALS LAAVNGPAST VVSGDEDAVA RVVELWRARG RRTKRLVVGH AFHSAHMDPV
LDAFRAVAEQ LRFAAPSVPI VSDVTGRPAT DAELRSPDYW ARHLRGTVRF HDGVRWLHGS
GVTAYLELGP DAVLTAPARD GVEAATDSES AASGTAEGDT RAAPAFAALL RADRPAALTA
TAAVAELHVN GGTVAWDAFF DPAGAHVVDL PPYPFQRDRH WLDVPAAAGG GDPADVGQSP
AGHPLLGAVV RLAEDGGSVL TGRLSLADHP WLADHAVAGT VLLPGTAFVE LALHAGEDTG
HDTVEELTLE APLVLPAEQA VQLQATVGVP DGTGRRAVSI HSRPEPADEA ASVPWTRHAT
GTLTAGAPAP NPAAEGGSRP PAGALPLDLA GAYDTLTARG YGYGPAFQNL TAAWQDGDHL
YAEIRLGADG PEQEPPHAAD YGIHPALLDS ALHALALAAD GGTRLPFAWS GVRLHATGAT
AARVHLTRIG EDAVAVELTD PAGQPLVTVE RLTTRPLDPA ALAAPAAGAG DAAFHRVEWT
ALPLAGAETD TDRWAVWGAD PVGLGLPSHP DLDALSDPAP AVALRFFAPP DGVDMVGRAH
AAAEGTLLRL QDWLGRPQTE DTHLVVFTSR GSSVDPADDP DLVQATVTGL VRTAQSEHPG
RITLIDLDGH PFSTAALIAA VATVRAADEP YAALRKGELS APRLTNTPQV QLTIPADSDS
AWRLALTSPG SPDHLALLPA PDLEQPLKHG QVRIALEAVG LNFRDVLITL GMYPQPAPHI
GSEGAGVITE IGPGVTGFEV GDRVMGILTH GTGATTVTDH RVLARVPQGW TPAQAASATL
AYATAYYTLV TLADLKPGQN LLIHTATGGV GQAATHLARH LGARLYATAS LPKHHTLTTE
LGYDAQDIAD SRTQDYADHF LTRTDNRGMD VVLHSLAHEH TDTSLRL
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