ID A0A3N1B030_9ACTN Unreviewed; 2129 AA.
AC A0A3N1B030;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase C {ECO:0000313|EMBL:ROO62111.1};
GN ORFNames=EDC02_4081 {ECO:0000313|EMBL:ROO62111.1};
OS Micromonospora sp. Llam0.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO62111.1, ECO:0000313|Proteomes:UP000275308};
RN [1] {ECO:0000313|EMBL:ROO62111.1, ECO:0000313|Proteomes:UP000275308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Llam0 {ECO:0000313|EMBL:ROO62111.1,
RC ECO:0000313|Proteomes:UP000275308};
RA D'Agostino P.;
RT "Genome mining of underrepresented organisms for secondary metabolites.";
RL Submitted (NOV-2018) 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:ROO62111.1}.
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DR EMBL; RJJY01000001; ROO62111.1; -; Genomic_DNA.
DR Proteomes; UP000275308; 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 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; 3.
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; IPR013149; ADH-like_C.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
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; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 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.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000275308};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2030..2104
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2107..2129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2129 AA; 223889 MW; 2794CC432FF029F7 CRC64;
MFDNDGTDPT QLIAVVGMAG RFPQAPDVDS FWRLLRDRGD AIAPVPGDRW DASAQLDPER
HVQDVAGFVD DVDLFDPGFF GISPREAEDI DPQQRLMLET VWRTLEDAGQ PAAGLRGSRT
GVYVGASWHD YEILRKERGL GATTHSAVGN ALDVIAARVS YFLRLTGPSL VVETGCSSSL
VALHLAGQAL RAGETDAALV GGVNLILAPD VSIGLTAFGG LSPEGRCKAF AATADGFVRA
ECVAALMLKR LDRAIADGDR IRGVIVRTVV NNDGGGESLV TPNPAGQEDL LRRAYQGLDG
VVDRLRYVEA HGTGTGRGDP IEAGAIGRVL GRAGARARAG DGGQVGAPLA LGSVKTNIGH
AEAAAGLAGL VKVLLALEHR VVPPSLHSAE LNPAIDFTGL NLRLVREPLP LPVDEAVCLG
VNSFGWGGTN AHVVVADPPA GTNRRPEPAT AATGPGVPAV LPVSAHTNQA LNQRLRDLRD
RLAAGAEPQR LAGALAHRRD HFPLRTAVVA ADAEAAVTLI DAHLDDPQAD LAGITAGRAD
ASGRTAFVFP GQGAQWAAMG QRLYAEVPTF AKVIDRCADA LRPYVDWDLT QVVSGAAGDG
WLSRVDMLQP TLWATSVGLA ELWRANGVVP DVVVGHSQGE VAAATVAGIL SYSDAAMVVA
RRSALALRTS GNGRMLAVSL DRDAALDALA GFEELVSLAV HNGPSSCVLS GETEAVLTLK
ELLDADEVFC RLVDVDYASH SPQMDALTDD LLAALHELRP GQGEVELMST VRVAPLAGPE
MDARYWVDNL RQPVQFHDTM GRLFDDGVTH VVEISPHPVL VPALEQLAAA RPQPPRVLST
LRRDQGTPAD LAAAFGRGYV AGLAPFAGLP DGFGVDLPGY PWQRSTHWPP AARRRSRTAG
TEITLVPSPS ETDLWQAELE LGADDQPWLD DHRVHDAVVV PGAAMIVLGL GIGRARTGRL
PATLHRTTFH SDLTLADGPA RLGMLWRDDV TEGGSFVLQS LGSDGSGWFR HATAQIRHTT
GAADPVEFPG QRLTDPATEV DPETFYAGCH QRGLRYGPAF QGIRRLRHGT DWALAELALP
DRCRAGAAAY PLHPALLDAA LQASLALHAG PATVVPTGVD RVDVLGELAE PTVQAWSYVS
RRDDGRYDVH LYDADRTPLL SLRGLTLQEL DVSGPADPDA GLLHQLRFLP RPVQQPGTPA
GRWLVIGSGD TTDTDTVGGG DTADLAANIA GELRRVGADA DVPAADGDVD AVRDGDLTGL
VYLAPAAPAG LDRQRQALAG LADLVRACLG RPAPPRLVLV TVDAQTATAA DRPDPGSALF
WGFARVLRRE HPELVATVVD LTGTADAAGS AGTQSTDPAA ALVAELGAAD GDDQVALRPD
GRYVGRILAT GRADLDRVAD GTRPRWRTPR QPFRLIPARA GGWDGLEFRP LRRRRPGPGE
VEVEVTAAAL NFIDVMKAVG TYPDPVGAGL LGGECAGRVT ALGAGVTGLT VGDRVVACVF
GALASHVTVS TGRVRPIPPE LSDEDAAALP LVGVTAWYGL AELGRTGPGD TVLVHSAAGG
LGLAAIAVAR HLGAEVIATA GTESKREHLR RLGIRHVFDS RDLSWAEQVL AATGGRGCDV
ILNSLTGAAI TRGLDVLAED GRFIEVGKKD IYADRTISLS AFRKGISLAS VDVAGLMQRR
PARFTEQFGQ VWELVRTGQL GRLPVIDYPF GQATEALREM SQGRHIGKFV LSRPDSVVSV
APEPLPGGRF RDDGTYLITG GLGALGLSLA EFAAAAGGGA IALLGRSAPD ADAAARIDAV
RHGGVQVRTY QVDVADRAAL ADVLTRVRTD LPPLRGVVHA AGVLDDATIA TLHTGQLDRV
LAPKVDGARH LDALTGADPL DLFVLFSSAA ALVGNAGQAA YAAANAYLDG LAEDRRRRGL
AGLSVQWGPF AGVGLAARDG NRGDRLAERG MGSFPAEQAW PALTRLLATD ATVVGYLPLN
LRQWFDAYPD TAALPSWQEL RAGRAAAAAG GDAGQFLDQL RNTPADDRAP LVEAKVRELT
GRVLRIDPTV IDRDTPFKAL GLDSLMSLEL RNRLEAAFDL KLSPTLLWTY GTSGALTGML
CDRLPTGDDE RPVSAPDAVP APDAVPATE
//