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Database: UniProt
Entry: A0A3N1B030_9ACTN
LinkDB: A0A3N1B030_9ACTN
Original site: A0A3N1B030_9ACTN 
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
//
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