ID A0A0K9XAJ9_9ACTN Unreviewed; 2457 AA.
AC A0A0K9XAJ9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNB50449.1};
GN ORFNames=AC230_20940 {ECO:0000313|EMBL:KNB50449.1};
OS Streptomyces caatingaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB50449.1, ECO:0000313|Proteomes:UP000037288};
RN [1] {ECO:0000313|Proteomes:UP000037288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT from Caatinga biome, from dry forest semiarid of Brazil.";
RL Submitted (JUL-2015) 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:KNB50449.1}.
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DR EMBL; LFXA01000014; KNB50449.1; -; Genomic_DNA.
DR RefSeq; WP_049717844.1; NZ_LFXA01000014.1.
DR STRING; 1678637.AC230_20940; -.
DR PATRIC; fig|1678637.3.peg.4486; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000037288; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
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:UP000037288};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2372..2449
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1534..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1553
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2457 AA; 256445 MW; D6FF51D3724D0EA2 CRC64;
MAQDDDVIAI VGAACRLPGG IEDLAGLWSA LEAGRDLVTI VPADRFDPGA FVDEHRRRPG
RSCTPAGGFL ADVAGFDAEY FGVSPREASR MDPQQRLLLE LAVEALDDAG IAPAATAGSD
TAVFIGVSSH DYGDLQSADP ESANAYSMSG AAMANTANRL SHTMDWHGES MAVDTACASA
LTAVHRACEH LRAGRSRTAL AGGVNILLNP FGFVGFSAAA MLSPTGRCRT FSAAADGYVR
AEGGGVVVLK RLSDALADGD RPHALVLASG ANSDGRTPGI ALPNSAAQEA LLREVYARAR
VEPDDLAYVE AHGTGTPSGD PIECAALHHA LTARRTKGPL PIGSVKSNLG HLEAASGMPG
LFKALLVLRH RRVPPTLHAE PLNPHVPFAD WKLAPAVRPL RLDATPRPVA GVNSFGFGGA
NAHVVLAPPP DTPAPVRTTT PSALPVLVTA RTPAALAAAA ARLADRLTGP DRPDFHDVVH
TLARRRGRHE HRAVVLAAGP ADAAHGLRAL ADGREPPAGA AAEEAVTRGK VAFVYSGNGS
QWAGMGADLL ATEPVFRTAV EEADAALRPH LGWSVRAELA GRCARPADAE FSQPLLFAVQ
TGLTALLASH GIVPRAVLGH SVGEIAAAHA AGALDLPSAA LVVAARSRAQ APTAGHGRMA
AVGLSEQDAR AELAARPGTI EIAGINSPVD VTLSGPEHDL LALGRDLTAR GVFHRMLDLH
HAYHSRAMDP VEQPLRAALR ALRPRPGTLP FLSSVTGELL PGDRLDAAYW WHNVRRPVLF
APAAEALLDE GCDILVEIGP HPVLTPYLKR TAALCPEPVA TVTTCTRSGD GPAELRRAVA
RALAAGADAD WTRALPGTGR VVDLPAYPWQ RERHWNGEPG WWTRRGHGRP SPHPLLGTRL
PAAEPVWSGT LEPARLPWLA DHRVDGAVVM PAVGYAEMAL AAVRQTAGGP AEIHHLTIGR
PLPVPWDDET TALEVQVSLS TEDRTLRVAG RTAGTDGDWQ EHARCRARRL LRPAPEPLDI
DSVLKRVHTD ISVDEAYRTA ADRGLHLGPA FRTLHRLVLG DGEALSAYRA TSDTTGPGTQ
PALMDAGLQT ASHLTGVING LDALYLPVAV DTISSWNDLP PAGWIHARRQ GTGELESCWD
LTFTDDDGTV ALEMTGCRLR RAAGSAAPVQ RLETVLRAAP RPDDDGRPSP MPAPGALLAA
TAPRRAALAA AYERTHPART RAAEQAVRAH LFLRTVTEIL PGADTFTVES LLAAGVRREQ
AGTVRLLCSL AEEQGLLERT TADGDAPRWR PAGPPDPGAA LRAALTEGPP PDPAALALTA
RWGERLTGIL RGQAAEEDAE TDLHLVRQCQ EGGAERRFLD RTARELVRAT AEAWPADRPL
RILQTGTCGE AGTAAGGLTA ELLSVLPPDR TRYVLGDAAP PSGTRPRPHT RHTLDHRRLD
LNADPAAQGF TEGGFDLVVA VGPPGRAADP RPALRRCAWL LADGGALLVL DGQDTPAGAP
ARRPHPLTTA GLLEEAGFGD VHAVTPGRTV LLGRRTPRPA PLPPAAPPPA SPPPSHWIVA
AERPDDALTG ALAAALEKYG TVNVTRPPAG DDADGGWEAV LTAEASRRPH IVLLLGEDPA
AADDPHAALD EAVTRLGTLA ALARRDRFTS AAHPALSLVT RPCGALPAPE AATHPRDAAV
WGAARTFANE HPSATVRRVS LERGPDPEHD ARRLARELAV PTEDDEVVLT PGGRFTPTTA
PQHPPAGPPG TGGPGAYRLE LREPGLSPRL AWTAEEPVTP DAGQVVIDVR AAGLNYRDAL
FAAGLLPPGA DPDAASARGL GLECAGVVTA VAPGAGAFAP GDRVFAITRG ALASGPVADA
RLVAPIPSGT DFAAAATLPV VHLTAHYALN HLARLAPGET VLVHGGAGGI GQAVLHVARH
RGATVIATAG TPAKRALLRL MGVEHVLDSR GPGFADAVRG ITGGRGVDVV VNSLAGEGLT
RSAEAMAAGG RFIELGKRDI YANSPFPLGL LRDNQAFFAV DLARLLRDPG TLAAAFRETA
GHIAAGHYPP LPYRLWPAPR VDEALHTLQH SRHLGKVVVD LGERPPVEAA PRPARLDPDA
TYLLAGGLGG LGAATAGWLV EQGARHLALV GRRGADTPGA AGLVASLAAA GAHVTVHAAD
VTDAGALGRV LETAAAAGHP VRGVVHSTMG VDDAPLAELT PERVRAVLAP KMLGGMLLDR
LTAGRRPDLF LVHSSVAAHV GNLGQAPYAA GNLALEALVR ARRRAGLPGL AVAWGALAGT
GHAARDRQVT ERLSRAGIGT LTAQECRAAV EACLSAGTTH LTAGRFDWER ARHVLPALDR
PRFAPLLASG AHRPDAGPGE LRRRVAALPP DDAEALVADV LTEELAAVLQ TDAGRIDRAR
RLDRLGLDSL MAAELVVAVR RRLGCSLPSV EVVQAAGVTD LARRSLPRIL TAPAGRT
//