ID A0A0H4C8B2_9ACTN Unreviewed; 5346 AA.
AC A0A0H4C8B2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:AKN70876.1};
GN ORFNames=QR97_14585 {ECO:0000313|EMBL:AKN70876.1};
OS Streptomyces sp. PBH53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN70876.1, ECO:0000313|Proteomes:UP000036399};
RN [1] {ECO:0000313|EMBL:AKN70876.1, ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|EMBL:AKN70876.1,
RC ECO:0000313|Proteomes:UP000036399};
RX PubMed=26227608;
RA Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT Urban Environment.";
RL Genome Announc. 3:e00859-e00815(2015).
RN [2] {ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA Gosse J.T., Boddy C.N., Hill P.B.;
RT "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT urban environment.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011799; AKN70876.1; -; Genomic_DNA.
DR STRING; 1577075.QR97_14585; -.
DR PATRIC; fig|1577075.3.peg.2998; -.
DR Proteomes; UP000036399; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine 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; cd08956; KR_3_FAS_SDR_x; 3.
DR CDD; cd00833; PKS; 3.
DR Gene3D; 3.30.70.3290; -; 3.
DR Gene3D; 3.40.47.10; -; 3.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 3.
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; 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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
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:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 3.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 3.
DR Pfam; PF00109; ketoacyl-synt; 3.
DR Pfam; PF02801; Ketoacyl-synt_C; 3.
DR Pfam; PF08659; KR; 3.
DR Pfam; PF21089; PKS_DH_N; 3.
DR Pfam; PF00550; PP-binding; 3.
DR Pfam; PF14765; PS-DH; 3.
DR SMART; SM00827; PKS_AT; 3.
DR SMART; SM00826; PKS_DH; 3.
DR SMART; SM00822; PKS_KR; 3.
DR SMART; SM00825; PKS_KS; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 3.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 6.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 3.
DR SUPFAM; SSF53901; Thiolase-like; 3.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000036399};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..460
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1704..1782
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1800..2224
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3451..3526
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3546..3969
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 5191..5266
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1386..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 5346 AA; 551284 MW; F2DD57982A2EDB3A CRC64;
MSGPDDQIVN ALRASLKENA RLQQENSKLA ATVAEPIAIV SMACRYAGGI RTPEDLWRVV
TDGTDVYTTF PEDRGWDLEG LYHPDPDNPG TTYVREGAFL HDAGEFDAAF FGISPREALA
MDPQQRQLLE VSWETLERAG IDPHSVRGSD MGVFAGIVHQ DYAPDLSGHE GYLSLERALG
TAGGVASGRV AYTLGVEGPA VTVDTMCSSS LVAIHLAMQA LRRGECSMAL AGGSTVMSTP
GGFVGFARQR GLAFDGRCKS YAAAADGSSW AEGVGVVLLE TLSQARERGH RVLAVIRGSA
VNQDGASNGL TAPNGPSQQR VIRKALAGAG LTTADVDMVE GHGTGTVLGD PIEAQAILAT
YGQDRPDGQP LRLGSVKSVI GHTQAASGVA GVINMVQALR HGLMPASRHI DAPTPQVDWS
SGAVELLTEA REWPDTGRPR RAGVSSFGAS GTNAHLILEQ APEEETAQAA PAAPAGVMPL
VVTAASAASL TGQADRLAAF LADAPDTPLT AVAGTLATRR AVLGERAVVV AKTHDEALAA
LTALARDEQA PGTVRGTATA AGAGKTVLVF PGQGTQWIGM GRELLDSSPV FAARIEECAR
ALERWVDWDL EAVLRGEADP DLLHRVDVVQ PASFAMAVGL AAVWASVGVV PDAVIGHSQG
EIAAACVAGA LTLDDAARIV AVRSQVIRGR LAGLGGMASV ALTEDDVTAR LERWAGRVEV
AAVNGPSSVV IAGDAEALDE VLDTLEDQGV RVRRIAVDYA SHSRHVQAVQ EALTEAFADI
RGQAPAIPFL STVTGEWVRE AGVLDGGYWY RNLRQQVRFG PAVEALLAEG HTVFVESSAH
PVLVQPVTEI ADAADAVVTG SLRRDDGGLR RLLTSLAEVF ASGAHVDWRG VLPEAARTAH
ADLPTYAFDH RHYWIRLTAN GGDAASLGVT GSEHPLLGAV VPLPQTDGLV FTSRLSLRTH
PWLADHAMQG VVIVPGTVYV DLAVRAGDEF GCGTLEELVI EAPLVLPAQG GVRVQVAVGG
ATPNGSRTVD VYSLREDAAD ADGHGEWTRH ATGLLSGSPA RFTEPAVDYA AWPPPGAEPV
AIDDFYAALV ARGYAYGPAF QGLRGVWRRG EELFAEAALP QDHRENADKF AIHPALLDAA
LHTNAFANPD DDRNVLPFAW NGLVLHAEGA SALRVRVAPA GPDALSFQAA DETGALVLTM
DSLVSLPVSA EQLGAAAGAH RDALFAVDWV QLPAPEGAAT APAWVPVADA DDVTALAARE
SAPGAAILDA DSDGADPQTL TTRVLRVLQA WLAAPGLEAA RLVVATRGAV AAGGDRAVTD
PAGAAVWGLV RAAQAENPDR VILVDLDPAA ATGAGPVLAQ LLATGEPQLA VRGTALSAPR
LVRADTADTG GTADTPAPAA GTEAAAAGTG EPADATAAFD ADGTVLLTGG TGSLGALVAR
HLVERHGVRH LVLAGRRGPD APGAAALTTE LTALGAAVSV VACDVSDRDA VAALLRGIPA
EHPLTGLVHL AGVLDDGVIS ALTEERVAGV FAPKATAVRH LDELTRELAP GLRSFVVFSS
AAALLGSAGQ GNYAAANAYL DALMAHRRAA GLPGVSLAWG LWEQSAGLTA HLSETDQARM
SRGGVLALTP EEGLALLDTA LHADRALLVP IKLDLRALRS DAASGTAVPH LLRGLVRAGR
RSARAAAGDG SGLLRRLAGL PEAEQEAVLL GIIQAEATAV LGFSGPELAQ GTRGFGDIGF
DSLTAIELRN RLSAATGVKL PATLIFDYPT PVALARHLRE ELGESAAGAA APTVVATDPD
EPIAIVGMAC RLPGGVTDPA GLWRLVLDRR DGITEFPDDR GWNLDELFDA DPDKAGTSYV
HKSGFLHGAA EFDAEFFGIS PREALAMDPQ QRLLLEATWE ALENTGIDPS STRGADIGVF
SGVSIHDYLE SLSNMPPELE GYVTTATAGS VASGRVSYVF GFEGPAVTVD TACSSSLVAL
HLAAQALRQG ECSLALAGGV AVMGSPIGVL GMSRQRGLAA DGRVKAFSAG ADGTILSEGV
GIVVLERLSE ARRNGHQVLA VVRGSAVNQD GASNGLTAPN GPSQQRVIRR ALAAAGLAAT
DVDAVEAHGT GTALGDPIEA QALLATYGRD REQPLWLGSL KSNIGHTQAA AGVAGVIKMV
QALRHGVLPP TLNVTEPTPQ VDWSAGAVEL LTEERQWPET GRPRRAGVSS FGISGTNAHV
ILEQAPEEPV VVRVPQDGVV PLVVSAASEG SLAGQAERLA AFTADTDASL TDVAGALVRR
RAVLSERAVV VAGSREEATA GLAALARGEA APGLVKGSTA SAGRTVLVFP GQGSQWPGMG
RELLESSPVF AERIEECARA LEPWVDWDLR AVLRGEVDLM DRVDVVQPAS FAVMVGLAAV
WASVGVVPDA VVGHSQGEIA AACVAGALSL EDAAQIVAVR SQVIAGELAG RGGMASVALP
EAEAAERIAA WDGRVEVAAV NSPSSSVIAG DAEALDEALA ALEADGVRVR RVAVDYASHT
RHVEAVEAAL ADAFADIHGQ APLVPFFSTV TGEWVREAGV LDGGYWYRNL RQQVRFGPAV
EALLAEGHTV FIESSAHPVL VQPVSEIVDE TRADAVATGS LRREEGGPRR LFASMAEVFV
QGVAVDWTGV LPEGAGDAPL DLPTYAFDHR HYWLQTAPAT DAASLGQAAA DHPLLGAVVP
LPQSDGLVFT SRLSLRSHPW LADHVVGGAT VVPATGLVEL ALRAGDEAGT ARLDELTVET
PLVLPEEGGL RVQVAVGGPD DTGARTVDIY AAGGEDTAPD AWTRHATGRL TPAPPTPVEA
SAGLTLWPPT GARPVDADEL YADLLRLGHP FGPAFRGVTA LWRRGEEVFA EVALPEEQRA
GAERFGIHPA LLDAAVHSGL RHAATADPDG TGQRLWQPAA WQGLTLHATG ATTLRVRLAP
SGSGRLSLEA TDQAGGLVVT LDALGFLPVP ADQLTAATGD GGRSLFRVEW TELPAASAET
QQVPQWVPLF HADEVEILAG AATGPLVAVV EAVTPDGTAD DALAQTNRML AVLQAWFAAP
SLEESRLVVL TRGAVPADGD DTVTDPAGAA VWGLVRAAQA ENPGRIVLID TDTDPDIAYG
TAVEPLLATV LAAGEPQVAV RGAVLSVPRL VRAAEAGPAA AFRPGGTVLV TGGTGSLGAL
LARHLVERHG VRHLVLAGRR GAEAPGAAEL AAELAELGAE SVSLVAADVS DRAQVARLLD
AVPAEHPLTG VVHTAGVLDD GVISALTPER MAGVFGPKAN AAAHLDELTR TLDLTVFAVY
SSGAGLFGSA GQGNYAAANA YLDGLMARRR AAGLPAVSLA WGLWEQSTGL TAHLSATDQA
RMGRGGVRAL TPEEGLALFD AALGAEQALV VPIKLDLRAA RADAASGGPV QPLMRGLIRV
TRQAARTTAA DRSGGGLADR LAGLAPDEQE ALLLDVVRGQ VATVLGHAGA DQVRAEKAFK
DAGFDSLTSV ELRNRIREAT GLSLPTTVVF DYPTPLALAR HLHSHFGHVT AAPAAPEPAV
ATADPGEPIA IVGMACRLPG GVTGPEDLWD LVAEGRDAMS GFPSDRGWDL EGLFDSDPGR
VGTSYVDQGG FLYDAGQFDA GFFGISPREA LAMDPQQRLL LETSWEALER AGIDPLALKG
TDVGVFSGVM TQGYGFGGEL PPELAGFTAT GSAGSVASGR VSYVFGLEGP AVTVDTACSS
SLVAIHLAAQ ALRNGECSMA LAGGATILAN PYTFVEFSRQ QALSPDGRCK AFSSSADGTG
WAEGAGVIVL ERLSEARRKG HRVLAVIRGS AVNQDGASNG LTAPNGPSQQ RVIRKALASA
GLSVSEVDAV EAHGTGTVLG DPIEAQALLA TYGQDREEPL WIGSVKSNIG HAQAAAGVAG
VIKTVEALRH AVLPPTLHVD QPSTEVDWST GAVEVLTEAR AWPQTGRPRR AGVSAFGVSG
TNAHVILEQA PEEPAPAAVA PADGVLPMVV TARGTAALAG QAARLAAFVR ATEAAPAAVA
GALVSRRAVL PERAVVVAGS REEAAAGLAA LAAGEPSPLV VTGSESTGGT VFVFPGQGSQ
RLGMGRELYD RYPVFARALD EACAALDARL AGWADHAVKD VIFGQVGNAG GGLLDQTVFT
QAGLFAVETA LYRLLESWGV RPDVVAGHSI GEVVAAHVAG VLSLPDAAAL VAARGRLMQA
LPPGGAMVAV AASETEIEEY LGAGVDLAAV NAPGSVVLSG DEGAVEAVAE KLREQGRRVK
RLTVSHAFHS ALMEPMLTEF ATALAGLTWN EPTIPVVSNV TGRLAEPGQL TDPAYWVDHV
RRPVRFADGI SATGGSVFLE LGPGGALSGA ITESAGEDAV SVPALRDDRG EAQTLLVSVA
HLFVRGTKVD WAAVLPEGAT EAHVDLPTYA FEHRHYWLQT APATDAVALG QSTADHPLLG
AVVEVPETGG VLFTSRLSLR THPWLADHAV GGVVLVPGTG LVELAVRAGD EVGCGVLDEL
VIEAPLVVPE QGGVRVQVAV GGPDDSGLRS VAVYSARENT AGEIGTDAWT RHATGTLTGT
AADTPAFDTT VWPPAGAEPV GLDTTAFYAD LASHGYAYGP AFQGLRAVWR RGEEIFAEVA
LPDEQRDEAA RFGLHPALLD AALHTDAFAQ PDDGHNVLPF AWNGLVLHAA GAASLRVRIA
PRGTDVLSLV AADENGGLVL TVDSVTFRPV DVGQLDAAAT ADEGRDALFG VAWTELPAPA
EAPATAPTWT RVATAADVTA LKGEVPEAAV LELHGSGDGD AEALTRTAAA LAVVQAWLDD
PEFEDARLLV VTRGAVPAGG AATLTDAAGA AVWGLVRAAQ AENPGRLVLL DLDPATDTPA
DDLLTAVLAT ALASGEPQLA ARGTALSVPR LVRAPEAEPA VAFRPDGTVL VTGGTGSLGA
LVARHLVERH GVRHLVLAGR RGPEAEGAAE LAADLAALGA ESVSLVAADV SDRTAVARLL
DTIPAEHPLT GVIHTAGVLD DGVISALTPE RLAGVFAPKV SAVRHLDELT RTLDLTAFAV
FSSASGLFGS AGQGNYAAAN AYLDAVAHQR RAAGLPATSL AWGLWEQTSG MTAHLGSADQ
ARMSRGGVLP IGPAEGMRLL DAALDTAEPL LVPIKLDLRA LRADAAAGRT VQPLLRGLVR
TGRQPVRATA ADGTGGLTRR LAGLDPAEQE ALLLDLVRGH VATVLGHAGA EQVGPETAFK
DAGFDSLTSV ELRNRLRETT GLKLAATVVF DYPNPLALAR HLHAELGTTN DALSLVHEKI
EDIESLIAGL LSDESKKADI VLRLQGLVAK CNGAVEETQG SAVAEQLESA SADEVLDFIN
DELGIV
//