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Database: UniProt
Entry: M3C452_STRMB
LinkDB: M3C452_STRMB
Original site: M3C452_STRMB 
ID   M3C452_STRMB            Unreviewed;      3669 AA.
AC   M3C452;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:EME98736.1};
GN   ORFNames=H340_20048 {ECO:0000313|EMBL:EME98736.1};
OS   Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME98736.1, ECO:0000313|Proteomes:UP000011740};
RN   [1] {ECO:0000313|EMBL:EME98736.1, ECO:0000313|Proteomes:UP000011740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40847 {ECO:0000313|EMBL:EME98736.1,
RC   ECO:0000313|Proteomes:UP000011740};
RX   PubMed=23558536;
RA   Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT   "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT   mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT   Transglutaminase.";
RL   Genome Announc. 1:E0014313-E0014313(2013).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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:EME98736.1}.
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DR   EMBL; AORZ01000068; EME98736.1; -; Genomic_DNA.
DR   STRING; 1223523.H340_20048; -.
DR   PATRIC; fig|1223523.3.peg.4085; -.
DR   eggNOG; COG3321; Bacteria.
DR   Proteomes; UP000011740; Unassembled WGS sequence.
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; 2.
DR   CDD; cd00833; PKS; 2.
DR   Gene3D; 3.30.70.3290; -; 2.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
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; 2.
DR   Pfam; PF08990; Docking; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 2.
DR   Pfam; PF21089; PKS_DH_N; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 2.
DR   SMART; SM00827; PKS_AT; 2.
DR   SMART; SM00826; PKS_DH; 2.
DR   SMART; SM00822; PKS_KR; 2.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 2.
DR   PROSITE; PS52004; KS3_2; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          40..465
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1750..1825
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1845..2273
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          3507..3585
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          469..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3669 AA;  381798 MW;  D2569F85668A5A5B CRC64;
     MTTVDTPVQK IAEALRASLL ENERLRRRYD EAAAASAAAV EPVAIVGMSC RFPGDVESPE
     DLWRLVDAGT DAITAFPGDR NWDLDAVYDP EGQRPHTSYT GQGGFLHRAP EFDAAFFGMS
     PHEATATDPQ QRLLLEVAWE AFERSGIDPQ SLAGSRTGVY AGVMATDYPV RVGTVPDGAE
     GFMVTGTDGS IVSGRISYTL GLEGPAVSID TACSSSLVAL HLAVQALRKG ECTLALAGGV
     TVMSTPRTFV EFSRQRGLAL DGRCRAFADA AAGTGWGEGA GMLVLERLSD ARRNGRRILA
     VVRGSALNQD GASNGLTAPN GPSQQRVIRQ ALADARLGPA DVDVVEAHGT GTVLGDPIEA
     QALMATYGKE RPEGRPLWLG SVKSNIGHTQ AAAGVAGVIK AVMAMRHGVL PRTLHVDAPS
     SKVDWEDGTV ALLTEPVPWE GGGPRRAAVS SFGLSGTNAH VILEEAPPAD PAAAEAAGTG
     QAGTGAVEDG KAGVKETDAE QTGAREAAAP LPFLLSARGD AALRAQAGRL ADRLAADPAL
     RPADVAHSLL TTRAALEHRA VLVADGTEEL LAGLRAAAAG EAPDDLVRGT VAGGRSKVVF
     VFPGQGSQWA GMARELLDSS PAFAERIRQC AAAVGRFVDW DLLAVLRGEP GTPDLERVDV
     VQPALFAVLV SLAELWRAHG VKPAAVVGHS QGEIAAACVA GALSLEDAAR VVTLRSQAIA
     RRLAGPGGMM SVSSPADRVA ERLLRWDGRL SVAAVNGPGS VAVSGDSDAL DELLTELRAE
     DVWARRIPVD YASHSAHVES IEAELLEALA DIRPRASRIP FYSTVTASRI DTSGLDAAYW
     YRNLRQTVRF EETTRALLAD GHGVFVESSP HPVLSMGVQE TADAAGRTVA AVGSLRRQDG
     GARRFLLSLG EVWAQGVAVD WSVPLAPYAP SWVELPTYPF QRRFYWPRPD ASGADVVSAG
     LDSADHPLLG AVVALAGADG ALLTGRIGLD THPWLADHAA GGAVLLPGTA LVELAVRAGD
     QVGCGRIDEL TLTEPLLLPA KGGVQVQVRV GVPGADGRRP VSVHARPLTG AAADGADPEW
     TAHAEGFLVA EPAPAPEAAW ASDAPDVWPP AGATALDVSD LYERLAGQGY GYGPAFQGLR
     AAWRRGDEVF AEVALPEDAR ADAARFGLHP ALLDAALHAA GLGPFDTAAS DGADGGVRLP
     FSWTGVSLRA VGAQALRVRV SPAGDDAVAL RLADMAGAPV ASVDALLLRP VAAGALSAAA
     APHRDALFRV EWQTAAGAEA AGPVPWALLD EGAGSDAYAD LLPSGGPVDG PEPDLLLLPC
     PPGGGVMDAD DVEAVPRRLR EVLGTVLEAL QRWSAEGRPD SSRLAVVTRG AAGPAGQASS
     AGSSVDPIGA AVWGLVRAAQ AETPDCFVLV DTDGTPESAR RLAVAALTSG EPELALREGE
     MHVPRLVRTT PRPASDEPAL TGFEDWGPQD SALITGGTGG LATLLAEHLI THHHITNITL
     ASRQGPNHPG ATELVNRLTE LGGNITLTAC DVSDPTQVTD LLTGIPHLKA IIHTAGVLND
     ATLTNQTPHH LHTTLTPKAD AAWHLHHTTQ HLNLPLTHFI LYSSAAATLD GAGQANYAAA
     NAFLDALAHH RHTHHLPAQS LAWGLWTQDT GMTSHLSSAD VDQMARSGVR GLSAAEGLAL
     FDTAVADGTP VLLPVRLDPA ALRERPGGLP PLLSRLVRPA ARRATASAAT GDGGTLAHQV
     LRMAAPERER LLLDLVRTQV AGILGHESGD AVEPDRAFKD LGFDSLTSVA LRNRLGAAAG
     VRLPVTLVFD HPTPAALAAY LGSELTGGEA EPQGASPATG ARAADEPIAI VGMSCRFPGG
     VTTPEELWRL LAEGRDGITP FPEDRGWDLE TLCDTSGLRP NTSHADTGGF LYDAAEFDAE
     FFGISPREAL GTDPQQRLLL EASWEALERA GINPHTLRGT TTGVFTGIMY HDYASRLTHT
     PLPEGVDTYL GNGSLGSVAS GRISYTLGLE GPAVSIDTAC SSSLVALHLA IQALRNGECS
     LALAGGVSVM FTPETFVDFS RQRNLAPDGR TKAFAGAANG TSLSEGVGML LVERLSDARR
     NGHRVLAVVR GSAVNQDGAS NGLTAPNGPS QQRVIRQALD NAGLTPIDVQ AVEAHGTGTK
     LGDPIEAQAL LATYGKDRAA ERPLWLGSVK SNLGHTQAAA GVAGVIKMVM AMRNGVLPKT
     LHVDEPTPHV DWTAGHVRLL TEATPWDDET APRRAGVSSF GISGTNAHVI LEEAPREPAA
     PAPEPSSTRP VLWPLSATSA QALRAQARRL LDVLPDDDGL APIGLALATT RAHFDHRAVV
     TGRTRTELVT ALTALTDGTS APGLTQGTAR TTGRTAFLFT GQGAQRLGMG RELYETFPVF
     AKALDEVCAH LDQPLKDVLF GQDGELLNRT EYAQPALFAV ETALFRLVES WGVRPEVLAG
     HSIGEIAAAH VAGVLSLADA CALVAARGRL MQALPEGGVM AALQATETEA LTLLGDAQDA
     AIAAVNGPRA VVVSGAEATV TAIVEKLREQ GRKTSLLKVS HAFHSPLMEP MLEDFRTVVA
     GLSFTEPRIP IVSTVTGLAA TAEELTSVEY WVEHVRRPVR FADAITTLTT DGITTFLEIG
     PDAVLTAMAA DHTTATCVPL QRRNRPEDRE ALTALAHLWT HGHPIDWQTL HPATPTSQVD
     LPTYPFQRRR YWIDPAPEAG DVTAVGQAAA GHPLLGAVVQ RAGSDETILT GRVSLRTHPW
     LADHAIGDTV LVPGTALTEL ALRAGEHAGT PHVEELTLQE PLVLLPEQSL DLQVVVGAPD
     GSGARPVTVH SRPHSADALT DESWTQHAQG TLVGRLPAGE APEAAETETW PPAGSRPIPV
     DDAYAELASQ GYHYGPVFQG LQAAWRLGDD VCAEVALPEE AHGDAGAFGI HPALLDAALH
     AIDAGRAGET SEDGSGTLLP FAWQGVSLHA TGATRLRVRI RRTAEHALSV VATDERGAPV
     VTIRSLVLRA LSGERLRAAG QRPLFTVTWT PADRPGPGSG PADVLTVRPG GGTPDADAWV
     ADAEALLPDV LPAHVVVRCD ADPTSSPEAP DGLSAAVRAG AGRVVALLRR WLADERFAGS
     RVTLVTRRAV AAGRPGEAAG DVPDLAGSAV WGLVRAVREE HPGRVGLVDV DGAPESEDVL
     PAVLASGEPE AAVRGGTVLL PRLVRVSARG TEADASSAPF GDGTGTVLVT GGTGGLGRVL
     ARHLAASHGV RHLLLLSRRG PAAEGVGELI AELAESGATA DVVACDAADP DELAAVLARI
     PADRPLSGVV HAAGVLDDAT LASLTPERFE SVLRPKVDAA LTLHRLTADA GLSAFVLFSS
     AAGTLGAAGQ GNYAAANAFL DALALHRRAQ GLPGLSLAWG LWEAGSGMGD RLSEADLRRM
     ARSGVRALSP DEGLALFDAA LSAGPAAVLP MALDTARVRS GGGTDEVPAM LRSLVRAPAR
     RPAAAGAGAE APGTALAERL AALSEEEQER TLLHLVRSHT AEVLGYARAQ DVDPLRGFVE
     SGFDSLTALE LRNRLGGASG VRLPSTLIYD HPTPLAAARH LRAELVGATV PAGPSLEAEL
     AALEAAMAGA APDPDEHARI AARLRSLAAR WGAALHPAGE QTPEDDRAEL ESATADELFD
     ILDGELDVS
//
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