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Database: UniProt
Entry: A0A344UAT4_9ACTN
LinkDB: A0A344UAT4_9ACTN
Original site: A0A344UAT4_9ACTN 
ID   A0A344UAT4_9ACTN        Unreviewed;      3100 AA.
AC   A0A344UAT4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Beta-ketoacyl synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C0216_31345 {ECO:0000313|EMBL:AXE28005.1};
OS   Streptomyces globosus.
OG   Plasmid unnamed2 {ECO:0000313|EMBL:AXE28005.1,
OG   ECO:0000313|Proteomes:UP000252004}.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE28005.1, ECO:0000313|Proteomes:UP000252004};
RN   [1] {ECO:0000313|EMBL:AXE28005.1, ECO:0000313|Proteomes:UP000252004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LZH-48 {ECO:0000313|EMBL:AXE28005.1,
RC   ECO:0000313|Proteomes:UP000252004};
RC   PLASMID=unnamed2 {ECO:0000313|EMBL:AXE28005.1,
RC   ECO:0000313|Proteomes:UP000252004};
RA   Ran K., Li Z., Wei S., Dong R.;
RT   "Draft genome Sequence of streptomyces globosus LZH-48.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; CP030864; AXE28005.1; -; Genomic_DNA.
DR   KEGG; sgz:C0216_31345; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000252004; Plasmid unnamed2.
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; 1.
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; 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; 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; IPR036299; Polyketide_synth_docking_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
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; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 2.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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.
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   Plasmid {ECO:0000313|EMBL:AXE28005.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252004};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..443
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1650..1728
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1747..2169
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          3020..3095
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          441..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1253..1272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2606..2631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2943..3003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2973..2997
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3100 AA;  320564 MW;  3AEB32CEBD1A0EBB CRC64;
     MTNEDKLRDY LRRVTAELQS TRQRLRDAEE RSAGPVAIVG MACHYPGGVE SPDDLWSLVA
     EGRDGITPFP GDRGWDLDTL YHPDPDHPGT TTVREGGFLH GAARFDAGFF GISPKEALHT
     DPQQRLILQT SWEAVERAGL DPTALRDSRT GVFTGVMHHD YPGAQGAGSV VSGRVAYHLG
     LRGPAITVDT ACSSSLVALH LAVRSLRRGE CDMALVGGAT VMATPAAFVE FSRQRGLAPD
     GRCKPFAAGA DGTAWSEGVG VIVVERLATA LAAGRRILAV VRGTAVNSDG ASNGLTAPNG
     PAQQRVIRDA LVDAGLTPQQ VDAVEAHGTG TPLGDPVEAQ AVLAAYGRDR DRALRLGSVK
     SNLGHTQAAA GIAGIVKMAM AMRHGVLPRT LHLDAPSPYV DWSAGAVELL AEEAPWPAGT
     EPRRAAVSSF GVSGTNAHVI LEEPPLPADG RTAGQPDARR PAAAADAGDA RDAADSGNAG
     RTEPPLTPQA PPGPLAWTLS ARSDAALRAQ AAALAAFLAD RPQDPRPEDV ALSLATTRAS
     HEHRAAVVGG DRAGLLAALD DLAAGRPSPA VVEGVTGPAG GVAFLFPGQG SQWRDMAVGL
     LDTNEVFRER IAQCERALAP HVDFRLTAVL RGEQDLDRVD VVQPALFAVM VSLAEVWRSL
     GIHPAAVAGH SQGEIAAACV AGALTLEDAA RVVALRSRAL TALTGRGGMM SLALGADEAR
     DRLRRWDGRL SLAAVNGAAS VVVSGDTDAL DELLAACEED GVRARRVDVD YASHSAHVEA
     VRTQILQALA PLRPLAPAIP FFSSVEGRWI EDADAFDADY WYRNLRQTVR FDEAVTALVR
     RDCTTLLEVS PHPVVTTGAQ ETVDALGTDT AVAHTLRRDE GGPEQLLHAV ARLYVKGVRP
     DWSALWPGAR PTDLPTTAFL TEPYWIVPGP GAGGAGALGL DEVDHPVLRA ALPAADGLVL
     TGRLGLASQP WLADHTVEGQ VVLPGAALAE LASRAADEAG CAAVDQLTLL TPVVIPGTGD
     IRLRVDVAAP AEDGSRALTL HTLAGAGHWT THATGVLRPD AAEPAAAATE WPPADAEPQD
     VEAVYATLAD AGLDYGPAFR GLRALWRGRD GDLHAEVALP DAAEAGAFTL HPALLDACLH
     PVALGGFPTT GDGRRPALPF EWQGLRLHAA GAEAVRVTLS AAGPDAVRLT LTDTTGAPVA
     SVDTLVLREL PAGALGRPDR GDVLRPDRVT LPLPAGTHED YAVRDPELAR KLGKEPTGEP
     ARHVLVPAPT GEPGEAVRGA LTLVQDWLSD DTRADSTLVL VTRNADTDVA EAAVAGLVRS
     ARLEHPGSFR ILDLADLDAA TLAAIPAALA ADEPQLTLAS GTATATRLVR GLPAPAATGE
     LGPTLVTGAS GTLGQLVARH LVHAHGVRDL VLAGRRGGGA PGMAALVEEL AGAGAKVRAV
     ACDISDRAGL AALTAGEHFR TVVHAAGVLD DGLVTGLTPE RVDRVLAPKL DAALHLHELL
     PQARLVLFSS AVGILGGLGQ ANYAAANAGL DALSRRRHAA GLPGTSLAWG LWDATSGMTD
     GVDRDRLGRS GFRPLPTADA LAALDAALAS DEPVLAPIRL DPGALRAQGE DVAAPLRGLA
     GKPARRSAAP GGAAAVSELA ARLAGKSGPE RLRTLLDLVV GHTAAVLGHA SPEAVEPGRA
     FKDAGFGSLA AVELRNRLAA ATGLRLPATL VFSHPSPAAV ARHLDGLLAG TAPAPAHAVR
     AAAADEDDPV VLVGLGCRLP GGVRTPDDLW EMLVRERDGI GPFPDDRGWP LERLYDPDPA
     TPGTASTRHG GFMADATVFD AAFFGIAPRE AVAMDPQQRI LLETVWETCE DAGIDPDSLR
     GSRTGVFVGA MYQDYGRLLE NAAAEGFLAP GVGGGVLSGR VAYTYGLEGP TVTVDTACSS
     SLTALHLAAQ AVRAGECDLA FAGGVTVLST PVPFVEFSRQ RGLAADGRCK PFAAAADGTA
     LAEGAAVVLI ERLSRARAQG HEVLAVLRGS ALNSDGASNG LTAPNGTAQE NVMRAALAAA
     GLRPADVAAV EAHGTGTALG DPIEAQALLA VYGQDRPAPL LLGSLKSNVG HVQAAAGAAG
     VIKAVLSIRN GLLPRSLHID EPSPHVDWAS GDIALLDRAR PWPEGTAPRR MGVSSFGISG
     TNVHVLIEQA PAPEDTPAPL PPLDGVPWLL SARSEQALRE QARRLLDSDT ADVPAVARAL
     STTRSAHRHR AMIGGAGPEH KRAALAALAS GGPADGLHLA RATGRRLTLL FTGQGSQLPA
     MGRGLYEAFP VYAQAFDEVS AQFRLGTPLR EAVFERDDLL DRTEYTQAAL FAVQVAQFQL
     LSSWGVTPDL LIGHSVGELS AACVSGLMTL ADAAALVTAR GRVLGRLPAG GAMVAVRATE
     EETLAVLEGR TDRVGIAAVN GPRSVVLSGD EEEVLSAARE LAERGHRTRR LRVDVAFHSP
     RVDTALAEFR AAAAEVRFGR PAVPVVSTVR TAHAMDTPDY WADQLRGCVR FLDAVREAHG
     SGATAFLELG PDAVLAPAAE SCLPGLPVRP VSLLRRDRDD VRTAAEALGR LHTHGVEVDW
     QAVHAGRPAT PVRLPKYAFQ GRRHWPEQPA AAQAAPAPAP VPEAQAQPAE GAPALAPLWS
     AVESADLGTA LDLLDLRGDE TPAQVLHALG RLRSGVTAPV LEAARWTRVP DGPAPGLAHD
     IVLLAPSTGG EELADAVAGT LVRHGARVRS GGAGRPDLVL ALPGTEPAAE PGVPRWALVD
     GDGAVPACDH TVILPKDLAA PARRRLCAAV AGGYREARID PDGLFVRAYE PLVRTGVWRP
     EGDVLVAGPA DALTAAIVDA VLASGARCLV AGGADRPTGA LAFGDVAEAA TLTAAIVRAG
     SGFEDVRAPL VAVVSLGETV QEAAGSLAAA VHPGLDPRAA VAGLWRAMST GETAVRLLDT
     APASPAAGPA AATAERAGAV PEPAETATAT AEPAPPAPVP EPEPEPKSVP TPEPEPDGSQ
     PRDSALRATL AELPRTEWAE AVLGGVRGLA AAVLGYESAS EIDAEGEFLD MGLTSVTALE
     LRDHLTGLTG LEWPADLLYE YPTPRELADA VADRLTAPAA
//
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