UniProt: A0A0X3V3S4

Database: UniProt
Entry: A0A0X3V3S4_9ACTN

LinkDB:  A0A0X3V3S4_9ACTN 
Original site:  A0A0X3V3S4_9ACTN

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Ontology (4)   
   GO (4)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (45)   
   InterPro (24)   
   Pfam (10)   
   PROSITE (4)   
   SMART (7)   
All databases (51)   

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ID   A0A0X3V3S4_9ACTN        Unreviewed;      1916 AA.
AC   A0A0X3V3S4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KUL39324.1};
GN   ORFNames=ADL15_09920 {ECO:0000313|EMBL:KUL39324.1};
OS   Actinoplanes awajinensis subsp. mycoplanecinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL39324.1, ECO:0000313|Proteomes:UP000053244};
RN   [1] {ECO:0000313|EMBL:KUL39324.1, ECO:0000313|Proteomes:UP000053244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL39324.1,
RC   ECO:0000313|Proteomes:UP000053244};
RA   Gilbert D.G.;
RL   Submitted (OCT-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:KUL39324.1}.
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DR   EMBL; LLZH01000052; KUL39324.1; -; Genomic_DNA.
DR   RefSeq; WP_067687512.1; NZ_LLZH01000052.1.
DR   OrthoDB; 3406074at2; -.
DR   Proteomes; UP000053244; 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; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
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; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR020802; PKS_thioesterase.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
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; 1.
DR   Pfam; PF08990; Docking; 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   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 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   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053244};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          38..460
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1549..1624
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1916 AA;  198391 MW;  BAABE896F5883152 CRC64;
     MSEPGQVPED RLRYFLKRVT AELHDTRERL RGAEQSAVEP IAIVGMACRF PGGVGSPQDL
     WDLVAAGRDA IGPFPDNRGW DVDTLYHPDP DHPGTTYSNQ GGFLPGAADF DPGLFGISPR
     EALAMDPQHR LLLETSWEAI ERAGLEPAAL RGSRTGVFAG VMYNDYALVV SGSSDAAEGF
     MGTGGSIASG RVAYTFGLEG PTVTVDTACS SSLVALHLAV QALRNRECEM ALAGGVTVMA
     TPNTFVGFSR QRGLAPDGRC KSFADDADGT GWGEGVGMLL VERLSDARRL GHPVLAVVRG
     SAVNSDGASN GLTAPNGPSQ QRVILAALAA AQLEPGDVDA VEAHGTGTPL GDPIEAQALL
     ATYGQRRTEP LWLGSVKSNL GHTQAAAGVA GIIKMVEAMR HGRLPATLHA ATPSTQVDWT
     AGAVELLTSS RDWPAVDRPR RAAVSSFGIS GTNAHVILEA VPDEVPAAPA ALPVTPLVFA
     AADEQALDAQ LARVAAHLAG HPGVSLPAVA ATLAGRARLP YRAVALGRDR SELAAALAAG
     GTVRGVAGQP GRLAVVFTGQ GSQRLDMGRG LYDAVEQTGW AQPAIFALEV ALLALVRSWG
     IHPDVVAGHS IGEIAAAYAA GVLTLADAAT LVSARSRLMQ ALPAGGSMLA VQASEDQVRA
     VFPDVDVAAV NGPHAVVVSG LAEDIAPVEA HGWKTTRLRA SHAFHSRLME PMLDDFRVAV
     KALTFAEPRL AVVSTVADGG DWTDPEYWVR QVREPVRFAD AVTRLDATRV LELGPDTVLA
     TLIPDAVGAL RRERSEPATL LSAIATLFTA GTAVDWPAVT GDGGHTDLPT YPFTHRRLWP
     RPGPGGGGDA AGLGLDPGGH PLLGAAVELP DTATLVLTGT LEPAGQPWLT EHTVRGRAVL
     PGTALAELAL AAGARAGVPA LDELVFQAPL TLPERGAAAI RVTVTEIDRV HTVTVRSRAA
     DGEPWTTHAT GTLSAAEPAD VDADLVSWPP DGAEELPLTG LYETFAEAGL GYGPAFRGLR
     RLWRRGPEVF AEVRTDAPTD GYGLHPALAD AVLHAIGPAA LLPGDGLRLP FAVAGVHRFG
     PAGAALRARL TAADGADAIR LDLADDTGLP VATFERITLR PVATDRFGGA AADRLLYDVA
     WVPQEATATA PDAVVPLGAA LPSPVATLLV DATAPGPAGT RTAALLTLLQ TWLADPAWAS
     AQLVVRTHGA VGERVTDPDG AALWGLVRSA QAEHPDRLRL LDGPDDASYP LAQAVIRDGV
     PLVPRLARLR PEHTAAGPVT FGAGTVLVTG AGGTLGSLLV HHLAQAHGVR DLLLLSRSGT
     GVDLPGAVVR SLVCDVADPQ AVARALHGER ITAVVHAAGV LDDALLADLT PDRLATVFRA
     KVDAARTLVA ATRDQPLAAF VLYSSAAGVL GNPGQGNYAA ANAFLDAYAI QLRADGVPAT
     SLAWGPWDAG MADALGEAGQ RRLRRGGILP LTAAQGLAAF DAALTTARPL LVPVAFDPAG
     LHAAASAGAL PAVLAGLVPA GAGAGGPDQR ALAAFQRRLT QLPADDLRAA LADLVARQAA
     VVLGHTAPDD VDAHQPFLEA GFDSLTSVEL RNRLGTATGL TLPTTLLFDH PTPDALVTHL
     AGRLARPDEA APQQAGTLGT LFREASATGR SGEFFAVLTA AAAFRPVFRT AAELPRPVDV
     VRLATGTEGA TLVCLPSILA ISGPHQYVRF AGALRGRRSV AAVAAPGFHH GELLPASVAA
     VISAQADAVV AHLAGRPAVL VGHSSGGMLA HGVAAELERR GAAVAALVLI DIYSHDVEAL
     AGIQPVLSAG MIEREDGYVP MDDTRLTAMG GYVRLFHGWQ PGPIAAPTLL VRAGEPMFGW
     SRDGDWRSSW PLPHRTLDTP GNHFSVMEEH ATTTARTVDT WLSELLPTDL DPKAAT
//

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