ID A0A0F0HME1_9PSEU Unreviewed; 1181 AA.
AC A0A0F0HME1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJK54898.1};
DE Flags: Fragment;
GN ORFNames=UK12_32090 {ECO:0000313|EMBL:KJK54898.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK54898.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK54898.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK54898.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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:KJK54898.1}.
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DR EMBL; JYJF01000219; KJK54898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0HME1; -.
DR PATRIC; fig|1427391.3.peg.3160; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000033409; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
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 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
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; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 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; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
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:UP000033409};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..427
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 914..989
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1007..1181
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 884..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1181
FT /evidence="ECO:0000313|EMBL:KJK54898.1"
SQ SEQUENCE 1181 AA; 123277 MW; C99CE09D561A8E60 CRC64;
MPMNYPTERA VAVVGMSCRV PGADSLDAFW QLLVDGVEAI TDVPAGRWDL DGLPDPADPA
VPRRGGFLDG VADFDPGFFG ISPREAAAMD PQQRLALELA WEALEHAGVV PDSLRGESAA
VLLGVTGDDY AALVHQHGPD AVSHHSLAGL SRGIIANRVS YHLGLRGPSL TVDAAQASSL
VAVQMACESL LSGAAALALA GGVHLNLVPD STLAFARSGA LSPDGRCYAF DARANGTVRG
EGGGVVVLKR LSDAIADGDR VQCVLLGGAV NNDGGGQALT VPDGGAQREL LRQAYDRAGV
DPAQVRYVEL HGSGTRAGDP VEARALGEVL GRERADGQPL LVGSVKTNIG HLDGAAGVIG
LIKVALSLRH GTIPASLNYS EPNPAIPMEQ LKLRVNAATG PWPEGPRLAA VSSFGLGGTN
CHLVVAPGPD QVAEETAAPT DPVPVPVTVS GTTEQALRAQ ARRLMERVEA DADLRPADLG
YSTATTRTAL GRRGVVVAAD RGDLLAGLGA LAAGQAAPNV VEGTAVPAPG VVWVFPGQGP
QWAGMGLELW ESSPVFAARM DECARLLEGR VDWSLREVLA DAAALGRMDV MQPALFAVQV
SLAEVWRSVG LAPAAVVGHS QGEITAACAA GILALPDALR LMVERSKAIV ARLSGRGAMA
LLAMPVEEVD RDRVAIGAVN GPNAVVVSGP VDTVHAMVAE SKARGVRARM VPIDYASHSP
QVAEIRDEVL RAAEGVTATP NEVAFYSTVT GGRLPAEALD AEYWYRNVRE TVRLEDAVRA
LAADGHRVFL EASPHPVLTV PIQDTVRDTC EAVVQGTLRR ADGGLRRLLL SMADVHAQGV
PVDWRAMFEG TGARSVELPG YAFQRQPYWL GARGAAAPAP RVEPVAPDAS VAPGAPDASA
APGAPARPTG PGERELADLV RAQAAAVLGH ADPRVVEADR SFKEIGFDSV TSVELSDRLS
RATGLRLPST LLFDRPTLTD LVRHLHDELS DDDAGESRVE RGADPQQDAI AIVGMGCRLP
GGVSSPEELW RLAADGVDTI SGFPEDRGWN PDPASTGNVR TGGFLRDAPG FDADFFRISP
REARAMDPQQ RLLLEVSWEA LERSGIDPAT LRGSRTAVFT GVMNQDYVPP LHQTPESFGG
HALTGGAPSV ASGRVAYTFG FEGPAVTVDT ACSSSLVALH L
//
