ID A0A0F0HMC9_9PSEU Unreviewed; 1028 AA.
AC A0A0F0HMC9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJK54888.1};
DE Flags: Fragment;
GN ORFNames=UK12_32145 {ECO:0000313|EMBL:KJK54888.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK54888.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK54888.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK54888.1,
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:KJK54888.1}.
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DR EMBL; JYJF01000225; KJK54888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0HMC9; -.
DR OrthoDB; 4537517at2; -.
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; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
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; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 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 SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 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 302..377
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 398..824
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KJK54888.1"
FT NON_TER 1028
FT /evidence="ECO:0000313|EMBL:KJK54888.1"
SQ SEQUENCE 1028 AA; 106993 MW; FED5A486EAB6C88D CRC64;
EGAVFGPSGT VLITGGTGAL GALVARHLVA EYGVRRLLLT SRRGADAPGA AELRAELAES
GAEVTLAACD AADREALAAV LASVPAEHPL TAVVHTAGVT DDGVLSSLTP ERIERVLRPK
AEGAWNLHEL TAGLDLTAFV MFSSAAGVFG GPGQGNYAAA NAFLDGLAHH RTARGLAATS
LVWGLWAQSS GVSGHLDRND LARMERSGLS ALSSDEGLAL FDAAVQTRSE AGTRHADAVL
VPMHVRIAAL RTQAAAGLVP PLLRGLVRTP VRRAVEAAAH GAGSESELVR RLAPLTVAEQ
ERALRDLVRG QVAAVLGYSG AEAVDGERAF KELGFDSLTA VELRNQLGAA VGLRLPATLI
FDYPNPATLA AHLRTELLGL QEDFDALAPT ASAAAADDDP IAIVGMACRY PGGVTSPEEL
WQLIAGERDG ISLFPTDRGW DLDALYDPNP DSPGTSYTRE GGFLHDSNYF DPAFFGISPR
EALAMDPQQR LLLETTWEVF ERAGIDPATV RGSRTGVFAG VMYHDYGTRL RTAPDEVEGY
LGTGSSSSVV SGRVAYTFGL EGPAVTVDTA CSSSLVALHL ASQALRNGEC TMALAGGVTV
MFTPGTFVEF SRQRGLAEDG RCKSFAAAAD GTGWGEGVGM LLVERLSDAQ RNGHQVLGIV
RGSAINQDGA SNGLTAPNGP SQQRVIRQAL ANAGVAAHEI DAVEAHGTGT TLGDPIEAQA
LLATYGQDRA EDRPLWLGSV KSNLGHTQAA SGVAGVIKMV MAMRHGVLPR TLHVDEPSPH
VDWSAGAVEL LTEKLPWPET GRPRRAAVSS FGISGTNAHT VLEQAPSATD SGAVGVADPA
GAQALPWTLS AKGEPALRAQ AARLHAWSDE QPELRPADVG HSLATTRAAL ESRAVVVAED
REEFLRGLAA LAAGESAANV VQGTASAGRT AFLFTGQGSQ RVGMGAGLYA AFPVFAGAFD
AVCAELEPHL ERPLREVVFA GEGGLLDRTA FTQPALFAVE VALFRLVESW GVRPDFLAGH
SIGEVAAA
//
