ID A0A1Q4WH11_9ACTN Unreviewed; 2095 AA.
AC A0A1Q4WH11;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OKI09388.1};
GN ORFNames=A6A06_01365 {ECO:0000313|EMBL:OKI09388.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI09388.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI09388.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI09388.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI09388.1}.
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DR EMBL; LWKZ01000001; OKI09388.1; -; Genomic_DNA.
DR RefSeq; WP_073757950.1; NZ_LWKZ01000001.1.
DR STRING; 1718985.A6A06_01365; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000185893; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase 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 GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
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; IPR020843; PKS_ER.
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:SF37; FATTY ACID SYNTHASE; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 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; 3.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000185893};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..439
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1990..2064
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2062..2095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2095
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2095 AA; 222348 MW; D097A5F8E021E53C CRC64;
MSSIRGDGCD VLPAPWDEPV AVVGAACRAP GGVDSLAALW RLLAEGRETV GPVPKERWDA
DAIAAGLPER VACRIRRGGF LEGDLGAFDA QAFGISGAEA TWMDPQHRLL LMTAWEACEH
AGIPVDALRG SQTGVFAGMY WMDNYLRGHR GPQETEGYWF SGGVHGVGVG RVAYLLDLHG
PSLSVDTACS SSLVAVHLAC QSLRAGECGM ALAGGVAAGL GPEVTVASSR WEMFSPTGRC
HAFDKKADGY LRAEGCGVVV LKLLKDARRD GDRVLAVLRG SAVNQDGRSV RLTAPSAQAQ
AAVFAAALRR AGVRGEQVGM IEAHGTGTTI GDPLEFSAIK EVYGAGDYPC AVGSIKTNIG
HTEAASGVLG LLKAIVSLRH GRVPATLHFT EFHPQIDAGE CRLYVPTSME PWPVPQGPRL
AAVSSYGVGG TNAHVIVEAA GDDAATRGGL ESVVEEGRRA VYLLSGSSQA AVRRYAARLA
DWLDSDDGQG VELPDIAHTL AVRRSHGARR AAVVAASRDE LVSRLRHLGA QEETGGTAAG
SVRPSGPGPV FVYSGHGSQW AGMCRGLLDT DEAFTAVIDE LEPLLRQEAG FSLRGVLGRE
DTVTGVARVQ PTLFAVQVAL TAMWRARGVQ PAAVIGHSMG EVAAAVACGA LSIRDGVRVI
CRRARLLTRV TGGAMAAVHL SADHVRRALV ERRAAEVEVA VLAAPESTVI SGDAAAVERL
VGLWEREGVG VARIQVEVAS HSAQMDPVLD DLRKRLAELA PGRPRCRFYT TVADDPRAEL
PLDADYWVAN QRRPVRFAAA VEAAAGDGHC AFVEINVHSM LARAITATLA DCDAFVTPTL
LRHGDEVLDF ETHVAALHCH GVPVAWRRQY GRGRLAEVPA TCWDPGHHWI EPSALTRGGT
VADAGGQPPH PLLGTRIRDP REPGRHLWQC DLAPHVTAWL RDHHAAGAPA MPGAAWAEMA
LSAARTIAPG GLCPRVRDLT FDAFLPLGAA GIRLTSQSEV RTDREAAWQV FSPTEGGSFE
RHSHATLTAV PQAGGPPPAR LDSLRAACPQ SIDVTAVRER WRTSCGISYG PAFDVMATLQ
VSPSGHGPAA LAAVAIPDAT RSLTARFQWH PALLDGCLQS LLALWTTRVD LPPGSAYPLG
IGELQVHGAT ADGVWCHVRA TSLDTHQITG SLCLLNADGA VLAHADGIRF VHQPTRAARR
LQPYLHQLHW QQQDLIAPAR TETGSWLAVT EGEPQGWQKQ LLAELAARAP LTRLPVPADA
DEATLGERLE AALPQTGPAV TDLLLIARQD DATDDQAVEQ AHRRIAHIIT TVQHLDRIRP
ATRLHLITHH AHSLPCDQHV ALAHAGIRGL HRVLTYEHPA LRPVLLDTDT LTSPGKIAAQ
LLADDPEDEV AWRSDQRYVL RIVPAPLTPH ERRTISCTPH TTSLQADTDG TTLTYTVQPN
VDAPPDETAI TVTATCSTDL GYDLPLMPCA GITDHGTVAA LVPTTAPTSR TTAAAHWTVP
VPATSNAAQV ACSLLPYLAA HYALHHLARL AAGERVLLHG ATGTLAAAAR HTATAAGADI
SVSAPDNEPG LRLPHTPGTI RADQLAGVNR RFDVILDTDG RAAPDFGSLL APGGRLVTCR
AGSRRPPTVT NHNTLTCTLN LAGLLRDDAD TASALLAEIG QALVQETLPP LPYTDHPLAD
LALTPGATPP DTRPAAYRWP HGPLTAHIPP QQIPLIRPDG GYVITGGLGG LGLVLCRWLT
DHGAGTIILS SRSSPTPEAT TAIERLRTAG TRIDIINADI AEPGTAERLL HAAQRHGHRL
RGIIHAAAVV DDAAVTRITP GLLDRVWQPK ANGAWLLHQA STRYDLDWWV AFSSFVPIIG
SPGQAAYAAA SAWLDELITH RRAAGLPALG INWGAWAEVG IGARTIGDRG FATIPLTDAL
DGLELLLTHD RTHSSFVNID FDKWLAPYPQ AAAAPFFSHL LRQSTAALTT SRHEDPLAAL
RSADSSRRPA LLARFITAQA AELLYCDPDR IAPHTSLLTV GVDSMIATQL LNRLQQSVGL
TIPQNVLWAN PTVTALTDYT LNHLPHQSPP TAPDPIPPNA PSLPPHAPAK PAPPP
//
