ID A0A0M8VPX2_9ACTN Unreviewed; 1269 AA.
AC A0A0M8VPX2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KOV70249.1};
DE Flags: Fragment;
GN ORFNames=ADK64_03130 {ECO:0000313|EMBL:KOV70249.1};
OS Streptomyces sp. MMG1121.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV70249.1, ECO:0000313|Proteomes:UP000037687};
RN [1] {ECO:0000313|Proteomes:UP000037687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:KOV70249.1}.
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DR EMBL; LGDV01000010; KOV70249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8VPX2; -.
DR STRING; 1415544.ADK64_03130; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000037687; 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 GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd08952; KR_1_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 6.10.140.1830; -; 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; 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; IPR041618; PKS_DE.
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; 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; PF18369; PKS_DE; 1.
DR Pfam; PF00550; PP-binding; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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:UP000037687};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 615..690
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 718..1145
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 315..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOV70249.1"
FT NON_TER 1269
FT /evidence="ECO:0000313|EMBL:KOV70249.1"
SQ SEQUENCE 1269 AA; 130666 MW; 76F0E6AC280FF850 CRC64;
GVGVDWSPLF AGGGVRRVEL PTYAFQRRRY WLDAPVVSSG APTTGEGEAE AGFWSAVERA
DAAELAMTLD ADGELVGELL PALSTWRRKS LDRSTVNSWR YKVTWRPLST PPAIGRLAGT
WLLAVPAALR DDPLVAEAAE ALTRSGAQVV PVEVDCATVE RAALAQTLAA ATSPQEPSPI
AGVLSLLGLD EAPHPDHPVV PQGVAATLAL VQALGGSADD GGSQIDAPLW LATRGAVSVA
GTDRLTSPAQ AQVWGLGRVV GLEHPERWGG IVDLPMELGE STGQRLAEVL GGTGGEDQLA
VRRSGTYIRR LVEAPQTAKN TRTSRSPRAN PTAWQPRGTV LVTGGTGALG SQVARWLAKS
GAEHLLLVGR RGAEAPGAEA LRAELHALGT EVTIAACDVA DREALARLLA EHPPTAVVHA
AGVGQLTPIT DTTLDGYAEV LGAKVGGAVN LDELLAPDQL EALVFFSSNA GVWGSGGQGA
YGAANAFLDA LAQHRRARGG HATSVAWGSW GGAGMAVEEG ADAHLRARGL RPMDPDLAIA
ALAGALDQDE TTVTVADVDW ARFVPLFTSA RSRPLIAELP AVRALLEEPE EPDSGSGDAA
LRQQLAALSA TGQADLLLAL VREQAAAVLG HSEPGTVAAG RAFRELGFDS LTAVQLRNRL
SARTGLRLPT ALIFDYPNAT ALAGHLRDQI LGVAAQGTTA QDAAQRAGAG SGAGPQGEDP
IAIVAMSCRY PGGAESPEAL WKLLADGVDT VTPFPTDRGW DLDALYDPDP DRPGTSYVRE
GAFVHDVGHF DPSLFGISPR EALAMDPQQR LMLEASWEAF ERAGIDPELM KGSATGVFVG
ASSQGYGAGA RQAAEGAEGY YLTGGATAVV SGRVAYTFGL EGPAVTVDTA CSSSLVALHL
ACQSLRQGES SMALVGGVAV VVNPVAFVEF SRQRGLAPDG RCKSFAAAAD GTAWGEGAGV
LLLERLSDAR RNGHEVLAVV SGTAVNQDGA SNGLSAPNGL SQQRVIRQAL AAAGLSGGDV
DAVEAHGTGT TLGDPIEAQA LLATYGQERP SGQPLWLGSL KSNIGHTAAA AGVAGVIKMV
LAMRQDTLPR TLHVDEPTPH VDWSAGAVSL LTEAVPWPRP DGRPRRAGVS SFGVSGTNAH
VIVEDAPAAV GDEGASAVGG AGTPPVVVPW VMSTASEPAL RAHARRLGAF AGASDDLDPA
AVGHSLATSR AMLDRRAVVL GRDVRQLTCG LDALARGEVS PDVVEGSVTE GALAFLFSGQ
GSQRLGMGR
//
