ID F2R780_STRVP Unreviewed; 1325 AA.
AC F2R780;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000313|EMBL:CCA53772.1};
DE EC=2.3.1.39 {ECO:0000313|EMBL:CCA53772.1};
GN OrderedLocusNames=SVEN_0485 {ECO:0000313|EMBL:CCA53772.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53772.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA53772.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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DR EMBL; FR845719; CCA53772.1; -; Genomic_DNA.
DR RefSeq; WP_015031691.1; NZ_JABVZO010000190.1.
DR STRING; 953739.SVEN_0485; -.
DR GeneID; 69862694; -.
DR KEGG; sve:SVEN_0485; -.
DR PATRIC; fig|953739.5.peg.6330; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_16_6_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
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; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
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; 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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:SF37; FATTY ACID SYNTHASE; 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; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 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 SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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; 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 ECO:0000313|EMBL:CCA53772.1};
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:UP000006854};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCA53772.1}.
FT DOMAIN 34..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 966..1040
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 452..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 140358 MW; FCE227D08D188AF2 CRC64;
MTGTEEKLVD YLKKVTAELQ ETRRQLRGAL AASREPIAIV GMACRYPGGV RTPEALWRLV
LDEQDAISGF PTNRGWDIDG IYHPDPDRPG TCYAREGGFL HDAALFDAEF FGVSPREAQA
MDPQQRLLLE TAWEAFERAG IDPTSLRGSD TGVFAGVVHH DYATARVPET LEPYLVTGLS
GGVASGRIAY TFGFEGPAVT VDTACSSSLV ALHQAAHALR SGECELALAG GVTIMATPRA
FLSFSRQRGL SPDGRCRAFG AGADGTGWAE GAGMLLVERL SDARRKGHPV LAVLRGSAVN
QDGASNGLSA PNGPSQQRVI RKALAHAGLA ARDVDVVEGH GTGTKLGDPI EAQALLATYG
QERDAGLPLH LGSMKSNVGH SQAAAGVGGV IKMIEAMRHG ILPRTLHADE PTPHVDWSAG
DIELLTRRRA WPETGRPRRA AVSSFGISGT NAHVILEAPP EEPARDAAET RPEARSREAA
EGRREAAGQG RTETGPGPSA TPPEAPGRAR PPVPWPLSGR DAGALRDQIG RLRAHLDAAP
ADPEDVAHSL ARRAVFRHRA VLLAAPQAPA GGSPRAVTGV ARPGGTALLF SGQGSQRVGM
GSELYETYPV FAESFDAVAE HTGLPLKDVV LGGTPDGLLD RTRYAQPALF AVEVSLFRLV
RALGLDVRAV VGHSVGEIAA AHVAGVMSMA DACRLVEARG RLMDALPPGG AMVAVEVTEA
EASAALAGLE DRVAVAAVNG PASTVLSGEE GAVLKLADAW RERGVRTHRL TVSHAFHSPL
MEPMVDAFRE VVAGLDLHRP TLAGLPAEVV DPEYWVRHVR RPVRFADAVA RAREAGAVRW
LEVGPGGVLT ALAQRIVPDT EEHVFAAALR TDRPEPEALL VALSQVHVDG GTVDWSGLCA
GGRLVDLPTY PFQRQHYWIE DQPLPPTAPR PGTAPSGTGT AAEGAAAAEV PLSERLARLT
GAERLAAVRE LVLAEASETL GHTGTLITAD RTRQELGFDS LTAIELRNRI SRTLGVRLPP
TLVFDHEDLG EIASFVDARL DDAATGRSTG HGPLGEDGSG LLTELFREAA AAGRLDDAVT
LTEAAARMRR TFTDAEDPAV RRTPVWFGRG PARPTVVCLP SFSAIAGVHV YARFADAFGD
GWRVAALAHP GFVPGEPLPD SVDVLAELHA RTVLDTVGAD PFLLVGRSAG GWVAHEVAAV
LERMGRAPDG VALLDTPARA DDPRGHAVMV GGMLERDSRL VTIDDYRLTA MGGYSRLFRE
WKPEPIAAAT LLVHAATPYG ADEARIASWD LPHQAVKVTG DHFTMLERHS ATTAEAVEQW
SRSLL
//
