ID A0A1Z2LCU9_9ACTN Unreviewed; 1720 AA.
AC A0A1Z2LCU9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Acyl transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SMD11_6574 {ECO:0000313|EMBL:ARZ72150.1};
OS Streptomyces albireticuli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ72150.1, ECO:0000313|Proteomes:UP000195755};
RN [1] {ECO:0000313|EMBL:ARZ72150.1, ECO:0000313|Proteomes:UP000195755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ72150.1,
RC ECO:0000313|Proteomes:UP000195755};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT "Streptomyces albireticuli Genome sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP021744; ARZ72150.1; -; Genomic_DNA.
DR KEGG; salj:SMD11_6574; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000195755; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
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; PF00501; AMP-binding; 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; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
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; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 554..630
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 645..1072
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1571..1648
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1720 AA; 179101 MW; A91D4CB1E6745FEB CRC64;
MVSVHTDDYA IDPPADTAGV LGGFTLPEVF EAAAATAPDA VAVVDGDRSW TWRQWRVEVD
ALARGLQESG VTPGDVVAVR LPNCWEFETL HLAAAAVGAV LLPVHQGTSE ADTRGLLTRA
EPVLLVLSAA GGTAPEAARA LLRDVPSLRS VLVTGAFEPE AGEPGIAPFD GLPAAWAGHT
PRPVDVTPEM PLLLVPSSGT GSARPGLCVH SHDGLLSNTA AVTAEASDVF RRPVLTACPL
THLFGLQSMH TALFAACGQV LLTGWDPDRF LELARRHDPG VVFAVPAQLH DLVTRLAGPD
GPTGFRPHQV RTAGAPVPSA LAGDVEAVLG CGLAVVWGMS EAGTGTCTRP GDPAGSVGRP
VNGSRVRVVD EHGAECPAGD TGELQFRGPG LFRGYFREPE RTRSAVTEDG WLRTGDLAAV
GPDGLVVLHG RATELINVGG RKFSAAEVQG LLAGLKGLGP LAVVGTPDPR LGECPTLVVT
DHADPAIGLT EVTAFLRGLG VADHKIPLEL AGVRALPLTP AGKLDRRALE RLLAGNEAAP
APVRPGAAPP RSTEEALELV RTCVGRVLGR GDSPGPFSPD AGFRRLGLDS LLTVRLRNLL
REETGLPLPA TLAFDFPTPL AVARVLTGQE ETAEEAPPAA GADSAEPVAI IGMACRLPGG
VDSPRALWDL LADGTDTMSG FPTDRGWDLD RLFDDDPDRP GTTYAREGGF LHDAGHFDAG
FFGLSDQEAT ATDPQQRLLL EAAWETFERA GIDPTSLKGT RTGVFTGAAH RDYAAGLAVA
QGELEGMLGT GTAGSAVSGR LAYTYGLEGP ALTVDTASSS SLVALHLACR SLRSGESTLA
LAGGVTVMAS PAPFTHSARL RALSPGSRAR AYADGADGSA WSEGAGLLLL ERLSDARRNG
HRVLALVRGS AVNQDGASNG LTAPSGPAQQ RVIRQALADA RLTPQDIDAV EGHGTGTPLG
DPVEAQALLA TYGRERPEGR PLWLGSVKSN IGHTQAAAGV VGVIKTVLAM RHGVLPRTLH
VDAPTSRVDW SAGSVRLLDE ARPWPRTDGR ARRAGVSSFG LTGTNAHAIL EEAPAEDDTE
TTAGTPEPAT AAPAPWILSA RSQAALRAQA QRLAERGQAR LGLTAQDVAY SLATTRALHR
HRAVISGPGH EELLSAAAGF GEGKRVSGVT VEHSAPGGLG IVFPGQGCQR LGMGREAAEA
FPVFAAALRE VCDVMDTLLE RPLTSVMWAD PDSEEADLLD ECGYAQPALF AVQVALYRLF
ESWGVVPDLV AGHSAGETVA TYVSGGLDLK DACVVTEARG RLMDELPPGG AMVAVRISES
EVAPLLAELP GPVAIASVNA PNSVVLAGAE GPLAALTDRL NAAGHKTRRV AVNGAGHSPL
VEPMLEELGA VARGLSYSTP TIPLVSTVTG RRMSPEDAHD PDHWVRHLRD AVRFTDAVDR
IRDERITRFL ELAPHPVLTP LIDECLEGAD PGHGAALVPT LRAGEGERQA LLTAVARLHA
HGVPVDWHAV LPDARPVPLP TYPFQRRRFW LASDPTGRAV AGPVGDAADE VATADGAPEL
AARLAGLEEP AQDALILSLV LDEISAVLGD EAGIDESGQT FKLMGVTSVS AVELRNRIHT
ATGVRLPATL VYDHPTPEAV VRLIRERLRP SATALPPRDV ASVVAELESL LASGAEVSGE
TVARLKAMAA GRDAETPSTG ALDLASASDD DLFRLMDGVG
//
