ID D2B1E2_STRRD Unreviewed; 1160 AA.
AC D2B1E2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Thiotemplate mechanism natural product synthetase {ECO:0000313|EMBL:ACZ85407.1};
GN OrderedLocusNames=Sros_2429 {ECO:0000313|EMBL:ACZ85407.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ85407.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ85407.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
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DR EMBL; CP001814; ACZ85407.1; -; Genomic_DNA.
DR RefSeq; WP_012889152.1; NC_013595.1.
DR AlphaFoldDB; D2B1E2; -.
DR STRING; 479432.Sros_2429; -.
DR KEGG; sro:Sros_2429; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_2_12_11; -.
DR OrthoDB; 4537517at2; -.
DR Proteomes; UP000002029; Chromosome.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 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 SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002029};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 499..574
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 605..1033
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1119..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1160 AA; 120660 MW; 62F539C4FAB97AC8 CRC64;
MQHTVVGRFL DVVNNNPDRV AVHSVDSSIT YAELAYTAGG IRHLVAAAGG RSGARVGLLT
GHDPTIIAAI MGTLLSGCVY VPLDPSYPVP RLAYMLDDAD VTVLVTTRGH EALARTLLGD
RSCQVVLVED ATPAPPLAAG PIEPDSLAYL RYTSGSTGVP KGVAQSHRNL AHCVGNQIES
LSITAEDRLS LLASVSFDAS IPDIYPALLT GAAVVPIDVR ALGPGELVRR LADLGVTVYH
STPTLYRYVL DALGPEGRLP SIRTVLLGGE RVTGADVAAG RGRFAGDCWF VNGYGATEAT
FVAHHRTPFD APQADPEAGP LVPIGRALPG YEVVLLASAG GEGEIALRSP YLALGYWRDP
ERTAERFTVD GEGRRVYRTG DLGRELPDGT LVCLGRLDRQ IKVRGFRVEP AEVETYLTGQ
PGVARAVVTL AGDRLVAHVQ PSAGAVLDPA AMRRGAAEVL PDYLVPTAVV VLDALPLTPT
GKVDTLALPA PGPARAGERP ATPAEATVHD AWCDVLGVAQ VGVTEPFFDA GGHSLLLGRL
QQRLADVFGT PVPMMTLFEH TTVRAQARAL SAPAAAPSPR PAVAAASAAA DPVDLDDFDD
FDDLDGHVAV VGLACRFPGA PDPAAFWSAL SDGVDAIWDY SDAELRELGI GAALLADPAH
VKAGGKLDGV ADFDAEFFGF TADEAARTDP QHRLFLETAW EALEDAGCDP DRFDGQIGVF
ASTSANRYFL FHLFGNPAAG SPDDPDDWEG RILPHQRADH LPGQVAYRLG LTGPAIAVQT
ACSSSLVAVC MAAQNLADHR CDLALAGGVT VTWPRHRHTP GGMTSPDGRC RAFDAAANGS
GFSSGSGVVA LKRLADAVAD GDHVYAVIPG WAIGNDGAAR AGFAVPGLTG QVSAVTEALG
DAGISPDEIG MVEAHGSGTP LGDAIEVEAL TRAFRAAGAR GTGYCALGAV KTNIGHTDAA
SGIAGFIKAV LAVRHGQVPG NLHLDSPNPQ LDLDRGPFYL PAKTAPWPDG RRRVAGVSAI
GIGGTGAHVL VAQAPEPAVT PPVTGGRYLF PVSARSPEAL RAAIVRLRDH LAANPHLSPA
DVAHTLTAGR RSFAHRAVVE CGSLAEAIAA LDPDLLMPRS GGADTPAPPP SGSVAPGRRV
PLPTYPFQRQ RYWIDPPGGT
//