ID D2B8U3_STRRD Unreviewed; 1929 AA.
AC D2B8U3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Polyketide synthase modules and related protein-like protein {ECO:0000313|EMBL:ACZ89699.1};
GN OrderedLocusNames=Sros_6999 {ECO:0000313|EMBL:ACZ89699.1};
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:ACZ89699.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ89699.1, 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; ACZ89699.1; -; Genomic_DNA.
DR RefSeq; WP_012893430.1; NC_013595.1.
DR STRING; 479432.Sros_6999; -.
DR KEGG; sro:Sros_6999; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_30_2_11; -.
DR OrthoDB; 4537517at2; -.
DR Proteomes; UP000002029; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 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 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; 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; IPR013968; PKS_KR.
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; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002029};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..461
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1929 AA; 204360 MW; 93EB11A1D7216EE3 CRC64;
MSRIAIVGMA CRYPDAASPR ELWENALAGR RAFRRLPDVR MRLEDYWDAD PATPDRFYAR
NAAVIEGYEF DRIAYKIAGS TYRSTDLTHW LALDMAGLAL ADAGFPSGEG LPRERTSVVV
GNTLTGEFTR ANVMRLRWPY VRRTLAATLK EQGWDDDRLA TFLDDFEATY KNPFPAIDED
TLAGGLSNTI AGRICNHFDL NGGGYTVDGA CSSSLLSVAT ASKALLDGDV DVAIAGGVDL
SIDPFEIVGF AKTGALAKGE MRLYDRGSNG FWPGEGCGMV VLMREADALE ARHRIYATIA
GWGISSDGKG GMTRPEVSGY QLALRRAYER AGFGIDTVEL FEGHGTGTAV GDRTELTALS
GARSAANPDA APAAVTSIKG MIGHAKAAAG VAGLIKAVMA VHEQVLPPTI GCVDPHEVLT
EESSSLRVLR KAEPWPAGAP VRAGVTAMGF GGINTHIVLE KTGPRRRVPL PSRTRMLASS
LQDVELLLAD AASPQALRER LTQLIDFVPQ VSYAQLSDLA ATLQRDLRDL PYRAAVVVSS
PEDAERQLRR VLEALDAGET SLFARDGRAF LGHADGTGRV GFLFPGQGSG RGTSGGALRR
RFAEVEEIYA KAALPTTGDM VATAVAQPRI VTGSLAGLRV LSALGVDADI AVGHSLGELS
ALQWAGAMDE ETLLHVAGVR GRAMADNSAS GTMAGVRATP DVVTGLAAGL PVVIAGYNGP
EQTVVAGPVE AIEAFGRKAA DAGVRCTRLS VSHAFHSPLV APAADALGAE LAGEEFGPIG
RQVVSTVTGE ELAPDTDVPA LLRRQITEPV LFTQAVELAA KDIDLFVEVG PGRVLSGLAS
ALTKVPAIAL DTDDESLGGL LRVAGAAYVA GVPIIHEELF QGRLIRPLEV GAEFTFFASP
AEQAPEVKLR AGVRKVDEPV KTVVTGTQQP EVQPGESSVD LLRRLAAERA ELPLEMVGED
SHPLDELHLS SVTVMHIIDQ ATQRLGVPAA QAPTNLATAS LRELAEALDA LAQNAQAADS
APARLVAGSA PWARPFAVDL DEVPLPARTT PEENGQWQVF GAGESPIAEP LRQALEREKV
GSGVLVCLPQ DCSEEHVEQA LLGAKAAVRG AQDSRFVLVQ HGRGAAGLAK TLQLEAPHLR
TTIVHVPAGP EAVGRVVAEV AATSAYAEVH YDGDGVRRVP TMRALPVRPA RTQQPLDGTD
VLLVTGGGKG ITAECALAVA VDTGAKLAVL GRSDPADDRE LADNLRRMAD SGVSVHYARA
DVTDLDQVRR GVAEVEAALG PVTAVLHGAG RNEPGGLASL DMAAFRRTFA PKVGGLRNVL
AAVEPGRLRL LVSFGSIIGR AGLHGEAHYA TANEWLADLT REVAEQHPQC RSICMEWSVW
SDVGMGERLS VVDGLARKGI TPISPEQGVQ IMRRLVADPD APTVVVISGR TEGIDTVRYD
LPSLPLLRFV DRPLIRYHGV ELVTEIEMNA GTDLYLADHL LDGNLLFPAV FGMEAMAQVA
SAATGWETVP VIEQAEFLRP IIVPPTGSTT VRIAATVTDH ETVEVAIRSA ETGFDVDHFR
ARLRFTGDGA PDGPPGQIGE GLPVVPLDPA AEMYGDVLFQ GTRFQRLRRY HRAAARHVDA
DVAAVEARDW FAAFLPGELL LGDPGMRDAL MHGNQVCVPD ATLLPTGIER VHPGGAALAE
AGELRYCATE RQRDGDTYIY DIAVRTAAGD VVERWEGLRL QAVRKKDGRG PWVTPLLGSY
LERTLEDLTG SRVAVAVEPH YPDVPEGDEG HRVLAAVAVG RALGHQAEIR YLPDGRPETG
GDRTVSASHT AGVTLGVASA GTVGCAVERV TERPAEAWRE LLGGHVPVAE QVSAQTGERL
DTAATRVRAA VECLRNAGLS PDAPLTPAPA QRDAWVVFAS GDLRIATLVT SLRDTPDPVV
FAVLTEGRS
//