ID C6WK73_ACTMD Unreviewed; 2107 AA.
AC C6WK73;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Thioester reductase domain protein {ECO:0000313|EMBL:ACU38286.1};
GN OrderedLocusNames=Amir_4440 {ECO:0000313|EMBL:ACU38286.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU38286.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU38286.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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DR EMBL; CP001630; ACU38286.1; -; Genomic_DNA.
DR RefSeq; WP_015803173.1; NC_013093.1.
DR STRING; 446462.Amir_4440; -.
DR KEGG; ami:Amir_4440; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3320; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000002213; 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:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR CDD; cd05235; SDR_e1; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; IPR013120; Far_NAD-bd.
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; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
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; 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; PF08659; KR; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 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 SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..457
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1631..1707
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1872..1895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2107 AA; 221139 MW; D69646D16D05B22B CRC64;
MPDDQKAVEY LKWVTADLRR TRDRLSELEA AADEPIAIIG MGCRFPGGAH GPDGLWRLVA
EERDAITEFP ADRGWDVAAR YDPRPGRPGK TYTRHGGFLH DAAEFDAEFF RISPREATAM
DPQQRLLLEV AWEAVEHAGI DPRSLAGSRT GVFAGIAAQT YNQSLDQREY AGYLATGVVG
SVASGRVAYA LGLEGPAITL DTACSSSLVA AHLAVRSLRA GDCDLALAGG ASVTGSLDGW
LEFSAQGNLA PDGRCKSFAA SADGTGWSEG VGLLLLTRLS RARELGHPVL ALIRGSAVNQ
DGASNGLAAP NGPAQERVIR AAVADAGITP ADVDAVEAHG TGTTLGDPIE AQALLAAYGR
GRPGDRPLWL GSLKSNLGHA QAAAGVGGVI KMVQAIRHGL LPRTLHVDEP TPEVDWSRGA
VELLRESRPW PEVDRPRRAG VSSFGISGTN AHLILEQAPE PEAAPAAEPA PAAPRDLAGV
VPLLLSAPTD AALRARAADL ADHLDAHDHH PADVAHALVA TRTRFDRRAV VVGGDRAELA
SGLRALADGS PDALTGSGRP GGLALLFAGQ GGQHAGMGQG LRAAHPVFAR ALDEAIDAVD
AELDGHAEHS VRAALERHDG LHDRMVYAQT ALFALETALF RLVESWGLRP DWVAGHSVGE
VAAAHAAGAL SLGGAARLVA ARGRLMDGLA PGGAMIALEA TEAEAERELA GEPLVGVAAI
NGPRSVVISG AHRPAEAVAA RFAARGRRVK RLRVSCASHS PLMEPMLAEF HRIASTVEHA
PPRVPLLSTV TGRPVEDGEL GPDHWTRHAR RSVRFLDAVT RLDELGVTAL LEVGPDGALT
AQAQRVLDDS ERDGRLAVPL LRPGHDEPRT AATALGALCA AGLTPDWAAV HGRDARPVEL
PTYPFQRRRY WLRATGSTEV ADLGLAPADH PLLGSLAQRA DADTALLAGR LSTAAHPWLA
DLPGSADAAL VDLALRAADR TDCDVVRELS LHGPVRLAAG DATTLQLAVA APDDAGERAF
TVHARADAAD GAWELVASGA LARQVALPAP PAEEWPPPGA QAVEVDAALA GLGVTAVLRR
GDELFADLAP PADRLAAGFG LHPLLLHAAT APRPGGDATR PRRWRDVRLH ATGAGALRVR
LTPGDGRSFA LTAHDRSGLP VLTVGEVATA PADRGRGAEH DALFRVTWEP TRLPAADRAP
EWAWDSDHRP GGRAPEVLLL RPSPARPHDP VPAAHDLLRH AMARLRDLLA DPALAATRLV
VLTEGAVATD AAEEADLAGA ALCGLVRSVQ SEHPDRVVLV DTATGGDPDP APVLAAALAV
GEPQFALRGD RVLVPRMSRL PLPWPPATPW RADGTVLITG GTGALGATVA RHLVRGHGVR
RLLLTSRRGP EAAGAADLVA ELTALGADVT VAACDVTRRE AVRDLLACVP DAHPLSAVVH
TAGVLADGML ASLTEDDLTS VLRPKVDAAW HLHELTRDAD LSAFVLFSSV TGVMGTPGQA
NYAAANSFLD ALAAHRARRG LPAVSVAWGL WEGASTMTEH LTEVHLTRMA KEGLLLLPVD
LGMAVLDAAA GQPEPAVVGM PVDLAATRAH HAQPVLMRGL TRTRLRPESA EAGAAGGGAL
LERLAALDAP ARRSLLLGIV AEHAAAVLGR DEPLAADQVF QDAGFDSLTA VDLRNRLAKV
VPAPLPATAV FDHRTPEALA GRLLADLLGE RVAETGVDLA AEIALAPDVV ADTAPHLTTD
PADVLLTGAT GFLGAFLLRD LLRHTRARVH CLVRGADEPD ARRRLLRTAE RYGTGIDLDR
VEVVVGDLAQ PGLGLAPEVF DRLARTAEVV FHAGAGVNWI YPYPELKAAN VGGTEEVLRL
AARHRTVPVH HVSSTGVYDQ RPGTRLTELD PTGPPEVLGN GYRRSKWVAE GLVELARRRG
VPVSVYRVDS ISGDQERGAC QDQDFVWLSV RGILESGAAP EGLDIAFHPT PVDFVSRAVV
ALAGRPASLG ETGLGETYNV SNEDSLTFTE VVTALRGMGY DLPEVPRERW SELVRRDPSN
ALTPLLDVFE LAFTGAGGYP DIATKKLDDA LTGTPVSCPP ITGELLATYL GFFVRTGYFP
PPPGGTR
//
