ID   A0A1I0C674_9ACTN        Unreviewed;      1416 AA.
AC   A0A1I0C674;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Thioesterase domain-containing protein {ECO:0000313|EMBL:SET14857.1};
DE   Flags: Fragment;
GN   ORFNames=SAMN05421811_102191 {ECO:0000313|EMBL:SET14857.1};
OS   Nonomuraea wenchangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=568860 {ECO:0000313|EMBL:SET14857.1, ECO:0000313|Proteomes:UP000199361};
RN   [1] {ECO:0000313|EMBL:SET14857.1, ECO:0000313|Proteomes:UP000199361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5598 {ECO:0000313|EMBL:SET14857.1,
RC   ECO:0000313|Proteomes:UP000199361};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOHX01000002; SET14857.1; -; Genomic_DNA.
DR   STRING; 568860.SAMN05421811_102191; -.
DR   Proteomes; UP000199361; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR   Gene3D; 3.30.70.3290; -; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
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; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199361};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1035..1110
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:SET14857.1"
SQ   SEQUENCE   1416 AA;  148419 MW;  62C48D57467DACC3 CRC64;
     GLREIILGES DVLDQTVFAQ AGLFAFETAL YRLLESLGVR PDFVAGHSLG EITAAHVAGV
     LELADACRLV AARGRLMQAL PAGGAMAAIG CGEEEIAPVL RGDISVAAVN APGAVVVSGA
     ASQVEQVIDW ARERGYRTRP LRVSHAFHSP LMEPMLAEFE QVVAGLTLRR PELALVSNVS
     GDLAGEEITD PGYWVEHVRR PVRFADGVQV MRERGVTHFL EVGPDAQLTP MVEQTLTRQD
     GEEPSVVALL RRDRDEITQL VAGLGQAWTR GTGVDWTAWP TGARGSDLEL PTYPFQHRRY
     WLQLPSTGDP VALGQTSVDH SILGAVVEQP DGGAILTGRL SVSAQPWLAD HVINGTAILP
     GTAFVELALR AGDQVGCPAI DELTLHAPLP IPDTDGVTLQ IILSPPDEDG RRQIGIHSKD
     DHGNWTRHAT GTLTPTPAIP ADLSHAWPPP DAQPLDVTGL YDRLVDHGYG YGPAFHGLTH
     AWQHGDDLYA EVSLPTDVAD PAGYGVHPAL LDAAMHVGML AGQGAGEDGP LIPFNWNGVS
     LHAAGAATLR VRLRRLDGDA VTRLDIADSS GRPVVSVEEL TARPLAPGQL SGAIPAQWLY
     EVAWRPVGER GAEAVGAAAE VLDVASLTGA GEPVDGDVPA RVRRVVGQVL NELQTWLTEG
     DTRPVVVVTR GAVAVTDAET PDPAQAAVWG LVRAAQSEEP GRITLVDLDP DLAGAQVTDG
     MSTPALRSGE PQVALRGDRL WAPRLERARL REELATPWPT DGTTLITGGT GGLGALMARH
     LVTEHGVRRL LLISRRGLDA PGAAELRDEL TEQGAEVTVA ACDVADRDAL TVLLEEIPDL
     RAVVHSAGAS ANAVLADLTP ELVDQVAAPK ADAAWHLHEL TQKHDLAEFV LFSSSASLVD
     NPGQGNYAAA NAFLNALAEQ RRAAGLPART LAWGLWGGEA GMQSLLRDDD LARIRRWGML
     PLPVDAGLAL FDAARRADAA VLAPIRLDPA AVRARADGVP ALLQDLAPAV RRTTAAPGGN
     ELEPLAALGP EERLERLVEL VRRRAAQVLG HADPEPVEPD ADLVGLGLDS LAAMELRNAL
     NSATGVRLPA TAAFDYPSVR ALARVLDEEM APAPVAAAPG VPATAHGDGP AAQDVPGAAE
     TLSGLFRAAA AAGKIEEGMT LLHAAAAVRP RYGVADAPAR TPVVLSTGPR RPRLFCLNSP
     MAFGGPHQFV PLATEFREVR DLAVLPVPGF VREESLPDSL DALVHGLARA VTGGAEAVAE
     PYALVGYSAG GVFAHALAGA MAAAGQGPAA VILLDTHVPG AGESTAVWSS IVGGLLDREA
     VFGPFTAARL SAMGWYAALL SQWRQGELAA PTLFIRANQG VATPGGTTAG VGAGWQPAIT
     PGTAVREVAA DHFSILESEA RQTAAVIEEW LAQLSG
//