ID A0A402A965_9CHLR Unreviewed; 1547 AA.
AC A0A402A965;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:GCE15724.1};
GN ORFNames=KTT_55830 {ECO:0000313|EMBL:GCE15724.1};
OS Tengunoibacter tsumagoiensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Tengunoibacter.
OX NCBI_TaxID=2014871 {ECO:0000313|EMBL:GCE15724.1, ECO:0000313|Proteomes:UP000287352};
RN [1] {ECO:0000313|Proteomes:UP000287352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno3 {ECO:0000313|Proteomes:UP000287352};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCE15724.1}.
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DR EMBL; BIFR01000002; GCE15724.1; -; Genomic_DNA.
DR OrthoDB; 139272at2; -.
DR Proteomes; UP000287352; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; 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; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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 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; IPR049490; C883_1060-like_KR_N.
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; IPR013968; PKS_KR.
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:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF21394; Beta-ketacyl_N; 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; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 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; 2.
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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000287352};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1439..1514
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1522..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 170047 MW; ED6087978979B06D CRC64;
MSERKKTLPP EMQVAVIGIA GRFPGAQNVQ EFWHNLSQGI ESITFFSPET LPIWKMQPDL
LKDPNFVAAK GVIQQPEYFD AAFFGYSQRE VEVMDPQMRL FHECVWEALE DAGYNPEGKN
GSVGLFAGAS ANVYWQGISL LSRSSSAGEQ FAALSYTDKD FMNAQVAYKL NLNGPGVTVD
SACSTSLVAI HLACRSILTG ECSMAIAGGV SVPVPSPAGY LYQEGMILSP DGHCRAFDEH
ATGTVPGEGV GVVVVKSLKR ALADGDHIYA VIRGSAINND GNRKIGFTAP SIEGQTDVIR
AAHRMSMVEP ESISYVEAHG TGTVLGDPIE IAALTAAFQT EKRGYCQIGS VKSNVGHLDA
ASGVAGFIKT VLALQQQQIP PSLHYEQPNP QIDFAHSPFV VATRLQPWLT EGGPRRAGVS
SFGIGGTNAH VILEEAPPRS ASGPSRPWQL LPLSARTETA LPQVITRLKQ HLETHPELVL
ADVAHTLQVG RAHFSHRRAL VCSSVAEAMA ALDEALHTPE QPRKRPQKTP TIAFLFPGQG
SQYVNMGREL YEQEAVFRAV MDDCFVRAEA YGLPELKAVL YPAQESLEAQ ERLTRTELAQ
PALFSVEYAL AQLMSSWGLR PHSLLGHSLG EYVAACLAGV LTLEDALRLV IRRGHLMGQA
QPGVMVSVSL SEGELQPYLQ GQLSLAASNA PALCVVAGSA SEIEALEERL QQDGRRFRRL
QTSHAFHSVL MEPILASFEQ EVRQVTLSEP RLPYLSNLTG GWMQAQEATS VRYWVQHVRQ
TVRFGQGIDQ LFENEDTILI EVGPGTTLST FARKSQRATR ESVIVSLLRH PQDQQPESAC
LLKGIGRLWE AGVDLEWSKL LRSEQRQRLS LPTYPFERQR FWLDETLVES AFLAERRLGP
TSPAAITHAS TQKTYFYLPT WERQPQLQQI HSQQPRSHAT YLFFQDDDGI TAALAERLQG
DGCTIITVTK GSAYTNQLAS SAHLFSIDPE QEEHFQRLID DISGTIDTII YGWGLEHSFA
HEDRPVHMQT SGYSGLLSLA RAVARKQAGS THITILSQSI FEVIGTENLR PEQALLLGPH
KIIPQEYKNI TCSMIDLALS QEDALLLDQL AAEVVYGRVE GIIALRGKYR WTQTFCPFQP
GENDASLLKS RGTYVITGGL GAIGLTFAAT LARTSQANLV LISRSHFPDR STWDEWLASH
AEDDKTSQTI RTLIALEQSG STLLIRQADV ADREAMKKVI ADVLSNFQCI NGVIHCAGVA
DGALIQGRTQ AWEQRILSAK VQGTLLLDEL LQDVAVDFVL LCSALSAVVA PIGQVGYVSA
NSFLDAFAQY KCRQSSTRWL SIGWDTWRDA GMAVVSDALL KASVSHADYQ ARLEEQTGYG
ISNEEGASIF LRTLPLSIPY ILTTRAELAQ KFDENRALAQ LYAQQTSVQS LGAPLQTIET
VVEIERVIHD IWTKFIEIDA RDQHSNWFDL GASSLDIIQV ASMINAALGT DVTVPDLFTF
STIQALADFI YHKNGKPEAV SVQENREERL DAGKSRLKNR LERTKRK
//
