ID A0A2P8KRY8_9BURK Unreviewed; 2444 AA.
AC A0A2P8KRY8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Type I polyketide synthase {ECO:0000313|EMBL:PSL85719.1};
GN ORFNames=C7T35_05415 {ECO:0000313|EMBL:PSL85719.1};
OS Variovorax sp. WS11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL85719.1, ECO:0000313|Proteomes:UP000241151};
RN [1] {ECO:0000313|EMBL:PSL85719.1, ECO:0000313|Proteomes:UP000241151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:PSL85719.1,
RC ECO:0000313|Proteomes:UP000241151};
RA Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT "Isoprene degraders from the Poplar phyllosphere.";
RL Submitted (MAR-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:PSL85719.1}.
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DR EMBL; PXZZ01000005; PSL85719.1; -; Genomic_DNA.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000241151; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd12117; A_NRPS_Srf_like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00202; Aminotran_3; 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; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 727..802
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 822..1248
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1733..1811
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1908..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2403..2444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2282..2309
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2444 AA; 260272 MW; 1DAFC592A9360A74 CRC64;
MEQEPLPSST ELAALSLADL FAPRSSKPAQ AAVQVSSLDI PQALASRWST EAQQGGYLPD
TLFAAAWVLL QSRWLGTPTV EFHEALGTGA SARLELHCDG DHSAWQWIAQ VDRARRDARP
AAASAPPFAH WLREGAAHDA GATVMLQLGF QAPASLRLTG AAALMDSAIE ISLLLALADA
ATDLLDHPEA RLREIRTLPA ADRQRQLDEW NAAPGVFDPA LTVHALFERQ VAARGDAVAL
IGETGALSYR ALDQEAERLA RRLQARGVRA GDTVGVLLDR SSAAVVALLG ILKAGAAYVP
VQPDFPAERI AFMLAHSDVV LVLTQAAYKA LVPAERPLLA IDKQSPGAEA ALPPFAPAAA
DGESVAYVMY TSGSTGTPKG IEICHRSILR LVVDANYVEL PPGEAMLHAA PLGFDASTLE
IWGPLLNGGI CVVHDEKVPS GAGLARTIAR HEVKTAWLTA GLFNAVVDDD PAQLAGLRQL
LTGGEALSVP HVRRALETLP GTTLINGYGP TECTTFAATH RIPRDLPADA RSVPIGRPIN
ETALRVLSPS MALLPAGLVG ELCIGGRGVA RGYLQSPELT AARFVADPYA PGERLYRTGD
QVRWLPDGTI EYIGRIDGQV KIRGHRIETG EIEAALLAHP ALKSCAVVPQ KDPAGRLRLV
AYLVARSTEL PWSALRQHLA EHLPEAMIPS AAVWLAQLPV TTNGKLDRRA LPEPARQRPE
LAQPYAEARN EAERRVCAAF ARVLGIDPIG RDDNFFDLGG DSLLVLRVLK ELQQGSARRL
TTTLFFRQPT PAALAADMQA AEVPVPVPAE PAPARPAARN DSEAVALIAM AGRFPGAADV
EQFWDNLMAG RESISFFDDA MLDAGVSAAL RADPLYVRAR GVLDGIENFD AAFFGINPKE
AELMDPQQRV FLEICWECLE RGGYAPDQAP GPVGVYAGMY NATYFQRHVA TRPDLVEMVG
DFQVMLANEK DYITTRVANK LNLTGPAVSV HTACSTSLVA VAQAFHALRT GQCRMALAGG
ASVTCPPRSG YLYNEGSMLS PDGHTRSFDA KAKGTVFSDG ATVVLLKRLS DAIADGDTIY
AVLRGAAVNN DGGAKASFTA PSVDGQAAVI EAALAQSGVP ARSISYVETH GTATPMGDPI
EVEGLVRAYA AHTADKGFCT IGSLKSNVGH MVTAAGAAGL IKTALALHSE AIPASLHYEA
PNPAIDFDAT PFSVNSQLRP WPREAAPRRA GVSSFGVGGT NAHVIVEEAP LREPSDPASG
PQLLMLSARS PAALATAAAQ LAEHLDAHRD LSLADVAHTL RVGRKAFAQR ACVVAGSIDE
AVAALRTADS PARAGAAAPA WMPQPVFMFP GQGAQYAGMG LALHAAEPVF RAAFDECLAA
FEGVLDYDLR ERIASNDAAA LSPTSVTQPA TFALEYALAR QLMSLGVTPV AMIGHSVGEF
AAAVLAGVMR LEDAARLVAR RGALMQAQPA GIMLSVRMAA AELLPLLPEG ISLAADNGPA
VSVAAGPAEA IEQLRAALEA KGIVAKALQT SHAFHSAMME PAVAPFEALV GELALSAPRL
PIYSTLTGRL LTAEEATDPR YWARHLRETV RFSPAVREVL AQLAHPLFIE LGPRNTLATL
VRQHATKAQP APAVSLLADQ PASECAAWRL AAGRLWAQGA EIDLSPLDRR ARKHRVRLPT
TPFERKRFWV DIASSAPVAP ALVSSPAPAV PPSPIPELSM TVAVAAATSA PPARRASLVT
RLRELFENLS GADMAEVDGS APFVEIGLDS LTLTQAALQV KKTFKVNLTF RQLMESYRSF
DALAEFLDAT LPPEAAPAAP VAAAMPAAVA PQQAVAAVPA AAMPALQAVQ VLQPVPMAAA
PGGSLVQQVI AQQMQLMQQQ LVLLSAAPTV PVSLGLPVPA VEQPTPMATA AATASNTTPE
PAAEEPVPAP KYDVKKAFGA IARIHTQSKE PTERQKARLA AFMRRYVERT KKSKAFTEHN
RAHMADPRVV NGFRPATKEI TYQIVIERSK GSRMWDIDGN EYVDTLNGFG MNLFGWTPDF
INEAVKKQLE LGYEIGPQHP LAADVTRLLC ELTGFDRAGL CNTGSEAVMA ALRIARTVTG
RSTVVLFTGS YHGTFDEVLV RAGRSAKGMS AAPGVLQGMF GDVRVLDYGT PEALEFIRAN
ADDLAAVLVE PVQSRRPDFQ PREFLREVRA ITEKSETCLI FDEVITGFRC DLGGAQALFG
IRADLATYGK VLGGGMPVGV IAGKRTYMDA LDGGPWQYGD DSVPTVGVTY FAGTFVRHPL
ALAASKAALE HLKQDNNKLQ TQLNLHTAAM ADELTAFCRE VGAPLEIRYF SSLWRVSWLE
DHPLQDLLFA MMRSRGVHIL DNFPCFMTTA HSQQDIATIK SAFKESIAEM QEAELLPRRA
APKMALDPAH PPTPNARLGR DKDGQPAWFV PDPKAQGKFT KYQA
//
