ID S5YUS4_PARAH Unreviewed; 2043 AA.
AC S5YUS4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AGT08966.1};
DE EC=2.3.1.111 {ECO:0000313|EMBL:AGT08966.1};
GN ORFNames=JCM7686_1865 {ECO:0000313|EMBL:AGT08966.1};
OS Paracoccus aminophilus JCM 7686.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT08966.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT08966.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT08966.1};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(2014).
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DR EMBL; CP006650; AGT08966.1; -; Genomic_DNA.
DR STRING; 1367847.JCM7686_1865; -.
DR KEGG; pami:JCM7686_1865; -.
DR PATRIC; fig|1367847.3.peg.1851; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_5; -.
DR Proteomes; UP000015480; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0050111; F:mycocerosate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 3.40.366.10; 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; 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; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF00550; PP-binding; 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 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:AGT08966.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000015480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGT08966.1}.
FT DOMAIN 22..449
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1916..1990
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1992..2012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2043 AA; 218727 MW; 48DE22A6192C2C72 CRC64;
MCDFEENPIE REDTARPKST ATEPLAIVGM GCRFPGGVES PEDFWTLMAE GRDGIVEIPA
DRLDLQKFYD VRPEAPGKIY VRHGGFLNQP IDAFDAEYFG MSPREAAYLD PQQRLLLEVA
HEALEDAGIP AETIAGSNTG VFIGGFMVDG MLTQFSPLGR HQIGQHTAVS STLTILSNRL
SYLLDLHGPS FTLDTACSSS LVAMHQACQA IRSGECDLAL IGGVNVIFRP ETLIAMCKGG
FLSRDGRSKS FDARADGYGR GEGAGVVVVK RLSAALADGD RIHAVIRGSG VNQDGRTDGI
TVPNGEAQAD LIRQVLERND CAPETVTYVE AHGTGTAVGD PIELKALASV FGMPDQPRLV
GSVKANIGHL EAAAGIAAVI KTALCLRRGQ VPPVANLDQV NPALQLDDWG LSLPRELQPF
PTRADGQPGR AAINSFGYGG TNAHLILECA TEAEPLNDTT HDRAQILALS ARSADALKAL
AEASIARLEG MSAQDFTDYC FSAAARRSAY EHRLAVVANN AEAAQTSLRN FLEGRGDPAL
IQGQTSRKDA SPAFVFTGMG PQWWAMGREL YQQEPIFRDF ADRVDAIFTK LAGWSVLAEM
LKPQDQSIVT RTHVAQPANF IVQGGLFHLL QSWGVEPGAL VGHSVGEVSS AYAAGVLGLE
DAVRVSWLRS KLQATKAGEG GMLAVGLGAL DVLPYLSGRE DLVSIGADNG PRTITLAGDV
DALAEIADEL TDDGVFNRKL QVETAYHSPI MDPLLAPLDE GLRDLQPQVP VIPLYSTVTS
LPAEGDDYGS AYWCRNIRDS VRFSETVQEL VNDGFECFLE VGPHPVLSSA LRECLTDANV
DGVLAATLRR EQPEVIQILR GIANLYVQGV RIDWQRFNAD RPHRFVALPS YPWQRRQLWN
ESAIARDDRL GRADEARLLG RRLAVPQPLW RSEFNRNRLA YILEHQVEDS VVMPGAAYCE
IALQLAEELG DGRALHLSNL RFDQALIVAE GDEIAMMTRF DPDTRIFSIH STATIEAESW
TRHAEGRMSQ IEPAETVKFD LAALSKRCDR RMSPAAHYEA MTARGLQYGP AFQSVTGIAT
SGEREVLAQI TAQGVDVSEA ILYPTLLDGC FQALISALPT DGKPATYVPT RIKDFTVHQR
PGASFTCYGK VTAWEGLTMT ADLWLLADDG SVLAELRGIT ARRLGAEDRG LPASIDANAL
MVRFECVEQL LADAAVRSNP APLSPIAILS GGSALGASLS EALEAKGLDV HLIAHDAFAA
DGFRQIVDLR GLEALASDPT GQRRAEASLG LLHAIPQDGV TRCLTVVARH DPEAPQSATL
GNAAQFGLLR VAANEYADLD LRMIQIGGEA LPALLAEIMA QSDEDDIVLT DDTRVVRRLN
RVDSAALGQE ASARRPGGPI PEAQAEIEVL AATSEAPVDV LGLVTSGQLS GKRILARLPS
DTAPQRFVRL PQAGLLELPT LALEDEAQLG LLPLSLAHSI LKLADLQPST KLGLLVTDPR
MAGALASVGE MIGARVAMIT SRHDIPVEGF DMICVDTMSE LTELLLEHLI DFGTAVHIGR
PLGPLQAPTK NRRDLFIAAL DLLNRAPARL CQSLDEIVAA VQARELTAGL KPELRRFAEG
QGEVAKAAAV STSVAAPQIN GTGAYLVTGG FGGFGFEIAK WLARNGAGHV ILAGRKGIDT
EGALDMIAEL RRLGASTMAM TMDVGDEASV ATGMRLIAGQ DQPLRGVFHA AGVLDDAPVY
LLTPEQLDRV MKPKALGAWN LHQATRELPL DCFVVISSIA ALLGSPGQGA YVAANSFLDA
LVQHRRRQGL PGIGINLGAL AEVGMAAKHE GVEKHFARVG VGSLRPEEAI GMLGYILREN
PVNMAAASMD YALWGNTYAK WAGSPRYRHL MPERAEDGGD GAGLSLAALS PDERRQKVTA
TLTELVASIL RLPADGVDTG KSLLAMGVDS LMAMELQLGI DRQLGLKIPT LELMKGIALR
ALCTTIAERL AGDPTDDAPQ PAAAPAPAPR KQDIGELLSR LDTLSAEEIE QAIAEFGTLE
GSN
//
