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Database: UniProt
Entry: A0A252BJQ5_9PROT
LinkDB: A0A252BJQ5_9PROT
Original site: A0A252BJQ5_9PROT 
ID   A0A252BJQ5_9PROT        Unreviewed;      2117 AA.
AC   A0A252BJQ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OUJ05447.1};
GN   ORFNames=HK24_12145 {ECO:0000313|EMBL:OUJ05447.1};
OS   Gluconobacter sp. DsW_058.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1511210 {ECO:0000313|EMBL:OUJ05447.1, ECO:0000313|Proteomes:UP000194786};
RN   [1] {ECO:0000313|Proteomes:UP000194786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Winans N.J., Newell P.D., Douglas A.E.;
RL   Submitted (JUN-2014) 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:OUJ05447.1}.
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DR   EMBL; JOPH01000068; OUJ05447.1; -; Genomic_DNA.
DR   Proteomes; UP000194786; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05195; enoyl_red; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
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; IPR013149; ADH-like_C.
DR   InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
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; PF00107; ADH_zinc_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; 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; SM00829; PKS_ER; 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; SSF50129; GroES-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; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194786};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..435
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2031..2108
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2117 AA;  227599 MW;  81797C510BA75F43 CRC64;
     MIDYGHEVAV VGIGCRLPGG IETTEALWRF LCEQGDATSD VPADRWGIKR FYDPEYETPN
     KTYMRRGSFI DQKIDEMDPL FFGISPREAT LMDPQQRLLL EVVWEAMENA GILPATLAGT
     RTGVFIGTFS LDWLVACGSP LNRPLITDHF AATAASATML AARISHNLGL QGPCMSIDTA
     CSSSLVAIHQ ARISLLNGES DVVVAGGVNI MVAPPASITM SKGHFLAADG RCKSFSADAD
     GYGRGEGAGI VLLKRLADAK RDGDVIHGVI AGTGVNQDGR TLSLTMPSED AQRALIEEVA
     QKAHIDLATI GYVEAHGTGT PVGDPIEARA LGTAIGHKRA SDSPLIVGSI KANLGHLEAA
     AGVTGLIKAL LCLKHGAIPP QANLTQVNPA IPFADLHLKV AQDTLTPLKA EAGTVYAGVN
     SFGYGGTNAV ALLRAPTVAD QPQKRLEEIV RMPSGRFLLP VNALVDASLK TLARSYASLL
     ASSATPSVAN VCFSAATYRT RLPMQAVVSG RDREELIAGL KALSEGQSSP AVTVGRRRNG
     EMQHPVFVFS GMGSQWKGMG QHILRHAPEP VSSTIQQIDS LFSALAGWSI LDEILKPAEH
     SRIDETVVAQ PAIFMVQVVL AELFRFHGVV PAAIVGHSVG EVAASYIAGA LSLEDAVTVI
     FHRSQQQARL AGRGAMLAIG MSGRQAAEKL LPSYEDRVSV AALNSAKSAT LAGEEAALKE
     LAVRCDQDGT FNRLLRVEVP YHSILMEEIR DDLLNPLAAL APKNPNIPLY STVTGTRWAD
     DALHDAEYWY GNARQPVLFH DAIQNLMGDG HRVFLEIGAH PVLGGLIRET AQQIDGDVAV
     IASLSRKDAE DTAIARSIAK LYMAAVPLDW SLLTGGHRTD LPHYAWSRSR FWSETEVSRK
     DRLDGTVHPV LGIPVSASRP GWLADINRNY MPWLPDHKVD GICLFPAAGY IEGGLALHRQ
     IERSDTAILE DLEIGQALLL DSLTPPVVEW AFDEETRVLT VSSSHGDDGE EEWIQHAKLR
     VLTSVPWAAD PVVPERLQAD LKHEILPETF YARLAEHGFS YGSTFQTIKE LKAGEGIAFA
     RLELADAESI AEYFLHPALL DGAFQALIGA GYSAAEERVF VPTGARQVVY RGGHHKVLLA
     HAALTRRSET GIEGDIRLFT EAGEPVAEIL GFKARAIRKL IAAGMGAENV RRFYRPAWVQ
     TELLPHFAEP LTALVLGRDG PLLEQFSQVS AGQGIMVDTL KIDDVDQAVL AEALAQTNDA
     ILYLCSPTED ATGKQGIAEI LRLVRAIRVS EDGEAAPKCL IVTRGAVSAE ALQSDDLDTG
     QAAIRGFARG VASERPDLAL RIVDIGRVVD EATLQQLCAE IVQQDTEDDI VLRPGLRAVG
     RLTPSETKPE PVPTLYHPNE TADGRLVGVR LVSASNGSLD RLHHERFVAD PLQPGQVLFR
     TLAAALNFKD ILKATGLIPQ SVVDDTFHGE TLGMEASAEV IALGEGVTDF APGERYLVSW
     PGCFASHFTA DAESIFALPI EGLGSPLEAA TLPVAFITAY YGLCRLAHLE KGETVLIHSG
     TGGVGLAAIQ LAKRVGARIF ATAGSPEKRQ YLKELGCEGV WDSRSLEFAE GIRDVTQGRG
     VDVVLNSLPG EGQTHSLSIV APYGRFVEIG KKDIIEKRGL PLAPFNENLS FFSLDLDRMM
     LERPALMRSL LSDVAALSKS GDVQPLPLES FPARDAAGAF RLLASAKHMG KVVIDYSDLD
     DLKASPLPRP QPQVSDGKTY LVTGGLSGFG WATAEWLIEQ GARNLVLLGR RTPEETGVSE
     QLAIQRAAGV HIHTILVDVS HEEAMQDVFE EIAFTSNLPP IRGIFHCAGI LDDALVQNLD
     EERIGRVLEA KAQGAIILDR LVQGMDLDYF VLFSSVTTVL GNVGQSAYIA ANAVLGAVAA
     NRWKDGEAAL AVDWGAIADV GMLSRNETAA RALEAAGLKG MPAHDALDHL PEMLALELPE
     VACVEIDWKK WAQIVPGANV LARFSLVRLA DASNGATSER LATLSALPED ERLPYVVEQV
     KVLIAQTLHL EPTSIDDRAR LSELGIDSLA GVELQTALRV EFGVEVSILV LARDESIRKM
     SQFLLNRVKI GQTAQLP
//
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