UniProt: S5XXF6

Database: UniProt
Entry: S5XXF6_PARAH

LinkDB:  S5XXF6_PARAH 
Original site:  S5XXF6_PARAH

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (38)   
   InterPro (20)   
   Pfam (8)   
   PROSITE (4)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (46)   

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ID   S5XXF6_PARAH            Unreviewed;      3161 AA.
AC   S5XXF6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=6-deoxyerythronolide-B synthase {ECO:0000313|EMBL:AGT08110.1};
DE            EC=2.3.1.94 {ECO:0000313|EMBL:AGT08110.1};
GN   ORFNames=JCM7686_1001 {ECO:0000313|EMBL:AGT08110.1};
OS   Paracoccus aminophilus JCM 7686.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT08110.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT08110.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT08110.1};
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; AGT08110.1; -; Genomic_DNA.
DR   STRING; 1367847.JCM7686_1001; -.
DR   KEGG; pami:JCM7686_1001; -.
DR   PATRIC; fig|1367847.3.peg.965; -.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_35_8_5; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000015480; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0047879; F:erythronolide 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; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 2.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
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; 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; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 2.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 2.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 2.
DR   PROSITE; PS52004; KS3_2; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:AGT08110.1};
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:AGT08110.1}.
FT   DOMAIN          44..459
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1447..1522
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1565..1980
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          3056..3131
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1528..1561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1541..1561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3161 AA;  334785 MW;  00CB6A3EE89B3AE3 CRC64;
     MSLSDDTAAP AAPAEERGAA QLRRAMGALR KLQTELSQLK QAQNEPIAIV GFAARMPQVG
     ASTDAFWEQL LAGADLTAPP SARRKAPCAT GLPQKAGFLP EIDCFDASRF EISPKEAGRL
     DPQHRILLEL ADAALDAAGL GSRAGHAAGP RKIGVYVGMS SGDYRELLDP QSAQLDAFCA
     TGTTPCFSAG RISYALNLTG PAMVVDTACS SALVALHLAC AALRRGECDA ALGGGVNIIT
     SAFAQALLEE TRSLSPSGIC RPFDARADGF VRGEGGALFV LKRLSDALAS GDEIRAVIRG
     SAINQDGKSN GLTAPNPEAQ TAVIREALRN ADLSAEAISY VEAHGTGTAL GDPIEMEALT
     EVFARAGEPC RVSSVKSNIG HLEAAAGAAS VLKLALCMAR HQLPAQSGFA TLNPHIAQSE
     GAPEILAEAR DWGKAGETVY AGVSSFGMSG TNAHVILSSA DDYAPARAPT TSELGEALIV
     PLSAADPERL LRRAAELGAR MQSAPDPVGA AAACCLAAGG QLERMAVVAR DPRELSQRLL
     DPPLSNPNVL RGRRDPNTRG KVAFLFSGQG SQYAHMGAAL YRSSASYRQA FDACDALFSP
     LLGESLRARV FSDDGGLERT EWTQPALFAV EYALAAFWRA LGVEPDFVAG HSIGEYVAAT
     VSGILSLEDA IAMVAARAQA MGALPKGGAM LAAWCDGQTT AQIATEICAE SGGPLALAAT
     NSDNQAVLSG AEQAIAEAER RLNARGVRTQ RLVVSHAFHS PLVAPAVAGF RAGCETIEFA
     PPKIPIVCNL TGKRAAAQEL ASLDYWSQQI VSTVRFAETV QTLRDNGVTT WLEVGPHPVL
     TPMLGARSNE NAAASLLRGR DDCLTMSKAV AGLWVAGVPI AWDKLFHGSA PHWRVSPEPV
     ARLSHWLPSG LSRTETLSSA DAAAGASVAP PQPNATEAAL EAPVEASIEI GWHSFELPAQ
     IAAMPAILLP LAPEAGEDFI QIAATHTEST VLDPGWTQGA TVAEMRDALL GEWDRQIAKD
     STAVANVFVL PPQRIDTSAE LGRELAVCTA VFQALSKRRD RQPLRLWLVT RGGQLANGME
     AQAVSAAAVH HGSLGGFAQV AALEYPDLVQ GVLDLPLVEE ASPADLARGL QAVEDNQHDW
     LALREGRVYG RIATSAAPRP PAGPVEFAAQ DWVIVTGGLG SIGLATLEWL AARGARQLLV
     ISRSAVDCAD PDRRDKRQRC LARLAAAGVR CEIFVGDAAD PALLGSAVDF AADHGGLGGV
     FCLSGTTSRQ NLDDMSATID PLPLVSKLES ASILSALCPE VRHFVVFSSV SALWGTPGEA
     VYAAANAGLD RLIAARRQCG QSGCALHWGA WAASAMVGDA DQEWLARLGM TALSAQDGLA
     FLSEELDAAP AAGPSTSGHR VLARMDWRRF VATYQARRRY SLFRDLGAML DLSPAQGNQR
     QGPQSARAIA ELVERTVSTI LGYDEGQSLP TNRGFTELGM ESISAVDLAR ALSAQLSVAI
     TPATVFDHPT VERLSEHLAK EMLKDEGPAQ PMAAKAPHSP EPQTARQTID QDVSQSTGRP
     VAPTGEAFAI VGVGCRLPGG VRDLDGLWRL LSSGKDGLSD IPWARWPHAG ADPALYVRRG
     GFLDAVYSFD ASFFGISPRE ADFMDPQQRL LLQCSWEAMQ DGALFQSDGA PKDTGVFVGI
     SNSDYGLMMA RSQIDQYFAS GSALSAVPGR IAHYYGFEGP TLAVDTACSS SLVALHLACQ
     ALTRRECATA LVAGVNLMLS HEVTLATCRN RMMSEKGRCA TFDAAADGYI RSEGCVVLAV
     KRLEDAQLNA DRILGVVRGS AVNQDGASSA LTVPNGDAQR RVIARALENA GLSGGQVHYV
     EAHGTGTPLG DPIEAEAAWD AYRGNSRDPA PLWIGSVKSN LGHLEAAAGL AGVLKGLGIL
     RHGQIPASLH FQDPNPHIPW DRIGLRVPQQ IVPLPAQEAG LVAVSGFGFT GTNAHVLLGR
     APEPDAATLA EPESRADHAA LAQHGLLSAR SPAALTALIE TYLERFAQTD RRDARARLRE
     ALNGRSQQHE FRAVLAFDEA LRPKAQARAE TAARFQTRLR LDLRGRPVLG AGAADLLRAL
     PEIAALTGPM DGDPAEAALL ATLAWMRLLG LEVEVVGAAW LGSASPRAAM VAPLNGPAPV
     ATGTSQKADD RLNWVVTDDR IIAPDGTEIM PSARLADTWD ALLAALFLNG MRLKMAALTG
     GRMVRHAPLA AYPWQLKDYR LPRAAGQPVF TMEAAQGAQS LAIGAHRADH PAYLTDHRLF
     KTVVVPAASH LAQLLVLLRR EEAAATVIAT DLAFPRALVL DDAEDVAVQI AIEGQPDAPR
     TLKVRSAKEA GTDAWTPHLV GRIATAAEGG DALARWADVP AIPAQSHEIS GKDFYAYFAA
     VGYTLGPSFR WIDRIWRREH EAFCRMKQPV LPDRVEDYSL YPGLIDSCFQ LLACWMVTEG
     SAEDDALAIP FHCDRLTLST KPPQGELTCH MRRRRSGDFD SQSEVVDIDL YDETGARYLE
     ARGFRTRRAA REVLQRSLHR GGGISYVEDW QVAPLGESPV EDRGGRYLLL SDGGAQAQSL
     TERLTAAGHE VAVLTLAPED LADLSQIREK LRAALGGRGV DHVVSLWGRA ASPAETTPHD
     TGPHDTTPHD TRLTFATTLV TAVSTALQGV LAHGGDSPGS INLVTEDAVS VTGEGIVLPE
     RATLVGLASA LRRELPGTEV RLIDLEDAAA DDWSATLVAE LARADEPRLC YRAGQRWVAR
     LRPADPSAAE APHLPEDRSF VITGGTGLLG LKIAERWIGH GAKRVALISR GQPSEAVRAR
     MADLAADLAA EVAFYQADVG DLDQLRAVLH RIRADLGPIG GVIHAAGVLT DAAFAQQSPE
     LFATAMSAKA GGLRWLDQET RGDCLSHFIV FSSVASRLGS AGQASYAAAN AFADALIEER
     RLQGLPGLAV NWGPWSGGGM LAEAGAAAQR RLDLLGVHEL DETGLAALDE ALTSPGSHRI
     VIDADWDRYK AALRRPDPLF DALGTARPVA PEPAEAAPRA GLLRRLSEAR TAQRPEILSQ
     GLTEIVARIM NIDDLGSVNW SLGFTDLGLD SLMALDLQSR LKDELALEVS ATVALDYPDI
     ERLSAHLLDQ FDFGPTEELS SEDALLEAAL KQLNQLNGTG V
//

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