UniProt: A0A0E3WJ57

Database: UniProt
Entry: A0A0E3WJ57_9BACL

LinkDB:  A0A0E3WJ57_9BACL 
Original site:  A0A0E3WJ57_9BACL

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (33)   
   InterPro (18)   
   Pfam (7)   
   PROSITE (5)   
   SMART (3)   
All databases (40)   

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ID   A0A0E3WJ57_9BACL        Unreviewed;      2232 AA.
AC   A0A0E3WJ57;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Hybrid nonribosomal peptide synthetase/polyketide synthase {ECO:0000313|EMBL:CQR58208.1};
GN   ORFNames=PRIO_5821 {ECO:0000313|EMBL:CQR58208.1};
OS   Paenibacillus riograndensis SBR5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC   Paenibacillus sonchi group.
OX   NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR58208.1, ECO:0000313|Proteomes:UP000033163};
RN   [1] {ECO:0000313|Proteomes:UP000033163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; LN831776; CQR58208.1; -; Genomic_DNA.
DR   RefSeq; WP_020429585.1; NZ_LN831776.1.
DR   KEGG; pri:PRIO_5821; -.
DR   PATRIC; fig|1073571.4.peg.6251; -.
DR   HOGENOM; CLU_000022_70_2_9; -.
DR   Proteomes; UP000033163; Chromosome I.
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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd19534; E_NRPS; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 1.10.1240.100; -; 1.
DR   Gene3D; 3.30.300.30; -; 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR010060; NRPS_synth.
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; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01720; NRPS-para261; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 2.
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; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   SUPFAM; SSF53901; Thiolase-like; 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; 2.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          40..460
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          663..738
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1713..1787
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2232 AA;  250510 MW;  93D7A0E6DA8155C5 CRC64;
     MDDTSIIKKY ILEQIKAQSM DSEMALRMLK ELTHKEKKDS NEIAIIGISC KFSNAGNTRE
     YWSNIVNSVG CIRDLPQVRK TDLDPLMNYA EMDAYFQAGF IEEIDKFDAA FFRISPREAM
     LMDPKQRLFL ETVYHAIEDS GYAGRKIYGS DTGMYVGHDH SGDLKISYAS LIKDSDMIAM
     TGTYPGILAS RTSYIFNLKG PCLVVDTACS SGLVSVHLAC NALKNEECSM AIAGGVNLFL
     LPQQTGMMSE IEAGNGQISI FDKNAKGTMW GEGISALVLK PLNRAIEDGD HIYAVIKGSA
     INNDGASNGI TAPSAEAQGE LIVRAWENAK IDPETIAYIE THGTGTILGD PIEIKGIANA
     FKKYTARKQF CGIGSVKPNI GHTVAASGIA SLIKTVMAIK EGIIPPSINF REPNPLINFS
     NSPVYVSDRA RAWESGAEPK RAGVSSFGFS GTNCHIVLEE APARAVNAES PHPVEILTLS
     AKNKKSLQEL IANYVQFLNE DGEFDLPGLC YTANTGRKHC EYRVCLKIKD KAELIREMNK
     LNDNPIHLPN LKKLSHAEDR ELKNSARQKV EAYNKSGRTE TDILNEICSL YEKGGEVDWE
     SLYEGEKRGK ISIPVYPFLK ERHWVNAPRR KTAEPDEEEQ EGLWQNSLEA AAAGIQLEGR
     DSGRYSKAEI SVGQVWGAVL GMNPMSVTAD FYEIGGDSII AIEIVNTLNT IMGLSLQVPV
     LFEHSNIERL AAYIEGQAGT DKDTRGNSAI PRIAAAEHYE VSSSQKRIYI LNQLNARSTS
     YNIPLFVMME GPLDEGRLEH SFEALIQRHE VLRTSFSFVN KELVQAVDDH VHLAVEKYHA
     DDETDLDQIT SQFIRPFDLS KAPLIRAGLV EIRKNKHLLM LDVQHIIADG SSIPLLQKEI
     IHLYEHNPLP ELNIQFKDFA KWQNDLFKTD YMNKQKKYWL DVFSGELPIL NLPVDYPRDS
     GQGDQGERLT CNAGRELTQR LNEYSSKEKT TLFMTLLAAF NVLLFKHTGQ EDIIVGSPIA
     GRKHKELEQM IGMFVNTLAL RNRPSAHMVF KEFLAGVKEN ALQAYEHQDY PFEELVDHLN
     MDRNLSGTAL FNVMFVLQVM DNPAFEVNGM HYAPYPYHNK TAKFDLALQV FPGLDELKFE
     FTYAAKLFKR STIESFARRF LRVLEQVVAL EHVLIGDIDV LDREELRDIR RYGQAGLPAA
     YNTKTIVEMF EAQAARIPDH LAVSGFDRSL TYRELNEQAN QLARVLIRNG ACKDRVVGII
     AERSTNFAVG IMGVLKSGAA YLPIEPAYPP ERKRFMLEDS GACMVLTDTA HRRSLQHGIR
     EICLEEVAGN SGEQGNLEAT ASADSLAYVI YTSGSTGKPK GVMIEHRSVT NLAEALDEKI
     YSLHGPNLNV ALLAPFVFDA SVKQIFSAFL LGHHLNIVPG DVRQDVIQLA EYYKQNKIDI
     SDGTPAYLRL LAETSLCARI GVAHFIIGGE ALSIAEVKRF YTSFANHKPP YITNVYGPTE
     CCVDATAFTI KPEETGQIQE MPIGAPIKNC SVYILDEQKR MVPRGVLGEL YIGGHGVARG
     YCNNKALTSS RFVEDIYHPG MYMYKTGDMG KWTEDGLIHF AGRADHQVKI RGFRIELDEI
     RHRLLSCDGV QAAVVLVQKD QRQEPYLCAY VVCRDEQVLP GLRGYLGEYL PDYMIPRVIM
     PVDQIPMTAN GKADTSQLPD PQEMRDHSLG YGAPRNRTEE ILCTVWSEVL ELRRIGIHDN
     FFAAGGDSIK AIQAAARMEK YNLRLEVKHL FQYQTIGEVS KKVQDRAGHA GYGAVTGEAG
     LVPIQSWMVE HCRDTLQHRN LSFVLYREAG FGEDNIRKVF TEIIRHHDAL RMVFREQNRQ
     MLQHNRGLDG ELFDFYLIDL ADSPSFSEEA QAAVNQVQAS MDLEKGPLVK LALIRAGYGE
     HLLIVIHQMI IDHLSWRIIL EDFNTAYTQL LNHEDIGLPP KTAPFLQWSN HLHEYADSIE
     LLREQPYWDQ VESIKAEPLP TDYKADEARV RDNLTLYQAF DCTETEQVMS SIRSNPHFTT
     ESIMLTALAL TIRAWTGNAA VVVNLGNHGR DMDSKDIDTY RTVGRFSILY PVALQLPESR
     NIDLCLEYVK EYLSGIPKQG GGYGVLKYLS SHQEGIRFRL NPELSFNYMG QFDAEFNTST
     FRISPLSGGE DRSGEEIWSY KLKFISFIRM NQLNIGIEYN QQQYARETVN ALLQQYMEYL
     KKAAEISEAI QV
//

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