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Database: UniProt
Entry: A0A0Q9F105_9GAMM
LinkDB: A0A0Q9F105_9GAMM
Original site: A0A0Q9F105_9GAMM 
ID   A0A0Q9F105_9GAMM        Unreviewed;      2787 AA.
AC   A0A0Q9F105;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Non-ribosomal peptide synthetase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASE45_10945 {ECO:0000313|EMBL:KRD69624.1};
OS   Lysobacter sp. Root96.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD69624.1, ECO:0000313|Proteomes:UP000050805};
RN   [1] {ECO:0000313|EMBL:KRD69624.1, ECO:0000313|Proteomes:UP000050805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root96 {ECO:0000313|EMBL:KRD69624.1,
RC   ECO:0000313|Proteomes:UP000050805};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD69624.1, ECO:0000313|Proteomes:UP000050805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root96 {ECO:0000313|EMBL:KRD69624.1,
RC   ECO:0000313|Proteomes:UP000050805};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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:KRD69624.1}.
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DR   EMBL; LMJN01000002; KRD69624.1; -; Genomic_DNA.
DR   RefSeq; WP_056305609.1; NZ_LMJN01000002.1.
DR   STRING; 1736612.ASE45_10945; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000050805; Unassembled WGS sequence.
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:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd17643; A_NRPS_Cytc1-like; 1.
DR   CDD; cd12116; A_NRPS_Ta1_like; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 2.
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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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; 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; IPR042099; ANL_N_sf.
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; 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; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 2.
DR   Pfam; PF00668; Condensation; 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; 3.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 3.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050805};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          534..611
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          633..1059
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1544..1622
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2685..2762
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1624..1649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2787 AA;  299108 MW;  8D5BEDF865B13648 CRC64;
     MNKLSDGSSQ YRPLACIPQL VEQQASTRPD AIAVTCEGAS LTYRELNSRA NQLAHRLRAL
     GVGPETLVAI GLERSLEMVV GLLGILKSGG AYLPVDASYP RDRVQFMFED ARPAVLLTST
     GQRGALPATD VAILLLDGDW AEFAAEPVHD PEPLAQLDNI AYVIYTSGST GKPKGCQVTH
     ANVARLFVAT QPWFEFGPDD VWTFFHSHAF DFSVWEIWGA LIYGGRVVVV PFLVSRSPDA
     FHALLVRERV TVLNQTPSAF RGLIHADLAS ASEPSALALR YVVFGGEALE LQMLRPWFER
     HGDRYPRLIN MYGITETTVH VTYRPVARTD LERNAGSVIG EPIPDLRLYV LDPELVPVAA
     GEVGEIHVAG AGVSRGYLNR PDLTAERFFD WQSPQGERVR LYKTGDLARS LADGDLEYLG
     RSDHQVKIRG FRIETGEIES VLARHESVRA CAVIALDDRA GGEARLVAYV VPADVHASQA
     SLRAHLATVL PDYMVPGAFV ELQALPLTEN GKLDRRALPA PARQRPELAH AFEPAIGALE
     ASLCAAFGET LAVDNVGRHD NFFELGGDSL SAARLLQRLK QTGAHASAIP TAQLFRHPTP
     ATLAGSLEGR GAAEIDPARY ASARRRESGG IAVEPIAIVA MAGRFPGAAD VEAFWRNLCE
     GRDSITVFDP QDLDPAVSAQ DRDDPAYVPA RGVIDGVEQF DAAFFGIGPR EAELMDPQQR
     IFLELAWECL ERAGHVPDAT SAPVGVFGGM FNASYFQRHV SAHPDLVDKV GAFQVMLNNE
     KDFIATRVAH KLNLTGPAVS VHTACSTSLV AICQAVDSLT LGHCDMALAG GITVTCPPRS
     GYFYQEGSML SPDGHTRPFD ASAQGTVFSD GAAIVLLKRL SDAVADGNQV FAVIRGGAVN
     NDGGGKASFT APSSEGQAAV ISMAHDRAQV DPRSIGYVET HGTATPVGDP IEIEGLTRAF
     RRGTEERGFC RIGSVKSNIG HLVIAAGATG VIKTALALAE QRIPATAHFK SPNPAIDFSG
     SPFVVNDALT DWPVTDVPRR AGVSSFGVGG TNAHVVLEEA PKLPASDAAQ GPQLLMLSAR
     TPTALSRAAT QLADRLDADP DINLADVAWT LAVGRKAFAH RIAVVADDVA GAAAQLRSPE
     VAAAAARGKP VRQGDVVFLF PGQGATYPGM GRGLYDTEPA FRAAFDACAD ALLAELGFDL
     RERVFSSDPE ALLPTAIMQP ATFAIEYSVA QLWISRGIVP AAMIGHSIGE FVAATLAGVF
     ALPDALKLVA RRGALMQAQP AGGMLSVRLA WDELLARLPA DLSPAAENAP GSVVVSGTLE
     AIARFQAELE ADGVACRALR TSHAFHSQMM EPVVAPFRAE VAALQLSAPL IPIVSTATGD
     WLEEAAARSP DYWASHLRDP VRFATAVGKV LETPSRVLLE VGPRATLSGL SRQHPALLKQ
     QATAVSSLAD DPATEASSFL SAAGQLWCRG TPIDIAAFDR RHSRKRVLLP TYPFERQRFW
     VEAAASSNVV QLPSASAVHP VAIVPGPASA AEDATVPATS GAPDRHARLV SQLSDIFEDV
     VGLDLSEVDD EANFMELGLD SLMLTQVALR LQKIFSVKLT FRQLMGECSS LQRLATMLDA
     QLPPEPEAMP ASAAESAAPA GASESESGEN LARRLLEQQM QLLQQQLSEL DTSQGATAVA
     MPGDEAAQPM HTGHDPFAGG APALLAPTTE PQREIWLADQ LGPEASLAFN LSVSLQFHGD
     LNLEFMRDAL QELVDRHESL RASIGADGET FCVLERSALL LPIADLSSLN PIDRQMAVDE
     RIRLTVETPF ALDQGPLFRA ELLRLAEDEH LLLLTAHHIV CDGWSWWTIV RELGALYGKR
     FEMTAQPLPD AASFVGYALA EAGRQGDESQ AADEAYWLSR FATGTPVLEL PTDRPRPPNR
     SFASARLDHV LDSGLLEALR RTGAARGVGM FATLLAGFSA LLSRLSSQSD VVVGIPAAGQ
     AVCGADHLVG HCVNLLPLRF ELDSTKSFAH AIDDAQAMLL DALEHQRYTF GTLLRKLRLR
     RDPARIPLVS VLFNLDQAMD QECTAFRGVS MEFDSNPRSF ETFELFVNAV QAHGQLRLEC
     QYNRDLFDAA TIRRWLRAYE ALLRAAIERE TADFASLPLV DAVARTELSS LQPAAVAYDR
     ECRMHEYFEA QCDRTPDRVA LRAGPTSLSY AELEARSNRV AHVLREHGVR RGALVGLALD
     RGPDMLAALL GILKAGAGYV PLDPQFPTER LAYMAADAGL AMLLTTREHA AHFDLRGRPV
     LLFDEHAPQL ATAAATRLGR DEYAAQPEDP AYVIYTSGST GRPKGVIVPH RAVSNFLDSM
     RREPGLAAQD RLMAVTTLSF DIAVLELLLP LAVGAQIVLA DRETAGDGAA LRRLLESSGA
     TVMQGTPSSW RLLIDAGWNG NDGFKALCGG EPMAVDLATS LLSRCGSLWN VYGPTETTVW
     STCARIAADP DGQAPDIHIG RPIGNTSVWI LDAHGELCPF GVPGEICIGG EGVTKGYLER
     PDLTAERFVA DRYTATAAGA PGHDGVALLY RTGDRGSWRA DGNLEHLGRL DHQVKVRGYR
     IELGEIEANL ATREEIARAL VIVREDRAND QRLVAYVVAT PGATIEEAAL RAHLRELLPA
     YMLPQHFVVL DEIPLLPNGK IDRNALLPPV AKEEAVSPPP SATGAAADPR VRYLSEIWSE
     LLGLPAGPDD NFFELGGHSM LAVQMANRVE RDTGRRIKLI RLGAETLAQV AAGLPAATED
     AVPAGGVGGR ISSGLRRLFG LNQGSSP
//
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