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Database: UniProt
Entry: D3UYT2_XENBS
LinkDB: D3UYT2_XENBS
Original site: D3UYT2_XENBS 
ID   D3UYT2_XENBS            Unreviewed;      2384 AA.
AC   D3UYT2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Putative non-ribosomal peptide synthetase {ECO:0000313|EMBL:CBJ79460.1};
DE            EC=5.1.1.11 {ECO:0000313|EMBL:CBJ79460.1};
DE            EC=6.2.1.1 {ECO:0000313|EMBL:CBJ79460.1};
GN   OrderedLocusNames=XBJ1_0310 {ECO:0000313|EMBL:CBJ79460.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79460.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79460.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79460.1};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA   Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA   Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA   Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA   Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA   Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA   Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA   van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA   Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA   Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT   convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:E27909-E27909(2011).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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DR   EMBL; FN667741; CBJ79460.1; -; Genomic_DNA.
DR   RefSeq; WP_012986920.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0310; -.
DR   KEGG; xbo:XBJ1_0310; -.
DR   PATRIC; fig|406818.4.peg.282; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_000022_0_1_6; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047462; F:phenylalanine racemase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 2.
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; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 2.
DR   Pfam; PF00668; Condensation; 3.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:CBJ79460.1};
KW   Ligase {ECO:0000313|EMBL:CBJ79460.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          955..1029
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2016..2091
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2384 AA;  264669 MW;  44F9D897233F31D7 CRC64;
     MSIATDIGEP TSYERDLWVE ELHDPHCHQF TVALSELLPR SIDLVNLKGV AEQVLESEQA
     SHKSFHEQEG HLVLKKAPVV VCAELYEFKN EDDFALFFNE WSRKIWDLSV SPLVEIAIGQ
     TDQATILMVR AHHIVADGWG LNLLSKKILG AYADNHLGLN EQLKGVKRYA TKYPTLQGSK
     LDEAIHDVVV KIADTDPVLF PKSGAALSTS PSYIRPFKIS AHEVAHGIEN GFTPFLAVST
     ALAVLLSNAY GSEKFFIGVP FLNRTDAEIT SVSHRANILP VKVEVLPQNT LRAIYSQIKD
     FIVFLKDKES VPLGGIISAL ASSSRQLFDV TMSYLRYPEW GAIAGFEEKT QNIAHMHTQD
     AIAIHLYTYG NNADVWGDVC LNSSVFDTED SANAFLDTFI HLINNFGNNV DKHVSEVNLL
     TSKQMEQLRQ YENGPTKQYS VNETVVSLFE AKAEQFPENI ALRDQIGTSL SYSQLNAWSS
     TIAAALEGRG IGQGDIVAVS VERSPEMLAA IFGVLKTGAA YLPIDSDYPE DRIQYMLNDS
     NAKLVISNLP HVMKSDDPRL FRLDALPTEL PSHHQYRSKA QPHEPAYVIY TSGSTGRPKG
     VIVEHHSVVN RLEWMQEIHP LTSDDVILQK TSISFDVSVW ELFWWAMTGA SVALLKQGAQ
     RDPRELIQTI STLGVTVAHF VPSMFEPYVQ TLTDDRQSLL SVSSLKCLFT SGEALTPAVV
     NKYRKLFGRD TRPPRLINLY GPTEATVDVT YYELNLEQDS DINAVPIGFP INNTSVRIAS
     LHGVRQPIGI SGELQIGGVQ LARGYLNRPE LTAERFIIDQ NDSCSRWYRT GDLAAWAEDG
     SILYLGRMDG QVKIRGNRIE LGEIKNALLN LPEVLNAEVI VEDDARGKHL IAVYVGRQDL
     NERDIRAKLG KQLPSFMVPA RFVRLGGIPL TPNGKFDRAS ALREVSGNKA SPQTVKLDES
     ETIVAKIWEK VLGRSNIGAD DDFYTLGGDS ILMLKVRSEL ESHGYDVGLS DLAQYTTVCS
     LGNVLESVSR VLSSPKEALP PFALISATDQ KMLSSVYDDA YPVSQLQLGL LFHSREMEGA
     RTYKDVFRYT LKSAWNEAAF RSALQGLVRR HPALRTVFNL SDYHLPLQLI RPEILIDDVL
     SIKTPDVVEY EHTVLAHMDK WSRYNYSFLS GPLFHVAIFA NSESNYIDLV FSFHHAILDG
     GSVANLIREL LLSYSQGNDG ANLGYPEDEL PNPSIFVQNE IETLEASESK NYWKEYLSGA
     TNTLPIGLAG YSTAPVKRIF SYRFLIDPVL DVALNQLART IRVPIKHLYL AAHCTTIALM
     SGKEEIVTGV VTHTRPEIKH SERILGLFLN TLPLRVDIKN WNWLQVVEGL YRNEKRSHKH
     RCFPLSQIQA DNELLSVQTA FNYVHFHILQ DISAKSGIEI VAFDPKEETN FDILVNVMRD
     VDGERTSVRV DLNGSIYARE QGAVFSRLFN RVLERIAYQP ELPVSLSHSI TEVGCLVERT
     SDKVFISLPA MIRNSVQRDP DAVAITYDNV EWSYQQLWDA ATEIAFLLSE RGVHKQDVVG
     IALPRSFEQI ATVLAILRIG AICLPIDLSY PASRIELILK IANPAVVVTD HSITELPTSV
     RMLFLEHDSI AATAERDDAT IDSADAAYIL FTSGSTGTPK GVTMLHRGLT NLVGWQNKIS
     SGAKVTSTLQ FSPLSFDVSF QEILSTLSSG ATLHLISEME RRDPVALVRH LDRKGVERIF
     LPYIALQQLA ETAVMLEFFP KKLRVIVSSG EQLRVTKEIR TLVDNLPGGI LENQYGPTET
     HVVTSYTMSS DPSQFPALPP IGIPITGVGI VILDESSNVV PDGVPGEICV FGDALASGYY
     RSPEETKKKF IAHADVPGGM FYRTGDIGIR SACGEIISLG RKDTLVKVRG YRVELSEIEL
     KILEFFEKIK KNVEVAVVAR PRDDLDSYLI AYLVGKEDGI ALEELRQFIG AELPAYMVPT
     HITWINELPK TPSGKRDDAM LRKLDIQLVS EKNYRGPAGE YESRLCELTA ELLKIPEIAP
     EQSIFDCGAT SLTAMRIVVL VEKLYGINVP LSAFVSAPTI AKLAMLIQNG GGQFKFDPLV
     PLRKAGNSRP LFLVHPMGGN ILSYLRMLPY LPSDQPLYAL QASGVDAGSS PITTIEEQAA
     FYIEAIKRIQ PTGPYVIGGW SYGGFIAFEM ANQLIRSGEM VSNILILDTM ALSSQAKGQA
     SDDALLSWFF WELLWTSKGS SLPVHVVPSY IESLQEKFEY ITDHATQIGA IPEGSTKAVM
     QRLFEVYSAN WQAAAEYNAQ CPNLDVTLIR AKQPLPQILQ EMHNTIRSEY HDPLNGWGGK
     TSGRVNLIEV DGDHLTIMEE PFVGPMVSAI ITEINKVKGV NANV
//
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