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
//