ID B0RXN3_XANCB Unreviewed; 1326 AA.
AC B0RXN3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:CAP53419.1};
DE EC=2.7.7.- {ECO:0000313|EMBL:CAP53419.1};
GN ORFNames=XCCB100_4052 {ECO:0000313|EMBL:CAP53419.1};
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP53419.1, ECO:0000313|Proteomes:UP000001188};
RN [1] {ECO:0000313|EMBL:CAP53419.1, ECO:0000313|Proteomes:UP000001188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100 {ECO:0000313|EMBL:CAP53419.1,
RC ECO:0000313|Proteomes:UP000001188};
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O.,
RA Linke B., Patschkowski T., Ruckert C., Schmid J., Sidhu V.K., Sieber V.,
RA Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puhler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP53419.1; -; Genomic_DNA.
DR ESTHER; xanax-ENTF2; Thioesterase.
DR KEGG; xca:xcc-b100_4052; -.
DR HOGENOM; CLU_000022_2_13_6; -.
DR Proteomes; UP000001188; Chromosome.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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; cd12116; A_NRPS_Ta1_like; 1.
DR CDD; cd19533; starter-C_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; 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; 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; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 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; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Nucleotidyltransferase {ECO:0000313|EMBL:CAP53419.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:CAP53419.1}.
FT DOMAIN 954..1029
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1326 AA; 145255 MW; 87AAF22A5FFDF7B4 CRC64;
MHADSSPVYP LTRAQRGLWV ASKLHTDNTL MLSEALELFG PLDPEVLLRA SLQLTREFDT
LRLCIVEHDG VPSQVVMPEY TAPIHYFNFS DDPAPRNAAE HWVEEEIRKP EDLQNGPLWR
CAVFRLGEDH HMWVQCVSHL VMDGYCASIM MQRMAVLYTA YATGCEPAPA EYGSALSLIE
LEQQYRDSDR FQRDRNYWME QLADLPPPTT LARPGNQLST GLLRGTGEFS PQQVVQLRAL
GKHYGASLPQ MLIALIATYY YRCTGAEDLV LAMPVTGRIN ARYRQAAGLV ANVISLRLKM
DPQQPVHALF AQVASVVRSA LRHQQYRFED VRRDLGLFGI EQKFARLAVN IEAFDYVLRF
GEAYAVPHNL CNGPADDLTI FCYERGDGAA LRFDLDANPA LYDSEELAEH CRRLTHLADA
VLADPECALG QVDVLGDAER QRLLHTWNAT AAPLPEPSTL LHGMLQRAEL MPAAVVVQYD
NRTLDYATLC ELAARIAAQW VDDGVRPGDV VAIALPRSEQ LLVALLAVMW SGAAYLPLDP
ESPAARNRQM LNDSGAIALV CEPALCERYL LGGMVWLDPC PAVLPAAIAP LAQPDGTAYV
LYTSGSTGVP KGVEVSHRNL ANFLHAMEQE LALRPRDRVL AVTTFTFDIA GLELYLPLLT
GARVVIAPAG ITHDPRSLSR LIANEQISVV QATPSLWRIL LANQELALDR VHALVGGEAL
VPELAAQLLS RVGRLTQLYG PTETTIWSTI MPLQLSDAAA PPIGRPLLNT RVYVLDAQRQ
PLPTGAVGEL YIGGAGVAKG YRGKRQLTSE RFVHDPFADD GSTMYRTGDR VRQRRDGLLE
FIGRADGQLK IRGHRVEPAE IENALLLHTQ VAQAVVVGHH DGANALQLLA YVVGKHGTAP
STELLRAHLQ QRLPASMIPT LWMPLQALPL TANGKLDRRA LPAPGAVPQR AHLAPRDALE
QQLAAMLQDV LGIAVVGVDD NFFELGGDSL RAAEMAARFP QLFGVELPLG TLFHAPTIAG
LAEVIRRSTH TPNDPLGVLL PQRAGTAGVT PLFCIHPVVG LGWSYLTLLG QLDPQWPVYA
LQSPGLSDPL HRPDSIEVIA RDYLARLRAV QPHGPYRLMG WSLGGLIAHA ITAELHALGE
EVEVLAMLDS YPHRQQAAAL PESEGVRASV HALNLNLAHG QPMPTTVAEL ASLLCDHYGL
MSVPAVRQLL DQRPTLLDDL GAVTQHHLHL ARRYQPRALA QDVLFVEASV RMTSGGDDAL
WVDYRPQAWR PYVRTLQLHT LESDHHSMLS PAHSATLSTL LHAATAKTAR TDGCITTASD
GVAEYA
//
