ID   PMSE_PSEE4              Reviewed;         611 AA.
AC   Q1IAK8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Pseudomonine synthase PmsE {ECO:0000305};
DE            EC=6.2.1.61 {ECO:0000269|PubMed:18710233};
DE   AltName: Full=Nonribosomal peptide synthase PmsE {ECO:0000305};
DE   AltName: Full=Salicylate--[aryl-carrier protein] ligase {ECO:0000305};
GN   Name=pmsE {ECO:0000303|PubMed:18710233};
GN   OrderedLocusNames=PSEEN2505 {ECO:0000312|EMBL:CAK15309.1};
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC   STRAIN=L48;
RX   PubMed=18710233; DOI=10.1021/ja804499r;
RA   Sattely E.S., Walsh C.T.;
RT   "A latent oxazoline electrophile for N-O-C bond formation in pseudomonine
RT   biosynthesis.";
RL   J. Am. Chem. Soc. 130:12282-12284(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of the siderophore pseudomonine.
CC       Specifically adenylates salicylate and loads it onto its peptidyl
CC       carrier domain, via a thioester linkage to the phosphopanthetheine
CC       moiety. {ECO:0000269|PubMed:18710233}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + holo-[non-ribosomal peptide synthase] + salicylate = AMP
CC         + diphosphate + salicyl-[non-ribosomal peptide synthase];
CC         Xref=Rhea:RHEA:61648, Rhea:RHEA-COMP:15309, Rhea:RHEA-COMP:16647,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:30762, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:86464, ChEBI:CHEBI:456215;
CC         EC=6.2.1.61; Evidence={ECO:0000269|PubMed:18710233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61649;
CC         Evidence={ECO:0000269|PubMed:18710233};
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000269|PubMed:18710233};
CC   -!- PATHWAY: Siderophore biosynthesis; pseudomonine biosynthesis.
CC       {ECO:0000269|PubMed:18710233}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CT573326; CAK15309.1; -; Genomic_DNA.
DR   RefSeq; WP_011533708.1; NC_008027.1.
DR   STRING; 384676.PSEEN2505; -.
DR   EnsemblBacteria; CAK15309; CAK15309; PSEEN2505.
DR   KEGG; pen:PSEEN2505; -.
DR   eggNOG; COG1021; Bacteria.
DR   HOGENOM; CLU_000022_59_7_6; -.
DR   OMA; PNIRFIR; -.
DR   OrthoDB; 1015470at2; -.
DR   BioCyc; MetaCyc:MON-20463; -.
DR   BRENDA; 6.2.1.61; 12484.
DR   UniPathway; UPA00024; -.
DR   Proteomes; UP000000658; Chromosome.
DR   GO; GO:0008668; F:(2,3-dihydroxybenzoyl)adenylate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR011963; DHB_AMP_lig.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR02275; DHB_AMP_lig; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   1: Evidence at protein level;
KW   Ligase; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..611
FT                   /note="Pseudomonine synthase PmsE"
FT                   /id="PRO_0000454822"
FT   DOMAIN          533..608
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         569
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   611 AA;  66623 MW;  4FBDF0B209A4462D CRC64;
     MTIEFTDWPQ DRAQRYRDAG YWIDQPLTEI LHSRCQAQPQ ALAIICGERR FTYGELDTLS
     SILASRLAEQ GLGQGDTALV QLPNVAEFYI VLFALLKAGI VPLNALFSHR RLELTAYAKQ
     IVPKLLIASR EHEVFRDDAY VQAFAEVGAA PAVTLLLGES DPAASLAHWI ETPGSQPVAY
     APTAADQVAL FQLSGGSTGI PKLIPRTHND YHYNARACAD VCALNAHTRF LCAVPAAHNF
     LLSSPGALGV FHAGGCVVMA ASPEPLSCFA LVEQHEVNTV ALVPSAVALW LQAAPAHRDK
     LQSLAYLQVG GAVFADSLAR QVPGVLGCQL QQVFGMAEGL INYTRLDDSD EQIFTTQGRP
     VSPDDEIKIV DEQGVPVAPG EPGMLATRGP YTFCGYYKAP EQNASAFDAE GFYYSGDLVV
     LTPSGDLRVV GRIKDQINRG GEKVASEEIE NLLVLHPEVT HAGLVAMPDE ALGEKSCAFV
     VSRNPSLKAP ALRRHLMELG IAEYKLPDRI RLIEAMPLTA VGKIDKKQLR HLVSVENTRT
     WLQTRLRQLI EDSEELDPEE NLIFYGLDSL QVMKLAAELK ARGIEVSFEE LASTPTLASW
     WALVEARQKA A