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 27-NOV-2024, entry version 100.
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; Pseudomonadota; 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=salicylate + holo-[ACP] + ATP = salicyl-[ACP] + AMP +
CC diphosphate; Xref=Rhea:RHEA:61648, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:19022, 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 AlphaFoldDB; Q1IAK8; -.
DR SMR; Q1IAK8; -.
DR STRING; 384676.PSEEN2505; -.
DR GeneID; 32805679; -.
DR KEGG; pen:PSEEN2505; -.
DR eggNOG; COG1021; Bacteria.
DR HOGENOM; CLU_000022_59_7_6; -.
DR OrthoDB; 9803968at2; -.
DR BioCyc; MetaCyc:MONOMER-20463; -.
DR BRENDA; 6.2.1.61; 12484.
DR UniPathway; UPA00024; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0008668; F:2,3-dihydroxybenzoate--[aryl-carrier protein] ligase; IEA:InterPro.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR CDD; cd05920; 23DHB-AMP_lg; 1.
DR FunFam; 2.30.38.10:FF:000003; Vibriobactin-specific 2,3-dihydroxybenzoate-AMP ligase; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR050237; ATP-dep_AMP-bd_enzyme.
DR InterPro; IPR011963; DHB_AMP_lig.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR02275; DHB_AMP_lig; 1.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF10; SURFACTIN SYNTHASE SUBUNIT 1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 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
//
