ID   PCHD_PSEAB              Reviewed;         547 AA.
AC   A0A0H2ZF83;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Pyochelin synthase PchD {ECO:0000305};
DE            EC=6.2.1.61 {ECO:0000269|PubMed:10555976};
DE   AltName: Full=Nonribosomal peptide synthase PchD {ECO:0000305};
DE   AltName: Full=Salicylate--[aryl-carrier protein] ligase {ECO:0000305};
GN   Name=pchD {ECO:0000303|PubMed:10555976};
GN   OrderedLocusNames=PA14_09240 {ECO:0000312|EMBL:ABJ13501.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=10555976; DOI=10.1021/bi991787c;
RA   Quadri L.E., Keating T.A., Patel H.M., Walsh C.T.;
RT   "Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore
RT   pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase
RT   activity from PchD, PchE, and PchF.";
RL   Biochemistry 38:14941-14954(1999).
CC   -!- FUNCTION: Involved in the biosynthesis of the siderophore pyochelin
CC       (PubMed:10555976). Specifically adenylates salicylate and loads it onto
CC       the holo form of PchE via a thioester linkage to the
CC       phosphopanthetheine moiety (PubMed:10555976). Is also involved in the
CC       synthesis of the antifungal antibiotic dihydroaeruginoic acid (Dha or
CC       hydroxyphenyl-thiazolinyl-carboxylate), a precursor of pyochelin (By
CC       similarity). {ECO:0000250|UniProtKB:Q9HWG3,
CC       ECO:0000269|PubMed:10555976}.
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:10555976};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61649;
CC         Evidence={ECO:0000269|PubMed:10555976};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.8 uM for salicylate {ECO:0000269|PubMed:10555976};
CC         Note=kcat is 74 min(-1) with salicylate as substrate.
CC         {ECO:0000269|PubMed:10555976};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:10555976}.
CC   -!- PATHWAY: Antifungal biosynthesis. {ECO:0000250|UniProtKB:Q9HWG3}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CP000438; ABJ13501.1; -; Genomic_DNA.
DR   RefSeq; WP_003137468.1; NZ_CP034244.1.
DR   EnsemblBacteria; ABJ13501; ABJ13501; PA14_09240.
DR   KEGG; pau:PA14_09240; -.
DR   HOGENOM; CLU_000022_59_7_6; -.
DR   OMA; PMSPHDE; -.
DR   BioCyc; PAER208963:G1G74-771-MON; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
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   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Ligase.
FT   CHAIN           1..547
FT                   /note="Pyochelin synthase PchD"
FT                   /id="PRO_0000454823"
SQ   SEQUENCE   547 AA;  59840 MW;  F81DD8CD61088902 CRC64;
     MTSSPATPSA VDDAPDWPAA FVRRYLDAGH WQDQNFAEAL AASAARHPRR IALCDDDQRL
     SYADLLQRCR RLAAGLRQAG LAHGDTVVLH LPNGIAFVET CFALFQLGVR PVLALPAHRQ
     HEISGFCRFA EAKAYIGAER IDGFDPRPMA RELLASGACR MALIHGEAEA PLQALAPLYQ
     ADALEDCAAR AEDIACFQLS GGTTGTPKLI PRRHREYLYN VRASAEVCGF DEHTVYLTGL
     PMAHNFTLCC PGVIGTLLAG GRVVVSQRAD PEHCFALIAR ERVTHTALVP PLAMLWLDAQ
     ESRRADLSSL RLLQVGGSRL GSSAAQRVEP VLGCQLQQVL GMAEGLICYT RLDDPPERVL
     HTQGRPLSPD DEVRVVDAEG REVGPGEVGE LTVRGPYTIR GYYRLPEHNA KAFSADGFYR
     TGDRVSRDKD GYLVVEGRDK DQINRGGEKI AAEEVENLLI AHPQVHDATV VAMPDSLLGE
     RTCAFVIPRQ PAPSALKLKQ YLHACGLAAF KVPDRIELVP AFPQTGIGKI SKKDLRERLR
     RELEARA