PCHD_PSEAE
ID PCHD_PSEAE Reviewed; 547 AA.
AC Q9HWG3; P72175;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Pyochelin synthase PchD {ECO:0000305};
DE EC=6.2.1.61 {ECO:0000250|UniProtKB:A0A0H2ZF83};
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:8982005};
GN OrderedLocusNames=PA4228 {ECO:0000312|EMBL:AAG07616.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8982005; DOI=10.1128/jb.179.1.248-257.1997;
RA Serino L., Reimmann C., Visca P., Beyeler M., Chiesa V.D., Haas D.;
RT "Biosynthesis of pyochelin and dihydroaeruginoic acid requires the iron-
RT regulated pchDCBA operon in Pseudomonas aeruginosa.";
RL J. Bacteriol. 179:248-257(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore pyochelin
CC (PubMed:8982005). Specifically adenylates salicylate and loads it onto
CC the holo form of PchE via a thioester linkage to the
CC phosphopanthetheine moiety (By similarity). Is also involved in the
CC synthesis of the antifungal antibiotic dihydroaeruginoic acid (Dha or
CC hydroxyphenyl-thiazolinyl-carboxylate), a precursor of pyochelin
CC (PubMed:8982005). {ECO:0000250|UniProtKB:A0A0H2ZF83,
CC ECO:0000269|PubMed:8982005}.
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:0000250|UniProtKB:A0A0H2ZF83};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61649;
CC Evidence={ECO:0000250|UniProtKB:A0A0H2ZF83};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:8982005}.
CC -!- PATHWAY: Antifungal biosynthesis. {ECO:0000269|PubMed:8982005}.
CC -!- INDUCTION: Part of the pchDCBA operon. Is probably positively
CC controlled by PchR. Repressed by iron. {ECO:0000269|PubMed:8982005}.
CC -!- DISRUPTION PHENOTYPE: Insertion mutant does not produce Dha and
CC pyochelin. {ECO:0000269|PubMed:8982005}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X82644; CAA57966.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07616.1; -; Genomic_DNA.
DR PIR; G83116; G83116.
DR RefSeq; NP_252918.1; NC_002516.2.
DR RefSeq; WP_003114688.1; NZ_QZGE01000028.1.
DR AlphaFoldDB; Q9HWG3; -.
DR SMR; Q9HWG3; -.
DR STRING; 287.DR97_3683; -.
DR ChEMBL; CHEMBL3308937; -.
DR PaxDb; Q9HWG3; -.
DR PRIDE; Q9HWG3; -.
DR EnsemblBacteria; AAG07616; AAG07616; PA4228.
DR GeneID; 880566; -.
DR KEGG; pae:PA4228; -.
DR PATRIC; fig|208964.12.peg.4429; -.
DR PseudoCAP; PA4228; -.
DR HOGENOM; CLU_000022_59_7_6; -.
DR InParanoid; Q9HWG3; -.
DR OMA; PMSPHDE; -.
DR PhylomeDB; Q9HWG3; -.
DR BioCyc; MetaCyc:MON-15301; -.
DR BioCyc; PAER208964:G1FZ6-4301-MON; -.
DR PHI-base; PHI:6938; -.
DR PHI-base; PHI:6989; -.
DR Proteomes; UP000002438; 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 2: Evidence at transcript level;
KW Antibiotic biosynthesis; Ligase; Reference proteome.
FT CHAIN 1..547
FT /note="Pyochelin synthase PchD"
FT /id="PRO_0000454824"
FT CONFLICT 46
FT /note="Missing (in Ref. 1; CAA57966)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="R -> A (in Ref. 1; CAA57966)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="P -> A (in Ref. 1; CAA57966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 59901 MW; 57FF9D042D8AF638 CRC64;
MTSSPVTPSA VDDAPDWPAA FVRRYLDAGH WQDQSFAEAL ATSAARHPRR IALCDDDQRL
SYADLLQRCR RLAAGLRQAG LAHGDTVVLH LPNGIAFVET CFALFQLGVR PVLALPAHRQ
HEISGFCRFA EAKAYIGAER IDGFDPRPMA RELLASGACR MALIHGEAEA PLQALAPLYQ
ADALEDCAAR AEDIACFQLS GGTTGTPKLI PRRHREYLYN VRASAEVCGF DEHTVYLTGL
PMAHNFTLCC PGVIGTLLAS 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
