Q9HWG4 · PCHF_PSEAE
- ProteinPyochelin synthetase PchF
- GenepchF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1809 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Involved in the biosynthesis of the siderophore pyochelin (PubMed:11208777, PubMed:9846750).
Adenylates L-cysteine and loads it onto its peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety (By similarity).
Then forms a peptide bond between the salicyl-thiazolinyl intermediate bound to the second carrier domain of PchE and the cysteine bound to its own peptidyl carrier domain to form the salicyl-thiazolinyl-cysteinyl-S-PCP2 intermediate. It subsequently cyclizes the C-terminal cysteine to form the second thiazoline heterocycle in the salicyl-thiazolinyl-thiazolinyl-S-PCP2 intermediate (By similarity).
When this intermediate is released by the action of a thioesterase, it produces the tricyclic acid hydroxyphenyl-thiazolyl-thiazolinyl-carboxylic acid (HPTT-COOH), an advanced intermediate containing the aryl-4,2-bis-heterocyclic skeleton of the bithiazoline class of siderophores (By similarity).
Adenylates L-cysteine and loads it onto its peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety (By similarity).
Then forms a peptide bond between the salicyl-thiazolinyl intermediate bound to the second carrier domain of PchE and the cysteine bound to its own peptidyl carrier domain to form the salicyl-thiazolinyl-cysteinyl-S-PCP2 intermediate. It subsequently cyclizes the C-terminal cysteine to form the second thiazoline heterocycle in the salicyl-thiazolinyl-thiazolinyl-S-PCP2 intermediate (By similarity).
When this intermediate is released by the action of a thioesterase, it produces the tricyclic acid hydroxyphenyl-thiazolyl-thiazolinyl-carboxylic acid (HPTT-COOH), an advanced intermediate containing the aryl-4,2-bis-heterocyclic skeleton of the bithiazoline class of siderophores (By similarity).
Catalytic activity
- holo-[peptidyl-carrier protein] + L-cysteine + ATP = L-cysteinyl-[peptidyl-carrier protein] + AMP + diphosphateThis reaction proceeds in the forward direction.
Cofactor
Pathway
Siderophore biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ligase activity | |
Molecular Function | phosphopantetheine binding | |
Biological Process | amino acid activation for nonribosomal peptide biosynthetic process | |
Biological Process | secondary metabolite biosynthetic process | |
Biological Process | toxin biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePyochelin synthetase PchF
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9HWG4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Mutant can still form salicylate and Dha, but is no longer able to synthesize pyochelin.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000454828 | 1-1809 | Pyochelin synthetase PchF | |||
Sequence: MSLGELLETCRSRRIELWSEAGRLRYRAPQGALDAGLAERLRAEREALLEHLEGGPGWRAEPDMAHQRFPLTPVQAAYVLGRQAAFDYGGNACQLYAEYDWPADTDPARLEAAWNAMVERHPMLRAVIEDNAWQRVLPEVPWQRLTVHACAGLDEAAFQAHLERVRERLDHACAALDQWPVLRPELSIGRDACVLHCSVDFTLVDYASLQLLLGEWRRRYLDPQWTAEPLEATFRDYVGVEQRRRQSPAWQRDRDWWLARLDALPGRPDLPLRVQPDTRSTRFRHFHARLDEAAWQALGARAGEHGLSAAGVALAAFAETIGRWSQAPAFCLNLTVLNRPPLHPQLAQVLGDFTALSLLAVDSRHGDSFVERARRIGEQMFDDLDHPTFSGVDLLRELARRRGRGADLMPVVFTSGIGSVQRLLGDGEAPRAPRYMISQTPQVWLDCQVTDQFGGLEIGWDVRLGLFPEGQAEAMFDDFVGLLRRLAQSPRAWTDGDATEPVEAPPQALPGSARSIAAGFAERALLTPDATAIHDAAGSYSYRQVAQHASALRRVLEAHGAGRGRRVAVMLPKSAAQLVAVIGILQAGAAYVPVDIRQPPLRRQAILASAEVVALVCLESDVPDVGCACVAIDRLAADSAWPPPPAAEVAADDLAYVIYTSGSTGTPKGVMLSHAAVSNTLLDINQRYGVDANDRVLGLAELSFDLSVYDFFGATAAGAQVVLPDPARGSDPSHWAELLERHAITLWNSVPAQGQMLIDYLESEPQRHLPGPRCVLWSGDWIPVSLPTRWWRRWPDSALFSLGGATEAAIWSIEQPIRPQHTELASIPYGRALRGQSVEVLDARGRRCPPGVRGEIHIGGVGLALGYAGDPQRTAERFVRHPDGRRLYRTGDLGRYLADGSIEFLGREDDQVKIRGHRIELAELDAALCAHPQVNLAATVVLGETHERSLASFVTLHAPVEAGEDPRTALDAVRQRAAQALRRDWGSEEGIAAAVAALDRACLASLAAWLAGSGLFASATPLDLATLCQRLGIAEARQRLLRHWLRQLEEGGYLRAEGEGWLGCAERPAQSPEDAWTAFAGCAPAALWPAELVAYLRDSAQSLGEQLAGRISPAALMFPQGSARIAEAMYSQGLHAQALHEAMAEAIAAIVERQPQRRWRLLELGAGTAAASRTVIARLAPLVQRGAEVDYLFTDVSSYFLAAARERFADQPWVRFGRFDMNGDLLDQGVAPHSVDILLSSGALNNALDTPALLAGLRELLSADAWLVIQELTREHNEISVSQSLMMENPRDLRDERRQLFVHTGQWLEWLAAQGGDLACGVVPPGSALDLLGYDVLLARCKTDRARLEPAELLAFVEARVPRYMLPAQLRVLERLPVTGNGKIDRKALTGFARQPQADLRHGVAQAPADELENALLALWREVLDNPSLGVEQDFFGAGGDSLLIAQLIARLRERLESARRHPFDRLLRWALSQPTPRGLAERLRSAPEEGRGPALAAARGVAPAPAGMSRAPLAEGAVALDPLVRLVPGEGVPRVLVHEGLGTLLPYRPLLRALGEGRPLLGLAVHDSDAYLAIPAEHLNACLGRRYAEALHRAGLREVDLLGYCSGGLVALETAKSLVQRGVRVRQLDIVSSYRIPYRVDDERLLLFSFAATLGLDTAALGFPAPERLGQAVQAALAQTPERLVAEALAGLPGLADLVALRGRVLQAASGSADAVSVERDTLYRLFCHSVRASQAEAPEPYVGALRLFVPDAGNPLVPRYAEALETQWRAAALGACGIHEVPGGHFDCLGEALAQSLSKPMPEEASR | ||||||
Modified residue | 1442 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Induction
Expression of the pchEF operon is strictly dependent on the PchR regulator and is induced by extracellular pyochelin, the end product of the pathway. Repressed by Fur and iron.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 69-490 | Condensation/cyclization | ||||
Sequence: FPLTPVQAAYVLGRQAAFDYGGNACQLYAEYDWPADTDPARLEAAWNAMVERHPMLRAVIEDNAWQRVLPEVPWQRLTVHACAGLDEAAFQAHLERVRERLDHACAALDQWPVLRPELSIGRDACVLHCSVDFTLVDYASLQLLLGEWRRRYLDPQWTAEPLEATFRDYVGVEQRRRQSPAWQRDRDWWLARLDALPGRPDLPLRVQPDTRSTRFRHFHARLDEAAWQALGARAGEHGLSAAGVALAAFAETIGRWSQAPAFCLNLTVLNRPPLHPQLAQVLGDFTALSLLAVDSRHGDSFVERARRIGEQMFDDLDHPTFSGVDLLRELARRRGRGADLMPVVFTSGIGSVQRLLGDGEAPRAPRYMISQTPQVWLDCQVTDQFGGLEIGWDVRLGLFPEGQAEAMFDDFVGLLRRLAQSP | ||||||
Region | 520-915 | Adenylation | ||||
Sequence: FAERALLTPDATAIHDAAGSYSYRQVAQHASALRRVLEAHGAGRGRRVAVMLPKSAAQLVAVIGILQAGAAYVPVDIRQPPLRRQAILASAEVVALVCLESDVPDVGCACVAIDRLAADSAWPPPPAAEVAADDLAYVIYTSGSTGTPKGVMLSHAAVSNTLLDINQRYGVDANDRVLGLAELSFDLSVYDFFGATAAGAQVVLPDPARGSDPSHWAELLERHAITLWNSVPAQGQMLIDYLESEPQRHLPGPRCVLWSGDWIPVSLPTRWWRRWPDSALFSLGGATEAAIWSIEQPIRPQHTELASIPYGRALRGQSVEVLDARGRRCPPGVRGEIHIGGVGLALGYAGDPQRTAERFVRHPDGRRLYRTGDLGRYLADGSIEFLGREDDQVKIR | ||||||
Domain | 1407-1488 | Carrier | ||||
Sequence: APADELENALLALWREVLDNPSLGVEQDFFGAGGDSLLIAQLIARLRERLESARRHPFDRLLRWALSQPTPRGLAERLRSAP | ||||||
Region | 1584-1797 | Thioesterase | ||||
Sequence: LGRRYAEALHRAGLREVDLLGYCSGGLVALETAKSLVQRGVRVRQLDIVSSYRIPYRVDDERLLLFSFAATLGLDTAALGFPAPERLGQAVQAALAQTPERLVAEALAGLPGLADLVALRGRVLQAASGSADAVSVERDTLYRLFCHSVRASQAEAPEPYVGALRLFVPDAGNPLVPRYAEALETQWRAAALGACGIHEVPGGHFDCLGEALAQ |
Domain
Modular protein that contains a condensation/cyclization domain involved in the cyclization of the cysteine, an adenylation domain which activates the cysteine residue into an aminoacyl-AMP ester, a peptidyl carrier protein (PCP2) domain which bears a phosphopantetheinyl arm to attach the activated cysteine and a thioesterase domain (TE) that may release the newly synthesized peptide from the enzyme.
Sequence similarities
Belongs to the NRP synthetase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,809
- Mass (Da)197,084
- Last updated2001-03-01 v1
- Checksum39978C86A1BB5F0B
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 799-805 | in Ref. 1; AAC83657 | ||||
Sequence: LFSLGGA → AVQPGRR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF074705 EMBL· GenBank· DDBJ | AAC83657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE004091 EMBL· GenBank· DDBJ | AAG07613.1 EMBL· GenBank· DDBJ | Genomic DNA |