B6HLP9 · CHYA_PENRW
- ProteinNonribosomal peptide synthase chyA
- GenechyA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2382 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of the yellow pigment chrysogine (PubMed:29196288).
the NRPS chyA mediates the condensation of anthranilic acid and alanine into the intermediate 2-(2-aminopropanamido)benzoic acid (PubMed:29196288).
The remainder of the pathway is highly branched yielding at least 13 chrysogine-related compounds (PubMed:29196288).
The malonyl transferase chyE converts 2-(2-aminopropanamido)benzoic acid and 2-(2-aminopropanamido)benzamidine into 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 3-((1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)amino)-3-oxopropanoic acid, respectively (PubMed:29196288).
ChyD is an amidase, being responsible for the amidation of the carboxylic acid moiety of 2-(2-aminopropanamido)benzoic acid, 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 2-(2-((4-amino-1-carboxy-4-oxobutyl)amino)propanamido)benzoic acid (PubMed:29196288).
ChyC is involved in the same reactions as ChyD, but plays a more minor role in the amidation reactions compared to chyD (PubMed:29196288).
The oxidoreductases chyH and chyM are involved in oxidation reactions that form N-pyruvoylanthranilamide from 2-(2-aminopropanamido)benzamidine and (1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)glutamine, respectively (PubMed:29196288).
N-pyruvoylanthranilamide is further converted via two further branches in the pathway, yielding chrysogine and additional chrysogine-related coumpounds (PubMed:29196288).
Chrysogine is likely formed by a spontaneous ring closure from N-pyruvoylanthranilamide (PubMed:29196288).
the NRPS chyA mediates the condensation of anthranilic acid and alanine into the intermediate 2-(2-aminopropanamido)benzoic acid (PubMed:29196288).
The remainder of the pathway is highly branched yielding at least 13 chrysogine-related compounds (PubMed:29196288).
The malonyl transferase chyE converts 2-(2-aminopropanamido)benzoic acid and 2-(2-aminopropanamido)benzamidine into 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 3-((1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)amino)-3-oxopropanoic acid, respectively (PubMed:29196288).
ChyD is an amidase, being responsible for the amidation of the carboxylic acid moiety of 2-(2-aminopropanamido)benzoic acid, 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 2-(2-((4-amino-1-carboxy-4-oxobutyl)amino)propanamido)benzoic acid (PubMed:29196288).
ChyC is involved in the same reactions as ChyD, but plays a more minor role in the amidation reactions compared to chyD (PubMed:29196288).
The oxidoreductases chyH and chyM are involved in oxidation reactions that form N-pyruvoylanthranilamide from 2-(2-aminopropanamido)benzamidine and (1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)glutamine, respectively (PubMed:29196288).
N-pyruvoylanthranilamide is further converted via two further branches in the pathway, yielding chrysogine and additional chrysogine-related coumpounds (PubMed:29196288).
Chrysogine is likely formed by a spontaneous ring closure from N-pyruvoylanthranilamide (PubMed:29196288).
Pathway
Pigment biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ligase activity | |
Molecular Function | phosphopantetheine binding | |
Molecular Function | transferase activity | |
Biological Process | amino acid activation for nonribosomal peptide biosynthetic process | |
Biological Process | secondary metabolite biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNonribosomal peptide synthase chyA
- EC number
- Short namesNRPS chyA
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium > Penicillium chrysogenum species complex
Accessions
- Primary accessionB6HLP9
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Impairs the production of chrysogine and 13 other chrysogine-related compounds (PubMed:29196288).
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000443345 | 1-2382 | Nonribosomal peptide synthase chyA | |||
Sequence: MAAPSISPLFAPQMGVQRDFQDSEMQIATVNFPCTGQSNTSLANWLQQEEKSHLQLLQAAWSISLRSYTGSNDVLFSCLNTKDTAALGANSVVYVDEGNEDKYGSARRGNLREFDLAICFSKQNEANCPVIGIHHKPSVISTDFATMIAATVAKAIEEIVLHVDSLIASLDICSDADINCISRWNSPSDDGIPSAQCIHHIISQKCATQPESIAVSAWDGRLTYAELDGLSSSLAIRLQHLGVCQEIFVPLIFDKSKWAVIALLSVLKAGGAYFFLNPSNPIQYNLGLCSSLSPEVALCSPRHSTLAKSFAGTAIPVGEEHCELPESLPVDEKTPPCTAETTPSNAMYITFTSGTTGVPKGITTEHSAFYSMAMANGKALQVGPATRMLQFASYTFDVSNRDMLITLMFGGCICIPSELDRLNDLSGFINRQSVNLASLTPSLASTLNPALCPSLQGLVLGGESMNDSHISAWANHVRLFNAYGVSESAGIAALASDIQADYSPGNIGFGSGSTLWVVTIDQPDKLAPIGALGEMVIEGPSVARGYLGDKKRTEEQFTSTSKWKNRIRAQLSESRSSKRAFHTGDLVRYNLDGSLNFLGRKDHQVKIHGQRLELTAIEHHIAACLEVAESGFLHVAVVTAKNEGNGSVKLLAFLGLYTSRGSDSPSQLVSKKLEDVEALKVALRQHLLLCLPAFMVPVDFIFVQHMPLTTSGKINRLLLQEAAGHALLDDQKRNIDTSDLNGNQTPTTQNQRILIQSWAKALGIKSESIMRNDCFFRRGGDSIAAIKMAASLRQQELIISVSDVFKFSTFSDMASVLVKDHRPLQTAMLAPFSLIDNSQTVLDAVMEELGTGIDQIEDVYPCTHMQQGLIALTAQQPHSYIGRYTWQLAEMLDVEKFKNAWESAWLHNPILRTRIVQIPDGVFQVVVKTDMPWNTVTDISRGGDGKELREIDISNGPLIQFYLSKESFRLDIHHSLFDEWSLGLIMGQVERAYAGGGLRMQPFSPFVQHLLHERDTSLEDFWRQEFSGLQAEHFPAIASRPLSVEHPTEKVVLEHSVQLETGFSTKYTISSIVRLAWAIVLWHQTGSEDVVFGATVSGRNANIDGIDQLSGPTLATLPVRIKLAASQPIHEGLSQVQGQFVNMMVHEQAGLPRIRQVGREAAEACNFQNLLVVQPYEEQTESHMFKASANSASSSENAKSFASYPMVLICRPEKSGISMKAAFDPAILTPAAGHSILKQMSHVIQQLVTSDSTCIAAVSLVPPEDMATLRQWNHSLPNGVNTCIHARIQELCIGQPDTLAIHSQNLDLTYGQLDNYSDQFAQNLIGSGVKQGDFVPLFLERSPWVPVIMLAVLKTGAAFVLLDLSHPMQRLRTMCSMIDARIVVTSKEHADRSGNLLLPVIIFDPEAHAQNVSKQATAPELKPLTAVTTPDAPACVVFSSGSTGLPKGIVLPHSALTTSAAVMREYGMLGPKSRVFHFASFAFDISIGEILFTLAAGACVCVPHEEERKGNPAKAAGDLKVTWALLTPSVINLFDPSDVPTLEVLGSAGEPLTPQIVDTWAHRVKLYGMYAPAECTVISHIGRILPDTHHSNIGKSHGGVSWVVDPSDHNRLVPIGTVGELIVEGPTVSSGYLNDPAKTNEVFITSPSWLDEVRSHSGKMYKTGDLVRQTSEGSLEFVGRKDDQVKLHGQRLEVGEVEHCITSSCTAIKTATVECIKIREQNSRVSLVAFICPQTDEDWGQSLNDPSSEVGDLELISPPRDQFYSMIESLETSLRELLPAYMVPSFFVPLADVPLSLSGKVNRRLLRDQSTSWPMKRLGLYQLRRKSIPAEEVPVSIHGRKVQEIVGQALNLDPKSIPMNSNFFGLGGDSISAMQVSMLARRRGIRLTVADIFTQQTLSGLSLKCATENGDASQASKSRSLGRELPGSNIKSLHRCEIPRDKLPRQLPQEIADNIVEAMPATEFQTMTLHNFYSRYLWISLPERVNQEHLLNACDQLVQKHSVLRTVFYTNDDKSVVQLTLRKVPVNFVHYSNIENLEKHCADDSLAMGVPINSVPGFEVQLVTLRDSGMYLILRLPHAQFDGVSLDIICSDLSAAYSGDSLPPCAQFSDHIRHVWEKRIPESYNAWREVLGNVPMTSLNNKYLRNWGSASEMGSPNMGTDPDQPKVVTAMAETLPISPPPNITLATLVKLAWAITLSRLFTSIEEDDGASDDVVFGQVVHGRGLGISHEDRIVGPCLNIIPVRVHLPPRSNKLDLLGQVQQQHIQTMSVENLELGEITRNCTSWKAGTKFGSFIRFQNFTNNDDSTCSFDGSACETGLYSLPNRPSNTANVLVVPHGPTLSITMTISNQVLDRGSADFVAGYFSDVIESLASEETVCEYLE | ||||||
Modified residue | 782 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 1870 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 204-607 | Adenylation 1 | ||||
Sequence: QKCATQPESIAVSAWDGRLTYAELDGLSSSLAIRLQHLGVCQEIFVPLIFDKSKWAVIALLSVLKAGGAYFFLNPSNPIQYNLGLCSSLSPEVALCSPRHSTLAKSFAGTAIPVGEEHCELPESLPVDEKTPPCTAETTPSNAMYITFTSGTTGVPKGITTEHSAFYSMAMANGKALQVGPATRMLQFASYTFDVSNRDMLITLMFGGCICIPSELDRLNDLSGFINRQSVNLASLTPSLASTLNPALCPSLQGLVLGGESMNDSHISAWANHVRLFNAYGVSESAGIAALASDIQADYSPGNIGFGSGSTLWVVTIDQPDKLAPIGALGEMVIEGPSVARGYLGDKKRTEEQFTSTSKWKNRIRAQLSESRSSKRAFHTGDLVRYNLDGSLNFLGRKDHQVKI | ||||||
Domain | 745-821 | Carrier 1 | ||||
Sequence: TPTTQNQRILIQSWAKALGIKSESIMRNDCFFRRGGDSIAAIKMAASLRQQELIISVSDVFKFSTFSDMASVLVKDH | ||||||
Region | 857-1269 | Condensation 1 | ||||
Sequence: EDVYPCTHMQQGLIALTAQQPHSYIGRYTWQLAEMLDVEKFKNAWESAWLHNPILRTRIVQIPDGVFQVVVKTDMPWNTVTDISRGGDGKELREIDISNGPLIQFYLSKESFRLDIHHSLFDEWSLGLIMGQVERAYAGGGLRMQPFSPFVQHLLHERDTSLEDFWRQEFSGLQAEHFPAIASRPLSVEHPTEKVVLEHSVQLETGFSTKYTISSIVRLAWAIVLWHQTGSEDVVFGATVSGRNANIDGIDQLSGPTLATLPVRIKLAASQPIHEGLSQVQGQFVNMMVHEQAGLPRIRQVGREAAEACNFQNLLVVQPYEEQTESHMFKASANSASSSENAKSFASYPMVLICRPEKSGISMKAAFDPAILTPAAGHSILKQMSHVIQQLVTSDSTCIAAVSLVPPEDMATL | ||||||
Region | 1294-1687 | Adenylation 2 | ||||
Sequence: GQPDTLAIHSQNLDLTYGQLDNYSDQFAQNLIGSGVKQGDFVPLFLERSPWVPVIMLAVLKTGAAFVLLDLSHPMQRLRTMCSMIDARIVVTSKEHADRSGNLLLPVIIFDPEAHAQNVSKQATAPELKPLTAVTTPDAPACVVFSSGSTGLPKGIVLPHSALTTSAAVMREYGMLGPKSRVFHFASFAFDISIGEILFTLAAGACVCVPHEEERKGNPAKAAGDLKVTWALLTPSVINLFDPSDVPTLEVLGSAGEPLTPQIVDTWAHRVKLYGMYAPAECTVISHIGRILPDTHHSNIGKSHGGVSWVVDPSDHNRLVPIGTVGELIVEGPTVSSGYLNDPAKTNEVFITSPSWLDEVRSHSGKMYKTGDLVRQTSEGSLEFVGRKDDQVKL | ||||||
Domain | 1833-1909 | Carrier 2 | ||||
Sequence: VPVSIHGRKVQEIVGQALNLDPKSIPMNSNFFGLGGDSISAMQVSMLARRRGIRLTVADIFTQQTLSGLSLKCATEN | ||||||
Region | 1967-2373 | Condensation 2 | ||||
Sequence: MTLHNFYSRYLWISLPERVNQEHLLNACDQLVQKHSVLRTVFYTNDDKSVVQLTLRKVPVNFVHYSNIENLEKHCADDSLAMGVPINSVPGFEVQLVTLRDSGMYLILRLPHAQFDGVSLDIICSDLSAAYSGDSLPPCAQFSDHIRHVWEKRIPESYNAWREVLGNVPMTSLNNKYLRNWGSASEMGSPNMGTDPDQPKVVTAMAETLPISPPPNITLATLVKLAWAITLSRLFTSIEEDDGASDDVVFGQVVHGRGLGISHEDRIVGPCLNIIPVRVHLPPRSNKLDLLGQVQQQHIQTMSVENLELGEITRNCTSWKAGTKFGSFIRFQNFTNNDDSTCSFDGSACETGLYSLPNRPSNTANVLVVPHGPTLSITMTISNQVLDRGSADFVAGYFSDVIESLAS |
Domain
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase. ChyA has the following architecture: A-T-C-A-T-C.
Sequence similarities
Belongs to the NRP synthetase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,382
- Mass (Da)260,769
- Last updated2008-12-16 v1
- Checksum582DAC279F7F88E7
Keywords
- Technical term