IED ID | IndEnz0010000371 |
Enzyme Type ID | esterase000371 |
Protein Name |
Highly reducing polyketide synthase alnA EC 2.3.1.- Asperlin biosynthesis cluster protein A |
Gene Name | alnA ANIA_11191 |
Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Enzyme Sequence | MNLPGEIHHRFTYMYIAQVSFADLDITKHNLPISTMSSSDSPNYGDATMPIAIVGMAARFSGEATNPSKLWDMMVQGRTGHSAVPENRFDAEAWHHPSHERRGTIQPRSGFFLREDPAVFDAPFFSMTAKEAAGMDPMQRKLLEISYEAFENAGIPITKLPGTATGVYSGVMTNDYELMTAGDPMQLPQNAASGTSRAMLANRISWFYDLRGPSFALDTACSSSLYALHLACQSLQAGETDQALVTGVNLILAPNFISQLSSMHMLSPDGKSHSFDSRANGYARGEALAAVVVKPLYQALADGDTIRAVIRGSGANQDGKTVGITIPNPQAQAELIRKTYATAGLGLEQTGYFEAHGTGTPVGDPIELSAIGTSFGEHRSQNCPLFVGSVKTNVGHTEGAAGLAGVVKTVLALEAGIIPPLADFQELNEKLRLEEWKLALPLKATPWPMPGLRRASVNSFGFGGANAHVILDDAYHYLKSHGLSANHHTTLSESEDSSDSGLEMDSSTSDSGEGQSSKLLLFSAYDGAGIKRTEASWNSHLADILADSKTVDETMGMNDLAYTLSDRRTTFDFRSFAVASSVQDLKAKLENDGLPRLNRASRRSNPVFVFTGQGAQWPAMGRELLSNPIFRASIERSKAVLELEGCEWDVVQVLSDPQDQRIHIPAFSQPVCTILQVALVDLLQSWGIQPAATVGHSSGEVAAAYAAKMISQDEAVRIGYWRGFYSEQVKARLENIRGSMMAVGLSESQATSYLNRVPEGSVVVACINSPSSVTLSGEDHSIKTLEAILQADGHFARKLRVEVAYHSPHMKTVADEFLNAVGIITPQPSEIPMFSSVTETRVEDPATLVASYWMQNLISPVRFSGALATLLNDTPSVKANTRRRRTAGIVWSALIEVGPHEALKGPCRQIMSGLNTKLADQIPYMSVLSRGKSAVETSLTAAGLLWASGHPINIREVNQYRDTGERVITDLPPYPWNHEKGFWHEPAASISARLRKEPRNDLLGVPVAQQNPFERCWQNYLSVSECPWQKDHVITGTVLYPGAGHLIMAFEAAIRLAADNRPLKGVSFSDVHFDKGLVIPSDDHGVETRLCTRPHESLLDWYHYTLYSINATGDWTKHSWGSFSLHYEDAVSVQQAKRSKGEYDDINTRACRKLDVESFYEQLLSIGTEYGPTFRNLVHAAAAPGYHSGVGTITIPDTKSVMPHEFEYPHLIHPATLDAIFHLIFVAMGEGNALSESAIPTRVDRIYISTDLPRGVGAKYTGYGRAEPVSSRDTLGTIVVSDENWSAGPKIIVEGMTVTEVSAGASTSFNSLLIPGGQGRIATLEWKEDVDSLVGPTAESWLAQKGPSIGGQASDVTEAVQRLDAWLELSCFKSTDLGTLVICPSKLKGSFELVKKYGSKHGERYRFGRTTIIEFSENDISAAESAFAPHGIESSYAAIDLSATPEHAMEQLGMFDLIIAEENVIVQFPDVTKILHREGRVAIIRSHALPDERHFAATKGLLKEISFESQDGSILQIAGLGLEMDPAIRSLDDVVLLQHVDASPAAKNFEKRLTAQLTSLGAHVRSNTIANASSLSGNIVISLLEIDCQFVISWTSEEFEQFRQLTNARYVLWITRGGLLDADRASLDYAPSTGLLRTVRVEKPQIRLPHLDLSPSLDLNSDRAVEIVISAFHSSIKPSVKEKNLEMEYAESNGLLYIPRARGHAALDHELALRGEKVSSIPGPLSAPGIARRLETSLAGSPSQARWVPDETVGDKLADFDVEIQVSHVGLEHSKVENYLNGKQLSLAPGLGRVAVGTLTRAGAKVSRFIPGDQVFALHAAPFHTHLRVTEDAVHAVPDILSPAQAAHLPLAAARAWHSLIDVAAFRAGQSVFVNGASDTVGRLTVELARLLKGDVFASVSSDDEKHTLTKTYNIPEDHIFSLSHRTDWASDLKAAMGQGQLDIVINNATPSPAIRSLFQSIAPKGRFVDLTQRLDPSLLDPRMFQRNVTLSLVDWESLTNPQLGALMVRSLDLLRAGALTPIKEEYIFSVSDLPEALLSVGQQQHERVAAPVVVEFSADATVPLLPSLPAPLHLKPDATYILAGGLGALGLTIAENMCSHGAGHLVFLSRSGASSQRQQEALESFRARGCKVDVVKCDVTDQEQVQALATQIREQSWNVRGIIQLAMVLRDSIFENMTFDKWETAVNPKIKGTWNLHAELPKDVDFFIILSSLSGIIGNTAQANYCAGNTYEDALAHYRRKQGLAATTLNVGLVTDASHFNENSTIEDYLRKYSHWIAAQVTDSELQHTITAVMRRTVGDKNEPVPDQLLVGLSDNVRRDGNSLNLWPQDRKFDHRISLEDGLGVVEKDTNQQKLKASTTVAQAHEVVETALRLNVAAAMTASPDDIDIEKPLYAFGIDSLKGIEVRNWIFSELQADVSVFEVLSPMTLSRLALKIVSKSTLVGAELAAEAAADSVA |
Enzyme Length | 2458 |
Uniprot Accession Number | C8VJR7 |
Absorption | |
Active Site | ACT_SITE 221; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 221; /note=For beta-ketoacyl synthase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 697; /note=For malonyltransferase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 1032; /note=For beta-hydroxyacyl dehydratase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 2.3.1.- |
Enzyme Function | FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities (PubMed:30339758). The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA with cleavage of the PKS product by the esterase alnB (PubMed:30339758). 2,4,6-octatrienoic acid is further converted to asperlin via several steps involving the remaining enzymes from the cluster (PubMed:30339758). {ECO:0000269|PubMed:30339758}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:30339758}. |
nucleotide Binding | |
Features | Active site (4); Chain (1); Domain (1); Modified residue (1); Region (6) |
Keywords | Multifunctional enzyme;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Reference proteome;Transferase |
Interact With | |
Induction | INDUCTION: Expression is controlled by the asperlin biosynthesis cluster-specific transcription factor alnR. {ECO:0000269|PubMed:30339758}. |
Subcellular Location | |
Modified Residue | MOD_RES 2401; /note=O-(pantetheine 4'-phosphoryl)serine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00258 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 267,558 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |