Detail Information for IndEnz0010000371
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