A8NF97 · CPF1_COPC7

Function

function

Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of coprinoferrin, an acylated tripeptide hydroxamate siderophore (PubMed:31496254).
The biosynthesis of coprinoferrin depends on the hydroxylation of ornithine to N5-hydroxyornithine, catalyzed by the monooxygenase cpf2 (PubMed:31496254).
The second step, the acylation of N5-hydroxy-L-ornithine to yield N5-hexanoyl-N5-hydroxyl-L-ornithine is catalyzed by a not yet identified acyltransferase (Probable). Finally, assembly of coprinoferrin is catalyzed by the nonribosomal peptide synthase (NRPS) cpf1 via amide bond formation between three N5-hexanoyl-N5-hydroxyl-L-ornithine molecules to release the linear trimer (PubMed:31496254).
Interestingly, proteins seemingly not directly related to biosynthesis, such as transcription factors, replication factors, and autophagy-related proteins, are conserved among the clusters homologous to the coprinoferrin cluster, suggesting that the cluster may also play developmental and cell biological functions (Probable)

Pathway

Siderophore biosynthesis.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular Functionligase activity
Molecular Functionphosphopantetheine binding
Biological Processamino acid activation for nonribosomal peptide biosynthetic process
Biological Processsecondary metabolite biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Coprinoferrin synthetase
  • EC number
  • Alternative names
    • Coprinoferrin biosynthesis cluster protein cpf1
    • Nonribosomal peptide synthetase cpf1
      (NRPS cpf1
      )
    • Siderophore biosynthesis protein cpf1

Gene names

    • Name
      cpf1
    • ORF names
      CC1G_04210

Organism names

Accessions

  • Primary accession
    A8NF97

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Abolishes the production of coprinoferrin and fails to form fruiting bodies.

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00004527341-2410Coprinoferrin synthetase
Modified residue820O-(pantetheine 4'-phosphoryl)serine
Modified residue1361O-(pantetheine 4'-phosphoryl)serine
Modified residue1893O-(pantetheine 4'-phosphoryl)serine

Keywords

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region237-646Adenylation 1
Domain783-860Carrier 1
Region891-1260Condensation 1
Region1298-1317Disordered
Domain1324-1400Carrier 2
Region1436-1839Condensation 2
Domain1858-1932Carrier 3
Region1992-2315Condensation 3

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, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase. Cpf1 has the following architecture: A-T-C-T-C-T-C.

Sequence similarities

Belongs to the NRP synthetase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,410
  • Mass (Da)
    267,726
  • Last updated
    2010-08-10 v2
  • Checksum
    EBCA5161FD168D6E
MALRDTAGVPPLLQGYSIVEWPDLTCDRHPSPTPYTSTQPLSSFNVQSRGSLLLAAISRMLGAYCGASDILLAVQVPNKRDYVFVRVNWSDNETWQEVAARTASQTRKTKSKLLVGDIRRAFELPDKQNPCPVLVRFTPSEEPSYFSDFPAVFIFDAKKSSLTLSAPKSLLHPSINDQLLSQIISLYHHAGANPKTPVSSNPTFPSHLTSVYDRLPEEDISNAYPHIPLVKFATEYLERRAKTNPHDIAVRWFPELSIDDSNLPSETSTYEELDRKASQLGRWLVTRGLAPEDRVAVCLSRDLIFHAAFFGIMRAGGCYVPIDPELPDERKAYIARDSGAKFVLTTSELSSQDLFGSSTIYVDEPEVANAIDEQDGGTFNIATPEGLGYMLYTSGTTGNPKGCLLTNHGLAQAIIALSSTAADVRMKDIREGRYLAVASIAFDVHLAETIVPMALGMPLLSAPRSQLLENLPQYVKLLGITHLGIVPSLIEATLNASKDNEGGLALRYIASGGEKMSDSILDKWANHPQVRLANFYGPSEVTIGCCARYMDSNTPRANIGRPLANVSGYVVDADLNILPRGGVGELVVEGPLVGRGYHGRPDLTEKVFLEWPEKGRWAYRTGDLVRMMPDSTLEILGRIDTQIKVRGVRIESEGISAIVRKAEVPSADMVLDATTVLAKHPALGSEQLVSFVTWDSTVPVSTRKSLRPSLSIPPRGFLKSIRSICNKELASYMRPNHVIPLNWLPLSSNGKTDTKILVELFKNLDIAQLASLISSEDDVSVSRDCTPLEAEVFEIVQRHAPSYAQRPHPELNIFECGLDSMGVIRFAADLKLTFGKAIPATEIMKKPALQDIAQLVHVSTMNHSLVGTPLPTIDAATHKHLSSIYSNDIEDILPPFPVQEGVLARSVEDTSLYVQHVILHLDSGTSMSQLQRSWESVIAAHPILRTVFYVDRSVWQVVFKSFNLPNSWSDRSLSVKTVEEFRARFYSRFAGEITKDINRNLSSIPPFRLAYFRCTGFNVLVLSIHHALYDGTSLPVLLRDVENSYLGLERVQKASLRAILAEISKHDLALAQQFWRDSFREFEWPRPAFRQGSNALASSVKYLSVHFTQKLSVIREVANKKQVTLQALLSFTFAYLIGSRLYDSNDVAFGVIRSGRMLPVDNVDVALCPTITVLPMRVRLGDANSTLVNIQNGISTMTEHEHVPLGKVQNWLRPGEPLFEVLFSVSVQQQEESKIWRPCDYEPPAADYALSVEAVVNVHDDTLIVRAAWLDGLITQDHVADLLHGFEKVTLTLDKGEELPLPSRRSPEPVRKVNDDEDPSAQVLLDPVVVADLQQTICDFLEIPTAILTNRVSFISLGLDSIKAVGLAKRIRALGYDVSSTEILRASTLKRLARVVSNNKQKKEEPYEHYAQLVRQVEGYISKSEVQLSPEDEVKIIPSTALQSGMLSQTVGSDGRLYVHAFPLTLSPGVDVQRLKSAWEAAAEKIDILRTSFHFIPDNGTWVQVIHSFNELKWSIQNLEGFVNVTSAVKSFVESIECTDEFAFSTPPFWLRVFTPLKGPSVLALVMHHALYDGGSVNSLLDVVQRIYRGESISYPVQFADLLPDFFRQELQNLERTLLPLHSLPSSDPYHISIRQVEVKDVDLKRLLTETEVTLQCLLQGALAQSLAILTRSADVVFGNVVSGRVGRGTEEVVGPILNTIPCRVHISDHDSVDALLQSIHRFNMEAASWQQASLRSIQKALMVDRIWDCLFTFQPLAPPPQAAIWSLDIEEHEDIHIQYPLHVEIEQNKDGFSVRCACQSNVLDKAGLLNFMDTLSNTVQQFVANPKERIGRTFSVPSPSNTDPTPTTVVAPAPATVQAGIIHPVLLSAIRDFAPDAEVTFDTPLPALGIDSITAIQISGKCRRSGLRLTATQILNSSTVKDLVLQATEIKATAKSTQVSDGVFKPLSSEEKDSIARRFADDAKYIENISVTTAGMKWAIGGWQRTNGSLFQYLFTFKLPDDVDHARFKNAWHMFIRRHELMRSTFATAPGGTEPRIVTFSKDFKFDHWAEIVVDDAVFYRRLLGKMKEMVSDPVPISRPPVRAALFRSDKQSYFIFHIHHFQYDAWSMQVLLNDLSSIYYDQEPWAVTDLRAFTSLFDPNEERLSVQRRFWEKALSPSFKPSLLPSLLNEVQGPLATPTGQPQLIMVPGALTNVSRYEEQARKLGVTLQTVLLAAWAQVQANRSRTSASTFGVWQVSRSGHIDGIERLAVPCVNVLPIHVKVGGSLVEVTKRIQVDLSERLSQPVIEHSDLVNISKWTGMSGETPIFNVNVNVVKLPVTLKRDGLVEPVKAPYYIPRIAVPTVTPTLDRLAVSPLCQNDVVVDIIVYEESDSILMSIEAVDNIMTEGQAKDIIQEWASVVSTTLSYKD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AACS02000002
EMBL· GenBank· DDBJ
EAU88504.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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