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Entry version 95 (10 Apr 2019)
Sequence version 1 (05 Jul 2005)
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Protein

Catalase easC

Gene

easC

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592, PubMed:23435153). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).By similarity8 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

hemeBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ergot alkaloid biosynthesis

This protein is involved in the pathway ergot alkaloid biosynthesis, which is part of Alkaloid biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway ergot alkaloid biosynthesis and in Alkaloid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei71By similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi361Iron (heme axial ligand)By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • catalase activity Source: GO_Central
  • heme binding Source: GO_Central
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase, Peroxidase
Biological processAlkaloid metabolism, Hydrogen peroxide
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00327

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Catalase easCCurated (EC:1.11.-.-1 Publication)
Alternative name(s):
Ergot alkaloid synthesis protein C1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:easC1 Publication
ORF Names:AFUA_2G18030
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri330879 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002530 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:Afu2g18030

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Ergot alkaloids are known for their toxic effects on humans who consume contaminated grains or livestock that graze on grasses harboring ergot alkaloid-producing fungi (PubMed:19523108). Due to their strong affinity for monoamine neurotransmitter receptors they may also have clinical uses such as treatment of migraines, Parkinson's disease and cerebrovascular insufficiency (PubMed:19523108).1 Publication

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Accumulates the intermediate 4-dimethylallyl-L-abrine (PubMed:21409592).1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004364101 – 520Catalase easCAdd BLAST520

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

The expression of the ergot alkaloid synthesis cluster which leads to the synthesis of fumigaclavines is positively regulated by the brlA and stuA transcription factors (PubMed:19028996).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
746128.CADAFUBP00003305

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q4WZ63

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q4WZ63

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000087852

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q4WZ63

KEGG Orthology (KO)

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KOi
K03781

Identification of Orthologs from Complete Genome Data

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OMAi
KEGNWDW

Database of Orthologous Groups

More...
OrthoDBi
507937at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.180.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018028 Catalase
IPR024708 Catalase_AS
IPR024711 Catalase_clade1/3
IPR011614 Catalase_core
IPR037060 Catalase_core_sf
IPR002226 Catalase_haem_BS
IPR010582 Catalase_immune_responsive
IPR020835 Catalase_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11465 PTHR11465, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00199 Catalase, 1 hit
PF06628 Catalase-rel, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF038928 Catalase_clade1-3, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00067 CATALASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01060 Catalase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56634 SSF56634, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00437 CATALASE_1, 1 hit
PS00438 CATALASE_2, 1 hit
PS51402 CATALASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q4WZ63-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLIERGLLSI MASKCSGTWS TYKTYTTANG CPFMKPEGPP ADGRTLALND
60 70 80 90 100
HHLVESLAHF NREKIPERAV HAKGAAAYGE FEVTADISDI CNIDMLLGVG
110 120 130 140 150
KKTPCVTRFS TTGLERGSAE GMRDLKGMAT KFYTKEGNWD WVCLNFPFFF
160 170 180 190 200
IRDPLKFPSL MHAQRRDPRT NLLNPNMYWD WVTSNHESLH MVLLQFSDFG
210 220 230 240 250
TMFNWRSLSG YMGHAYKWVM PNGSFKYVHI FLSSDRGPNF SQGEQAKDNS
260 270 280 290 300
DLDPDHATRD LYEAIERGDY PTWTANVQVV DPAEAPDLGF NILDVTKHWN
310 320 330 340 350
LGTYPKDLPK IPSRPFGKLT LNRIPDNFFA EVEQLAFSPS NMVPGVLPSE
360 370 380 390 400
DPILQARMFA YPDAQRYRLG PNHHKIPVNQ CPMTFNPTLR DGTGTFDANY
410 420 430 440 450
GSLPGYVSES QGVNFARPQE HDPKFNAWLS QLSSRPWMQT NENDYKFPRD
460 470 480 490 500
FYNALPEFRS QEFQDKMVEN IIASVAQTRR EIREKVYHTF HLVDPELSAR
510 520
VKRGVEKMDA SFKQVSLSRL
Length:520
Mass (Da):59,342
Last modified:July 5, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2AABE8F13C451EC2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AAHF01000001 Genomic DNA Translation: EAL94102.1

NCBI Reference Sequences

More...
RefSeqi
XP_756140.1, XM_751047.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EAL94102; EAL94102; AFUA_2G18030

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3512715

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
afm:AFUA_2G18030

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000001 Genomic DNA Translation: EAL94102.1
RefSeqiXP_756140.1, XM_751047.1

3D structure databases

ProteinModelPortaliQ4WZ63
SMRiQ4WZ63
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi746128.CADAFUBP00003305

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAL94102; EAL94102; AFUA_2G18030
GeneIDi3512715
KEGGiafm:AFUA_2G18030

Organism-specific databases

EuPathDBiFungiDB:Afu2g18030

Phylogenomic databases

HOGENOMiHOG000087852
InParanoidiQ4WZ63
KOiK03781
OMAiKEGNWDW
OrthoDBi507937at2759

Enzyme and pathway databases

UniPathwayi
UPA00327

Family and domain databases

Gene3Di2.40.180.10, 1 hit
InterProiView protein in InterPro
IPR018028 Catalase
IPR024708 Catalase_AS
IPR024711 Catalase_clade1/3
IPR011614 Catalase_core
IPR037060 Catalase_core_sf
IPR002226 Catalase_haem_BS
IPR010582 Catalase_immune_responsive
IPR020835 Catalase_sf
PANTHERiPTHR11465 PTHR11465, 1 hit
PfamiView protein in Pfam
PF00199 Catalase, 1 hit
PF06628 Catalase-rel, 1 hit
PIRSFiPIRSF038928 Catalase_clade1-3, 1 hit
PRINTSiPR00067 CATALASE
SMARTiView protein in SMART
SM01060 Catalase, 1 hit
SUPFAMiSSF56634 SSF56634, 1 hit
PROSITEiView protein in PROSITE
PS00437 CATALASE_1, 1 hit
PS00438 CATALASE_2, 1 hit
PS51402 CATALASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEASC_ASPFU
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q4WZ63
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 8, 2016
Last sequence update: July 5, 2005
Last modified: April 10, 2019
This is version 95 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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