Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - E9QYP0 (SIDA_ASPFU)

Entry version 64 (25 May 2022)
Sequence version 1 (05 Apr 2011)
Previous versions | rss
Add a publicationFeedback
Protein

L-ornithine N(5)-monooxygenase

Gene

sidA

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

Annotation score:5 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

L-ornithine N5-monooxygenase; part of the siderophore biosynthetic pathway (PubMed:15504822, PubMed:16113265, PubMed:17845073, PubMed:20614882, PubMed:20650894, PubMed:22465572).

Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake; and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N2-acetyl-N5-anhydromevalonyl-N5-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265, PubMed:20614882, PubMed:20650894, PubMed:22465572).

SidA is highly specific for its substrate, only hydrolyzing l-ornithine, and has preference for NADPH over NADH, NADPH playing a role in stabilization of the C4a-hydroperoxyflavin intermediate (PubMed:20614882, PubMed:22465572).

Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073).

For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N5-hydroxyornithine (PubMed:17845073).

The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303).

The acetylation of N5-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789).

FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073).

Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073).

Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073).

Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).

8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

FAD3 PublicationsNote: Binds 1 FAD per subunit.3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 29 min(-1) with L-ornithine as substrate and 75 min(-1) with NADPH as substrate.1 Publication
  1. KM=1.7 mM for L-ornithine (in the presence of 1 mM NADH)1 Publication
  2. KM=1.7 mM for L-ornithine (in the presence of 1 mM NADPH)1 Publication
  3. KM=0.49 mM for L-ornithine (at 37 degrees Celsius)1 Publication
  4. KM=0.58 mM for L-ornithine (at 25 degrees Celsius)1 Publication
  5. KM=0.94 mM for NADPH (in the presence of 15 mM L-ornithine)1 Publication
  6. KM=0.90 mM for NADH (in the presence of 15 mM L-ornithine)1 Publication
  7. KM=4.6 µM for NADPH (at 37 degrees Celsius)1 Publication
  8. KM=2.6 µM for NADPH (at 25 degrees Celsius)1 Publication
  9. KM=18 µM for O2 (at 37 degrees Celsius)1 Publication
  10. KM=16 µM for O2 (at 25 degrees Celsius)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ferrichrome biosynthesis

This protein is involved in the pathway ferrichrome biosynthesis, which is part of Siderophore biosynthesis.6 Publications
View all proteins of this organism that are known to be involved in the pathway ferrichrome biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei102FAD; via amide nitrogen1 Publication1
Binding sitei107Substrate1 Publication1
Binding sitei168FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei279NADP1 Publication1
Binding sitei323Substrate1 Publication1
Binding sitei469Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi83 – 91FAD1 Publication9
Nucleotide bindingi254 – 257NADP1 Publication4
Nucleotide bindingi323 – 325NADP1 Publication3
Nucleotide bindingi466 – 468FAD1 Publication3

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionMonooxygenase, Oxidoreductase
LigandFAD, Flavoprotein, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.14.13.195, 508
1.14.13.196, 508

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

More...UniPathwayi		UPA00783

<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%5Fand%5Ftaxonomy%5Fsection">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:
L-ornithine N(5)-monooxygenase1 Publication (EC:1.14.13.1962 Publications)
Short name:
OMOBy similarity
Alternative name(s):
L-ornithine N(5)-oxygenase1 Publication
Siderophore biosynthesis protein A1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:sidA1 Publication
ORF Names:Afu2g07680
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Fumigati ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:Afu2g07680

<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 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

Moderatley reduced growth rate during iron starvation and in iron replete conditions. Only displays 1% of wild-type conidiospore production in iron-depleted and replete conditions. Completely attenuates virulence in a mouse model of invasive pulmonary aspergillosis.2 Publications

Miscellaneous databases

Pathogen-Host Interaction database

More...PHI-basei		PHI:377
PHI:486

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4295542

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004310701 – 501L-ornithine N(5)-monooxygenaseAdd BLAST501

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		746128.CADAFUBP00002315

<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

Secondary structure

1501
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		E9QYP0

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

More...SMRi		E9QYP0

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 31DisorderedSequence analysisAdd BLAST31
Regioni293 – 296Substrate binding1 Publication4
Regioni366 – 390DisorderedSequence analysisAdd BLAST25

<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 lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1399, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_020931_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		E9QYP0

Identification of Orthologs from Complete Genome Data

More...OMAi		YHGNTNY

Database of Orthologous Groups

More...OrthoDBi		1235295at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.50.50.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR025700, Lys/Orn_oxygenase

The PANTHER Classification System

More...PANTHERi		PTHR42802, PTHR42802, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13434, K_oxygenase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51905, SSF51905, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

E9QYP0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MESVERKSES SYLGMRNMQP EQRLSLDPPR LRSTPQDELH DLLCVGFGPA 
        60         70         80         90        100
SLAIAIALHD ALDPRLNKSA SNIHAQPKIC FLERQKQFAW HSGMLVPGSK 
       110        120        130        140        150
MQISFIKDLA TLRDPRSSFT FLNYLHQKGR LIHFTNLSTF LPARLEFEDY 
       160        170        180        190        200
MRWCAQQFSD VVAYGEEVVE VIPGKSDPSS SVVDFFTVRS RNVETGEISA 
       210        220        230        240        250
RRTRKVVIAI GGTAKMPSGL PQDPRIIHSS KYCTTLPALL KDKSKPYNIA 
       260        270        280        290        300
VLGSGQSAAE IFHDLQKRYP NSRTTLIMRD SAMRPSDDSP FVNEIFNPER 
       310        320        330        340        350
VDKFYSQSAA ERQRSLLADK ATNYSVVRLE LIEEIYNDMY LQRVKNPDET 
       360        370        380        390        400
QWQHRILPER KITRVEHHGP QSRMRIHLKS SKPESEGAAN DVKETLEVDA 
       410        420        430        440        450
LMVATGYNRN AHERLLSKVQ HLRPTGQDQW KPHRDYRVEM DPSKVSSEAG 
       460        470        480        490        500
IWLQGCNERT HGLSDSLLSV LAVRGGEMVQ SIFGEQLERA AVQGHQLRAM 

L
Length:501
Mass (Da):56,877
Last modified:April 5, 2011 - 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:iDD1D4DEDD2509506
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 57210 Da. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AY586511 Genomic DNA Translation: AAT84594.1
AY819708 Genomic DNA Translation: AAX40989.1
AAHF01000001 Genomic DNA Translation: EAL93065.1

NCBI Reference Sequences

More...RefSeqi		XP_755103.1, XM_750010.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		EAL93065; EAL93065; AFUA_2G07680

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3513640

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		afm:AFUA_2G07680

<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
AY586511 Genomic DNA Translation: AAT84594.1
AY819708 Genomic DNA Translation: AAX40989.1
AAHF01000001 Genomic DNA Translation: EAL93065.1
RefSeqiXP_755103.1, XM_750010.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B63X-ray1.90A1-501[»]
4B64X-ray2.28A1-501[»]
4B65X-ray2.32A1-501[»]
4B66X-ray2.90A1-501[»]
4B67X-ray2.75A1-501[»]
4B68X-ray2.29A1-501[»]
4B69X-ray2.30A1-501[»]
4NZHX-ray2.00A1-501[»]
5CKUX-ray2.10A1-501[»]
6X0HX-ray2.09A/B/C/D29-501[»]
6X0IX-ray1.95A/B/C/D1-501[»]
6X0JX-ray2.33A/B/C/D29-501[»]
6X0KX-ray2.23A/B/C/D/E/F/G/H29-501[»]
7JVKX-ray2.20A/B/C/D1-501[»]
7JVLX-ray2.10A/B/C/D1-501[»]
AlphaFoldDBiE9QYP0
SMRiE9QYP0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi746128.CADAFUBP00002315

Chemistry databases

ChEMBLiCHEMBL4295542

Genome annotation databases

EnsemblFungiiEAL93065; EAL93065; AFUA_2G07680
GeneIDi3513640
KEGGiafm:AFUA_2G07680

Organism-specific databases

VEuPathDBiFungiDB:Afu2g07680

Phylogenomic databases

eggNOGiKOG1399, Eukaryota
HOGENOMiCLU_020931_2_0_1
InParanoidiE9QYP0
OMAiYHGNTNY
OrthoDBi1235295at2759

Enzyme and pathway databases

UniPathwayiUPA00783
BRENDAi1.14.13.195, 508
1.14.13.196, 508

Miscellaneous databases

PHI-baseiPHI:377
PHI:486

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR025700, Lys/Orn_oxygenase
PANTHERiPTHR42802, PTHR42802, 1 hit
PfamiView protein in Pfam
PF13434, K_oxygenase, 1 hit
SUPFAMiSSF51905, SSF51905, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiSIDA_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: E9QYP0
Secondary accession number(s): Q4X250, Q5SE95
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 26, 2014
Last sequence update: April 5, 2011
Last modified: May 25, 2022
This is version 64 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

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again