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UniProtKB - O62137 (ACX12_CAEEL)

Entry version 153 (29 Sep 2021)
Sequence version 2 (10 Feb 2009)
Previous versions | rss
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Protein

Acyl-coenzyme A oxidase acox-1.2

Gene

acox-1.2

Organism
Caenorhabditis elegans
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

Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior (PubMed:25775534, PubMed:27551084).

Specifically, shortens ascarosides with 5-carbon omega side chain (asc-omega-C5) (PubMed:25775534, PubMed:27551084).

Does not shorten indol-3-carbonyl(IC)-ascaroside with 7-carbon or 9-carbon side chains (PubMed:29863473).

Does not catalyze the desaturation of fatty acids or hydroxylated fatty acids (PubMed:25775534, PubMed:27551084).

3 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

FAD1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by ATP (PubMed:27551084). ATP binding leads to a conformational change that promotes FAD cofactor binding and enzyme activity (PubMed:27551084). ATP binding likely occurs during acox-1.2 folding and/or dimer formation (PubMed:27551084). The preference for processing substrates with shorter fatty acid chains is likely due to the closed conformation of the active site (PubMed:27551084).1 Publication

<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 364 sec(-1) with asc-omega-C5-CoA (at 30 degrees Celsius and pH 7.4) (PubMed:25775534). kcat is 478 sec(-1) with asc-omega-C5-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.1) (PubMed:25775534).1 Publication
  1. KM=175 µM for asc-omega-C5-CoA (at 30 degrees Celsius and pH 7.4)1 Publication
  2. KM=152 µM for asc-omega-C5-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.1)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: peroxisomal fatty acid beta-oxidation

This protein is involved in the pathway peroxisomal fatty acid beta-oxidation, which is part of Lipid metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway peroxisomal fatty acid beta-oxidation and in Lipid metabolism.

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 sitei189FAD; via amide nitrogenUniRule annotationCombined sources1 Publication1
Binding sitei293SubstrateCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei299Important for asc-omega-C5-CoA binding and thus substrate specificity1 PublicationImported1
Binding sitei318FAD; shared with dimeric partnerCombined sources1 Publication1
Binding sitei340ATP; via tele nitrogen; shared with dimeric partnerCombined sources1 Publication1
Binding sitei390ATP; via carbonyl oxygenBy similarity1
Binding sitei394ATPBy similarity1
Binding sitei402ATP; shared with dimeric partnerCombined sources1 Publication1
Binding sitei409FAD; via amide nitrogen; shared with dimeric partnerCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei432Proton acceptorUniRule annotation1
Binding sitei434FADCombined sources1 Publication1
Binding sitei573ATPCombined sources1 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 bindingi147 – 150FADCombined sources1 Publication4
Nucleotide bindingi155 – 156FADCombined sources1 Publication2
Nucleotide bindingi338 – 341FAD; shared with dimeric partnerCombined sources1 Publication4
Nucleotide bindingi525 – 528ATPCombined sources1 Publication4

<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 functionOxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandATP-binding, FAD, Flavoprotein, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.3.3.6, 1045

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-CEL-193368, Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-CEL-389887, Beta-oxidation of pristanoyl-CoA
R-CEL-9033241, Peroxisomal protein import

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

More...UniPathwayi		UPA00661

<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:
Acyl-coenzyme A oxidase acox-1.2Curated (EC:1.3.3.-2 Publications)
<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:acox-1.2Imported
Synonyms:acox-2Imported
ORF Names:F08A8.2Imported
<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>OrganismiCaenorhabditis elegansImported
<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 identifieri6239 [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 › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditina › Rhabditomorpha › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis
<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
  • UP000001940 <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 I

Organism-specific databases

WormBase

More...WormBasei		F08A8.2 ; CE43421 ; WBGene00008565 ; acox-1.2

<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

Keywords - Cellular componenti

Peroxisome

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi432E → A: Increases ATP and FAD binding. 1 Publication1
Mutagenesisi496 – 661Missing in gk386052; increases production of asc-omega-C5 and reduces the production of asc-omega-C3. 1 PublicationAdd BLAST166

<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_00004523031 – 661Acyl-coenzyme A oxidase acox-1.2Add BLAST661

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O62137

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O62137

PeptideAtlas

More...PeptideAtlasi		O62137

<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

Induced by high temperatures (25 degrees Celsius) (PubMed:25775534). Down-regulated in dauer conditions (PubMed:25775534).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		WBGene00008565, Expressed in multi-cellular organism and 3 other tissues

<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

Homodimer (Probable) (PubMed:27551084).

Forms a heterodimer with acox-1.1 (PubMed:25775534).

1 Publication2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		6239.F08A8.2

<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

1661
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		O62137

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>Regioni283 – 286Substrate bindingCombined sources1 Publication4
Regioni431 – 432Substrate bindingCombined sources1 Publication2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi659 – 661Microbody targeting signalSequence analysis3

<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 acyl-CoA oxidase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0136, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000168827

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_014629_3_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O62137

Identification of Orthologs from Complete Genome Data

More...OMAi		TKWWIGA

Database of Orthologous Groups

More...OrthoDBi		416859at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O62137

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.540.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029320, Acyl-CoA_ox_N
IPR006091, Acyl-CoA_Oxase/DH_cen-dom
IPR012258, Acyl-CoA_oxidase
IPR002655, Acyl-CoA_oxidase_C
IPR036250, AcylCo_DH-like_C
IPR037069, AcylCoA_DH/ox_N_sf
IPR009100, AcylCoA_DH/oxidase_NM_dom

The PANTHER Classification System

More...PANTHERi		PTHR10909, PTHR10909, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01756, ACOX, 1 hit
PF02770, Acyl-CoA_dh_M, 1 hit
PF14749, Acyl-CoA_ox_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000168, Acyl-CoA_oxidase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47203, SSF47203, 2 hits
SSF56645, SSF56645, 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.

O62137-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANRSIRDGD NPELLEERRM ATFDTDKMAA VIYGSEEFAR RRREITDAVS 
        60         70         80         90        100
KIPELADIKP YPFLTREEKV TEGTRKISIL TKYLNQLIDR DNEEESLHLH 
       110        120        130        140        150
REVIGYEGHP FALHDALFIP TLQSQASDEQ QEKWLERARR REIIGCYAQT 
       160        170        180        190        200
ELGHGSNLRN LETTAVYDIA SQEFVLHTPT TTALKWWPGA LGKSCNYALV 
       210        220        230        240        250
VAELIIKRNN YGPHFFMVQL RDEKTHIPLK GVTVGDIGPK MNFNAADNGY 
       260        270        280        290        300
LGLNNLRVPR TNLLMRHCKV EADGTYVKPP HAKIGYSGMV KIRSQMAMEQ 
       310        320        330        340        350
GLFLAHALTI AARYSAVRRQ GHLDDKQVEV KVLDYQTQQH RLFPSLARAY 
       360        370        380        390        400
AFIFTGFETI HLYSQLLKDV DMGNTSGMAD LHALTSGLKS VVAHETGEGI 
       410        420        430        440        450
EQARMACGGH GYSMASYISV VYGIAIGGCT YEGENMVMLL QLARYLVKSV 
       460        470        480        490        500
ELIKAGKAKK LGPVASYLAD KSDETDLTSL NGYVKMFENM ARRQAWKATE 
       510        520        530        540        550
KFLKLMESGE SREVAWNKSA VELTRASRLH TRLFIIEAFM RRVSRIEDIP 
       560        570        580        590        600
VKEVLTDLLH LHVNYELLDV ATYALEFMSF TQLDYVRDQL YLYLEKIRPN 
       610        620        630        640        650
AVSLVDSFQI SDMQLRSVLG RRDGHVYENL FKWAKSSPLN NADVLPSVEK 
       660 
YLKPMMEKAK L
Length:661
Mass (Da):75,091
Last modified:February 10, 2009 - v2
<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:iEF005188A6A87472
GO

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
BX284601 Genomic DNA Translation: CAB16864.2

NCBI Reference Sequences

More...RefSeqi		NP_493262.2, NM_060861.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		F08A8.2.1; F08A8.2.1; WBGene00008565

Database of genes from NCBI RefSeq genomes

More...GeneIDi		173163

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cel:CELE_F08A8.2

UCSC genome browser

More...UCSCi		F08A8.2, c. elegans

<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
BX284601 Genomic DNA Translation: CAB16864.2
RefSeqiNP_493262.2, NM_060861.3

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
5K3JX-ray2.68A/B1-661[»]
SMRiO62137
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi6239.F08A8.2

Proteomic databases

EPDiO62137
PaxDbiO62137
PeptideAtlasiO62137

Genome annotation databases

EnsemblMetazoaiF08A8.2.1; F08A8.2.1; WBGene00008565
GeneIDi173163
KEGGicel:CELE_F08A8.2
UCSCiF08A8.2, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		173163
WormBaseiF08A8.2 ; CE43421 ; WBGene00008565 ; acox-1.2

Phylogenomic databases

eggNOGiKOG0136, Eukaryota
GeneTreeiENSGT00940000168827
HOGENOMiCLU_014629_3_1_1
InParanoidiO62137
OMAiTKWWIGA
OrthoDBi416859at2759
PhylomeDBiO62137

Enzyme and pathway databases

UniPathwayiUPA00661
BRENDAi1.3.3.6, 1045
ReactomeiR-CEL-193368, Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-CEL-389887, Beta-oxidation of pristanoyl-CoA
R-CEL-9033241, Peroxisomal protein import

Gene expression databases

BgeeiWBGene00008565, Expressed in multi-cellular organism and 3 other tissues

Family and domain databases

Gene3Di1.10.540.10, 1 hit
InterProiView protein in InterPro
IPR029320, Acyl-CoA_ox_N
IPR006091, Acyl-CoA_Oxase/DH_cen-dom
IPR012258, Acyl-CoA_oxidase
IPR002655, Acyl-CoA_oxidase_C
IPR036250, AcylCo_DH-like_C
IPR037069, AcylCoA_DH/ox_N_sf
IPR009100, AcylCoA_DH/oxidase_NM_dom
PANTHERiPTHR10909, PTHR10909, 1 hit
PfamiView protein in Pfam
PF01756, ACOX, 1 hit
PF02770, Acyl-CoA_dh_M, 1 hit
PF14749, Acyl-CoA_ox_N, 1 hit
PIRSFiPIRSF000168, Acyl-CoA_oxidase, 1 hit
SUPFAMiSSF47203, SSF47203, 2 hits
SSF56645, SSF56645, 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 nameiACX12_CAEEL
<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: O62137
<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: April 7, 2021
Last sequence update: February 10, 2009
Last modified: September 29, 2021
This is version 153 of the entry and version 2 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 programCaenorhabditis annotation project

<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. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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