Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 163 (17 Jun 2020)
Sequence version 1 (01 May 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Peroxisomal multifunctional enzyme type 2

Gene

Mfe2

Organism
Drosophila melanogaster (Fruit fly)
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

Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids.1 Publication

Miscellaneous

Complements functionally the S.cerevisiae peroxisomal MFE-2 in vivo.

<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 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

Catalytic efficiency is similar using full-length protein or the individual (3R)-hydroxyacyl-CoA dehydrogenase and enoyl-CoA hydratase 2 domains in a 1:1 mixture.1 Publication
  1. KM=85.3 µM for (2E)-butenoyl-CoA (at 22 degrees Celsius)1 Publication
  2. KM=66.7 µM for (2E)-hexenoyl-CoA (at 22 degrees Celsius)1 Publication
  3. KM=31.4 µM for (2E)-decenoyl-CoA (at 22 degrees Celsius)1 Publication
  1. Vmax=1.07 µmol/min/mg enzyme with (2E)-butenoyl-CoA (at 22 degrees Celsius)1 Publication
  2. Vmax=15.0 µmol/min/mg enzyme with (2E)-hexenoyl-CoA (at 22 degrees Celsius)1 Publication
  3. Vmax=31.4 µmol/min/mg enzyme with (2E)-decenoyl-CoA (at 22 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: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway 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 sitei24NAD; via amide nitrogenBy similarity1
Binding sitei43NADBy similarity1
Binding sitei102NAD; via carbonyl oxygenBy similarity1
Binding sitei154SubstrateBy similarity1
<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 sitei167Proton acceptorPROSITE-ProRule annotationBy similarity1
Binding sitei419(3R)-3-hydroxydecanoyl-CoABy similarity1
Binding sitei519(3R)-3-hydroxydecanoyl-CoA; via amide nitrogenBy similarity1
Binding sitei549(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygenBy similarity1

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 bindingi16 – 40NADBy similarityAdd BLAST25
Nucleotide bindingi78 – 79NADBy similarity2
Nucleotide bindingi167 – 171NADBy similarity5
Nucleotide bindingi199 – 202NADBy similarity4

<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

GO - Biological processi

  • fatty acid beta-oxidation using acyl-CoA oxidase Source: FlyBase

<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 functionLyase, Multifunctional enzyme, Oxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandNAD

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-193368 Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-DME-2046106 alpha-linolenic acid (ALA) metabolism
R-DME-389887 Beta-oxidation of pristanoyl-CoA
R-DME-390247 Beta-oxidation of very long chain fatty acids
R-DME-9033241 Peroxisomal protein import

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

More...
UniPathwayi
UPA00659

<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:
Peroxisomal multifunctional enzyme type 21 Publication
Short name:
DmMFE-21 Publication
Including the following 2 domains:
(3R)-hydroxyacyl-CoA dehydrogenase1 Publication (EC:1.1.1.n121 Publication)
Enoyl-CoA hydratase 21 Publication (EC:4.2.1.1191 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:Mfe2Imported
ORF Names:CG3415
<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>OrganismiDrosophila melanogaster (Fruit fly)
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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
  • UP000000803 <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 X

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0030731 Mfe2

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Peroxisome

<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_00004169351 – 598Peroxisomal multifunctional enzyme type 2Add BLAST598

Proteomic databases

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

More...
PaxDbi
Q9VXJ0

PRoteomics IDEntifications database

More...
PRIDEi
Q9VXJ0

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0030731 Expressed in midgut and 32 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9VXJ0 differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9VXJ0 DM

<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.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
58924, 11 interactors

Protein interaction database and analysis system

More...
IntActi
Q9VXJ0, 4 interactors

Molecular INTeraction database

More...
MINTi
Q9VXJ0

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0073988

<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

1598
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
Q9VXJ0

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9VXJ0

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini469 – 586MaoC-likeSequence analysisAdd BLAST118

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 – 309(3R)-hydroxyacyl-CoA dehydrogenase1 PublicationAdd BLAST309
Regioni310 – 598Enoyl-CoA hydratase 21 PublicationAdd BLAST289
Regioni390 – 391(3R)-3-hydroxydecanoyl-CoA bindingBy similarity2
Regioni496 – 501(3R)-3-hydroxydecanoyl-CoA bindingBy similarity6

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>Motifi596 – 598Microbody 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1206 Eukaryota
COG2030 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_010194_18_4_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9VXJ0

KEGG Orthology (KO)

More...
KOi
K12405

Identification of Orthologs from Complete Genome Data

More...
OMAi
CTQAAFP

Database of Orthologous Groups

More...
OrthoDBi
1120431at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9VXJ0

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029069 HotDog_dom_sf
IPR039569 MaoC-like_dehydrat_N
IPR002539 MaoC-like_dom
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00106 adh_short, 1 hit
PF13452 MaoC_dehydrat_N, 1 hit
PF01575 MaoC_dehydratas, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00081 GDHRDH
PR00080 SDRFAMILY

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit
SSF54637 SSF54637, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00061 ADH_SHORT, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9VXJ0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSSDGKLRY DGRVAVVTGA GAGLGREYAL LFAERGAKVV VNDLGGTHSG
60 70 80 90 100
DGASQRAADI VVDEIRKAGG EAVADYNSVI DGAKVIETAI KAFGRVDILV
110 120 130 140 150
NNAGILRDRS LVKTSEQDWN LVNDVHLKGS FKCTQAAFPY MKKQNYGRII
160 170 180 190 200
MTSSNSGIYG NFGQVNYTAA KMGLIGLANT VAIEGARNNV LCNVIVPTAA
210 220 230 240 250
SRMTEGILPD ILFNELKPKL IAPVVAYLCH ESCEDNGSYI ESAAGWATKL
260 270 280 290 300
HMVRGKGAVL RPSLDDPVTI EYVKDVWSNV TDMSKAKHLG AIAEASGTLL
310 320 330 340 350
EVLEKLKEGG GDAIEDAFEF NSKELITYAL GIGASVKNAK DMRFLYENDA
360 370 380 390 400
DFAAIPTFFV LPGLLLQMST DKLLSKALPN SQVDFSNILH GEQYLEIVDD
410 420 430 440 450
LPTSGTLLTN GKVFDVMDKG SGAVVVTNSE SFDESGRLLV RNQSTTFIVG
460 470 480 490 500
AGKFGGKKDP IAGVVPLQPA PNRQPDATVQ YTTSEDQAAL YRLSGDKNPL
510 520 530 540 550
HIDPQMALLA GFKTPILHGL CTLGFSVRAV LAQFADNNPA LFKAVKVRFS
560 570 580 590
GPVIPGQTLR VDLWKQGTRI NFRTVVVETG KEVISGAYVD LKSSQAKL
Length:598
Mass (Da):64,073
Last modified:May 1, 2000 - 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:i24205DE78964319A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
X2JFD6X2JFD6_DROME
Peroxisomal multifunctional enzyme ...
Mfe2 Dmel\CG3415, DmMFE-2, MFE-2, CG3415, Dmel_CG3415
598Annotation score:

Annotation score:2 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>

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
AE014298 Genomic DNA Translation: AAF48572.1
AY051493 mRNA Translation: AAK92917.1

NCBI Reference Sequences

More...
RefSeqi
NP_001285318.1, NM_001298389.1
NP_573109.1, NM_132881.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0074209; FBpp0073988; FBgn0030731
FBtr0340442; FBpp0309384; FBgn0030731

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
32582

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG3415

UCSC genome browser

More...
UCSCi
CG3415-RA d. melanogaster

<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
AE014298 Genomic DNA Translation: AAF48572.1
AY051493 mRNA Translation: AAK92917.1
RefSeqiNP_001285318.1, NM_001298389.1
NP_573109.1, NM_132881.3

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
3OMLX-ray2.15A1-598[»]
SMRiQ9VXJ0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi58924, 11 interactors
IntActiQ9VXJ0, 4 interactors
MINTiQ9VXJ0
STRINGi7227.FBpp0073988

Proteomic databases

PaxDbiQ9VXJ0
PRIDEiQ9VXJ0

Genome annotation databases

EnsemblMetazoaiFBtr0074209; FBpp0073988; FBgn0030731
FBtr0340442; FBpp0309384; FBgn0030731
GeneIDi32582
KEGGidme:Dmel_CG3415
UCSCiCG3415-RA d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
32582
FlyBaseiFBgn0030731 Mfe2

Phylogenomic databases

eggNOGiKOG1206 Eukaryota
COG2030 LUCA
HOGENOMiCLU_010194_18_4_1
InParanoidiQ9VXJ0
KOiK12405
OMAiCTQAAFP
OrthoDBi1120431at2759
PhylomeDBiQ9VXJ0

Enzyme and pathway databases

UniPathwayiUPA00659
ReactomeiR-DME-193368 Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-DME-2046106 alpha-linolenic acid (ALA) metabolism
R-DME-389887 Beta-oxidation of pristanoyl-CoA
R-DME-390247 Beta-oxidation of very long chain fatty acids
R-DME-9033241 Peroxisomal protein import

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
32582 0 hits in 1 CRISPR screen
EvolutionaryTraceiQ9VXJ0

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
32582

Protein Ontology

More...
PROi
PR:Q9VXJ0

Gene expression databases

BgeeiFBgn0030731 Expressed in midgut and 32 other tissues
ExpressionAtlasiQ9VXJ0 differential
GenevisibleiQ9VXJ0 DM

Family and domain databases

InterProiView protein in InterPro
IPR029069 HotDog_dom_sf
IPR039569 MaoC-like_dehydrat_N
IPR002539 MaoC-like_dom
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PfamiView protein in Pfam
PF00106 adh_short, 1 hit
PF13452 MaoC_dehydrat_N, 1 hit
PF01575 MaoC_dehydratas, 1 hit
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
SSF54637 SSF54637, 2 hits
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiDHB4_DROME
<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: Q9VXJ0
<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 18, 2012
Last sequence update: May 1, 2000
Last modified: June 17, 2020
This is version 163 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 programDrosophila 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. 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
  4. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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