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UniProtKB - Q12618 (ACO1_AJECA)

Entry version 97 (23 Feb 2022)
Sequence version 1 (01 Nov 1996)
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Protein

Acyl-CoA desaturase

Gene

OLE1

Organism
Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Status
Reviewed-Annotation score:

Annotation score:3 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

Stearoyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Has high specificity and catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides.

1 Publication

<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

Fe2+By similarityNote: Expected to bind 2 Fe2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi101Iron 1By similarity1
Metal bindingi106Iron 1By similarity1
Metal bindingi138Iron 1By similarity1
Metal bindingi141Iron 2By similarity1
Metal bindingi142Iron 1By similarity1
Metal bindingi246Iron 2By similarity1
Metal bindingi275Iron 2By similarity1
Metal bindingi278Iron 1By similarity1
Metal bindingi279Iron 2By similarity1
Metal bindingi384Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi410Iron (heme axial ligand)PROSITE-ProRule annotation1

<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 processElectron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport
LigandHeme, Iron, Metal-binding

<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-CoA desaturase (EC:1.14.19.11 Publication)
Alternative name(s):
Delta(9)-desaturaseCurated
Short name:
Delta-9 desaturaseCurated
Fatty acid desaturaseCurated
Stearoyl-CoA desaturaseCurated
<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:OLE11 Publication
<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>OrganismiAjellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
<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 identifieri5037 [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 › Onygenales › Ajellomycetaceae › Histoplasma

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 54CytoplasmicCuratedAdd BLAST54
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei55 – 75HelicalSequence analysisAdd BLAST21
Topological domaini76 – 80LumenalCurated5
Transmembranei81 – 101HelicalSequence analysisAdd BLAST21
Topological domaini102 – 110CytoplasmicCurated9
Transmembranei111 – 131HelicalSequence analysisAdd BLAST21
Topological domaini132 – 199LumenalCuratedAdd BLAST68
Transmembranei200 – 220HelicalSequence analysisAdd BLAST21
Topological domaini221 – 476CytoplasmicCuratedAdd BLAST256

Keywords - Cellular componenti

Membrane

<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_00001854041 – 476Acyl-CoA desaturaseAdd BLAST476

<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

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

More...SMRi		Q12618

Database of comparative protein structure models

More...ModBasei		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

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>Domaini349 – 427Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST79

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 – 35DisorderedSequence analysisAdd BLAST35

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>Motifi101 – 106Histidine box-1Curated6
Motifi138 – 142Histidine box-2Curated5
Motifi275 – 279Histidine box-3Curated5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The histidine box domains are involved in binding the catalytic metal ions.By similarity

<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 fatty acid desaturase type 1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...CDDi		cd03505, Delta9-FADS-like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.10.120.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009160, Acyl-CoA_deSatase_haem/ster-bd
IPR015876, Acyl-CoA_DS
IPR001199, Cyt_B5-like_heme/steroid-bd
IPR036400, Cyt_B5-like_heme/steroid_sf
IPR018506, Cyt_B5_heme-BS
IPR005804, FA_desaturase_dom
IPR001522, FADS-1_CS

The PANTHER Classification System

More...PANTHERi		PTHR11351, PTHR11351, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00173, Cyt-b5, 1 hit
PF00487, FA_desaturase, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000345, OLE1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00075, FACDDSATRASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01117, Cyt-b5, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55856, SSF55856, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00191, CYTOCHROME_B5_1, 1 hit
PS50255, CYTOCHROME_B5_2, 1 hit
PS00476, FATTY_ACID_DESATUR_1, 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.

Q12618-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALNEAPTAS PVAETAAGGK DVVTDAARRP NSEPKKVHIT DTPITLANWH 
        60         70         80         90        100
KHISWLNVTL IIAIPIYGLV QAYWVPLHLK TALWAVVYYF MTGLGITAGY 
       110        120        130        140        150
HRLWAHCSYS ATLPLKIYLA AVGGGAVEGS IRWWARGHRA HHRYTDTDKD 
       160        170        180        190        200
PYSVRKGLLY SHIGWMVMKQ NPKRIGRTEI TDLNEDPVVV WQHRNYLKVV 
       210        220        230        240        250
IFMGIVFPML VSGLGWGDWF GGFIYAGILR IFFVQQATFC VNSLAHWLGD 
       260        270        280        290        300
QPFDDRNSPR DHIVTALVTL GEGYHNFHHE FPSDYRNAIE WHQYDPTKWT 
       310        320        330        340        350
IWIWKQLGLA YDLKQFRANE IEKGRVQQLQ KKIDQRRAKL DWGIPLEQLP 
       360        370        380        390        400
VIEWDDYVDQ AKNGRGLIAI AGVVHDVTDF IKDHPGGKAM INSGIGKDAT 
       410        420        430        440        450
AMFNGGVYNH SNAAHNQLST MRVGVIRGGC EVEIWKRAQK ENKEVESVRD 
       460        470 
EYGNRIVRAG AQVTKIPEPI TTADAA
Length:476
Mass (Da):53,791
Last modified:November 1, 1996 - 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:iA91A9CE2A865CADB
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
X85963 Genomic DNA Translation: CAA59939.1

<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
X85963 Genomic DNA Translation: CAA59939.1

3D structure databases

SMRiQ12618
ModBaseiSearch...

Family and domain databases

CDDicd03505, Delta9-FADS-like, 1 hit
Gene3Di3.10.120.10, 1 hit
InterProiView protein in InterPro
IPR009160, Acyl-CoA_deSatase_haem/ster-bd
IPR015876, Acyl-CoA_DS
IPR001199, Cyt_B5-like_heme/steroid-bd
IPR036400, Cyt_B5-like_heme/steroid_sf
IPR018506, Cyt_B5_heme-BS
IPR005804, FA_desaturase_dom
IPR001522, FADS-1_CS
PANTHERiPTHR11351, PTHR11351, 1 hit
PfamiView protein in Pfam
PF00173, Cyt-b5, 1 hit
PF00487, FA_desaturase, 1 hit
PIRSFiPIRSF000345, OLE1, 1 hit
PRINTSiPR00075, FACDDSATRASE
SMARTiView protein in SMART
SM01117, Cyt-b5, 1 hit
SUPFAMiSSF55856, SSF55856, 1 hit
PROSITEiView protein in PROSITE
PS00191, CYTOCHROME_B5_1, 1 hit
PS50255, CYTOCHROME_B5_2, 1 hit
PS00476, FATTY_ACID_DESATUR_1, 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 nameiACO1_AJECA
<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: Q12618
<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 13, 2004
Last sequence update: November 1, 1996
Last modified: February 23, 2022
This is version 97 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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