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Protein

Acyl-lipid (8-3)-desaturase

Gene

DES1

Organism
Mortierella alpina (Oleaginous fungus) (Mortierella renispora)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Fatty acid desaturase that introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta8 double bond. Involved in the conversion of di-homo-Delta-linolenic acid to arachidonic acid. Essential in the production of eicosanoids.2 Publications

Catalytic activityi

An (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (5Z,8Z,11Z,14Z)-icosatetra-5,8,11,14-tetraenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O.1 Publication

Cofactori

Fe2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi64 – 641Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-lipid (8-3)-desaturase (EC:1.14.19.301 Publication)
Alternative name(s):
Delta(5) fatty acid desaturase1 Publication
Short name:
Delta-5 fatty acid desaturase1 Publication
Gene namesi
Name:DES1
OrganismiMortierella alpina (Oleaginous fungus) (Mortierella renispora)
Taxonomic identifieri64518 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisMortierellomycotinaMortierellalesMortierellaceaeMortierella

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Transmembranei150 – 17021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Acyl-lipid (8-3)-desaturasePRO_0000185409Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO74212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8277Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi171 – 1755Histidine box-1
Motifi207 – 2126Histidine box-2
Motifi387 – 3915Histidine box-3

Domaini

The cytochrome b5 heme-binding domain acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.Curated

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR012171. Fatty_acid_desaturase.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74212-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTDQGKTFT WEELAAHNTK GDLFLAIRGR VYDVTKFLSR HPGGVDTLLL
60 70 80 90 100
GAGRDVTPVF EMYHAFGAAD AIMKKYYVGT LVSNELPVFP EPTVFHKTIK
110 120 130 140 150
TRVEGYFTDR DIDPKNRPEI WGRYALIFGS LIASYYAQLF VPFVVERTWL
160 170 180 190 200
QVVFAIIMGF ACAQVGLNPL HDASHFSVTH NPTVWKILGA THDFFNGASY
210 220 230 240 250
LVWMYQHMLG HHPYTNIAGA DPDVSTFEPD VRRIKPNQKW FVNHINQDMF
260 270 280 290 300
VPFLYGLLAF KVRIQDINIL YFVKTNDAIR VNPISTWHTV MFWGGKAFFV
310 320 330 340 350
WYRLIVPLQY LPLGKVLLLF TVADMVSSYW LALTFQANHV VEEVQWPLPD
360 370 380 390 400
ENGIIQKDWA AMQVETTQDY AHDSHLWTSI TGSLNYQAVH HLFPNVSQHH
410 420 430 440
YPDILAIIKN TCSEYKVPYL VKDTFWQAFA SHLEHLRVLG LRPKEE
Length:446
Mass (Da):51,288
Last modified:November 1, 1998 - v1
Checksum:i8395741C5A3CC9A2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211G → D in strain: ATCC 32221.
Natural varianti88 – 881V → I in strain: ATCC 32221.
Natural varianti111 – 1111D → N in strain: ATCC 32221.
Natural varianti227 – 2271F → S in strain: ATCC 32221.
Natural varianti248 – 2481D → H in strain: ATCC 32221.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054824 mRNA. Translation: AAC39508.1.
AF067654 mRNA. Translation: AAC72755.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054824 mRNA. Translation: AAC39508.1.
AF067654 mRNA. Translation: AAC72755.1.

3D structure databases

ProteinModelPortaliO74212.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR012171. Fatty_acid_desaturase.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiD5FAD_MORAP
AccessioniPrimary (citable) accession number: O74212
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1998
Last modified: September 7, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.