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Protein

Acyl-lipid (8-3)-desaturase

Gene

DES1

Organism
Mortierella alpina (Oleaginous fungus) (Mortierella renispora)
Status
Reviewed-Annotation score: -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
An (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O.1 Publication

Cofactori

Fe2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi41Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi64Iron (heme axial ligand)PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19037

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 sedisMucoromycotaMortierellomycotinaMortierellalesMortierellaceaeMortierella

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Transmembranei150 – 170HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854091 – 446Acyl-lipid (8-3)-desaturaseAdd BLAST446

Proteomic databases

PRIDEiO74212

Structurei

3D structure databases

ProteinModelPortaliO74212
SMRiO74212
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 82Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST77

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi171 – 175Histidine box-15
Motifi207 – 212Histidine box-26
Motifi387 – 391Histidine box-35

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.10.120.10, 1 hit
InterProiView protein in InterPro
IPR001199 Cyt_B5-like_heme/steroid-bd
IPR036400 Cyt_B5-like_heme/steroid_sf
IPR018506 Cyt_B5_heme-BS
IPR005804 FA_desaturase_dom
IPR012171 Fatty_acid_desaturase
PfamiView protein in Pfam
PF00173 Cyt-b5, 1 hit
PF00487 FA_desaturase, 1 hit
PIRSFiPIRSF015921 FA_sphinglp_des, 1 hit
PRINTSiPR00363 CYTOCHROMEB5
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

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)DescriptionActionsGraphical viewLength
Natural varianti21G → D in strain: ATCC 32221. 1
Natural varianti88V → I in strain: ATCC 32221. 1
Natural varianti111D → N in strain: ATCC 32221. 1
Natural varianti227F → S in strain: ATCC 32221. 1
Natural varianti248D → H in strain: ATCC 32221. 1

Sequence databases

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

Similar proteinsi

Entry informationi

Entry nameiD5FAD_MORAP
AccessioniPrimary (citable) accession number: O74212
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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