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Protein

Acyl-CoA desaturase

Gene
N/A
Organism
Cyprinus carpio (Common carp)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Stearyl-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.By similarity

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.By similarity

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei42SubstrateBy similarity1
Metal bindingi87Iron 1By similarity1
Metal bindingi92Iron 1By similarity1
Binding sitei115SubstrateBy similarity1
Binding sitei122SubstrateBy similarity1
Binding sitei123SubstrateBy similarity1
Metal bindingi124Iron 1By similarity1
Metal bindingi127Iron 2By similarity1
Metal bindingi128Iron 1By similarity1
Binding sitei155SubstrateBy similarity1
Binding sitei156SubstrateBy similarity1
Binding sitei229SubstrateBy similarity1
Metal bindingi236Iron 2By similarity1
Metal bindingi265Iron 2By similarity1
Metal bindingi268Iron 1By similarity1
Metal bindingi269Iron 2By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Stress response

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.1By similarity)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase1 Publication
Fatty acid desaturase
Stearoyl-CoA desaturase
OrganismiCyprinus carpio (Common carp)
Taxonomic identifieri7962 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCyprinus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 39CytoplasmicBy similarityAdd BLAST39
Transmembranei40 – 60HelicalBy similarityAdd BLAST21
Topological domaini61 – 64LumenalBy similarity4
Transmembranei65 – 85HelicalBy similarityAdd BLAST21
Topological domaini86 – 184CytoplasmicBy similarityAdd BLAST99
Transmembranei185 – 204HelicalBy similarityAdd BLAST20
Topological domaini205 – 208LumenalBy similarity4
Transmembranei209 – 230HelicalBy similarityAdd BLAST22
Topological domaini231 – 327CytoplasmicBy similarityAdd BLAST97

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854031 – 327Acyl-CoA desaturaseAdd BLAST327

Expressioni

Inductioni

By cold. A 10-fold increase in transcript levels is observed 48-60 hours after cooling.1 Publication

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi87 – 92Histidine box-1Curated6
Motifi124 – 128Histidine box-2Curated5
Motifi265 – 269Histidine box-3Curated5

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003367.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDREIKSPI WHPEPGTVED VFDHTYKEKE GPKPPTVIVW RNVILMSLLH
60 70 80 90 100
LGALYGLFLF PSARALTWIW FFGCLLFSAL GITAGAHRLW SHRSYKASLP
110 120 130 140 150
LQIFLALGNS MAFQNDIYEW SRDHRVHHKY SETDADPHNA VRGFFFSHVG
160 170 180 190 200
WLLVRKHPDV IEKGRKLELS DLKADKVVMF QRRFYKPSVL LMCFFVPTFV
210 220 230 240 250
PWYVWGESLW VAYFVPALLR YALVLNATWL VNSAAHMWGN RPYDSSINPR
260 270 280 290 300
ENRFVTFSAI GEGFHNYHHT FPFDYATSEF GCKLNLTTCC FIDLMCFLGL
310 320
AREPKRVSRE AVLARAQRTG DGSHWSG
Length:327
Mass (Da):37,820
Last modified:May 1, 2000 - v2
Checksum:i3E794CB408D33089
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31864 mRNA. Translation: AAB03857.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31864 mRNA. Translation: AAB03857.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003367.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACOD_CYPCA
AccessioniPrimary (citable) accession number: Q92038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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.