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Protein

(11Z)-hexadec-11-enoyl-CoA conjugase

Gene

desat1

Organism
Bombyx mori (Silk moth)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Fatty acid desaturase that catalyzes 2 consecutive steps in the biosynthesis of bombykol, a sex pheromone produced by the moth. First acts as an acyl-CoA Delta(11) desaturase (1) by catalyzing the formation of Delta(11) fatty acyl precursors. Then acts as a (11Z)-hexadec-11-enoyl-CoA conjugase (2) by converting a single cis double bond at position 11 of (11Z)-hexadec-11-enoyl-CoA into conjugated 10 trans and 12 cis double bonds.1 Publication

Catalytic activityi

An acyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = an (11Z)-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O.1 Publication
(11Z)-hexadec-11-enoyl-CoA + reduced acceptor + O2 = (10E,12Z)-hexadeca-10,12-dienoyl-CoA + acceptor + 2 H2O.1 Publication

Cofactori

Fe2+By similarity

GO - Molecular functioni

GO - Biological processi

  • fatty acid biosynthetic process Source: UniProtKB
  • pheromone biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandIron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18415.

Names & Taxonomyi

Protein namesi
Recommended name:
(11Z)-hexadec-11-enoyl-CoA conjugase (EC:1.14.19.151 Publication)
Short name:
Bmpgdesat11 Publication
Alternative name(s):
Acyl-CoA Delta(11) desaturase (EC:1.14.19.51 Publication)
Acyl-CoA Z11/delta10,12 desaturaseImported
Gene namesi
Name:desat11 Publication
ORF Names:BGIBMGA0115631 Publication
OrganismiBombyx mori (Silk moth)
Taxonomic identifieri7091 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
Proteomesi
  • UP000005204 Componenti: Unassembled WGS sequence

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei37 – 57HelicalSequence analysisAdd BLAST21
Transmembranei65 – 85HelicalSequence analysisAdd BLAST21
Transmembranei101 – 121HelicalSequence analysisAdd BLAST21
Transmembranei185 – 205HelicalSequence analysisAdd BLAST21
Transmembranei216 – 238HelicalSequence analysisAdd BLAST23

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004347341 – 330(11Z)-hexadec-11-enoyl-CoA conjugaseAdd BLAST330

Expressioni

Tissue specificityi

Highly expressed in the pheromone gland.1 Publication

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi87 – 92Histidine box-1Curated6
Motifi124 – 128Histidine box-2Curated5
Motifi264 – 268Histidine box-3Curated5

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.Curated

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiH9JPV8.
KOiK21709.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiView protein in InterPro
IPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiView protein in Pfam
PF00487. FA_desaturase. 1 hit.
PRINTSiPR00075. FACDDSATRASE.
PROSITEiView protein in PROSITE
PS00476. FATTY_ACID_DESATUR_1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q75PL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPNSVDKTN ETEYLKDNHV DYEKLIAPQA SPIKHKIVVM NVIRFSYLHI
60 70 80 90 100
AGLYGLYLCF TSAKLATSVF AIVLFFLGNF GITAGAHRLW SHNGYKVKLP
110 120 130 140 150
LEILLMVFNS IAFQNTIFTW VRDHRLHHKY TDTDADPHNA TRGFFFSHIG
160 170 180 190 200
WLLVRKHPMV KIAGKSLDMS DIYCNPLLRF QKKYAIPFIG TICFIIPTLA
210 220 230 240 250
PMYFWGESLN NAWHITVLRY IFSLNGTFLV NSAAHLWGYK PYDKSLKATQ
260 270 280 290 300
SGMANAFTFG EGFHNYHHVF PWDYRADELG DRYINLTTRF IDFFAWMGWA
310 320 330
YDLKTASTNI IEKRALRTGD GTYKRPNGMN
Length:330
Mass (Da):38,077
Last modified:July 5, 2004 - v1
Checksum:i1A56524DC6C88B1C
GO

Sequence cautioni

The sequence BABH01015400 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti105L → I in AAF80355 (PubMed:10767556).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157627 mRNA. Translation: AAF80355.1.
AB166851 mRNA. Translation: BAD18122.1.
BABH01015400 Genomic DNA. No translation available.
RefSeqiNP_001037017.2. NM_001043552.2.
UniGeneiBmo.368.

Genome annotation databases

GeneIDi692567.
KEGGibmor:692567.

Similar proteinsi

Entry informationi

Entry nameiDESAT_BOMMO
AccessioniPrimary (citable) accession number: Q75PL7
Secondary accession number(s): H9JPV8, Q9NDH3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 11, 2015
Last sequence update: July 5, 2004
Last modified: September 27, 2017
This is version 60 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families