ID   ACO11_CHORO             Reviewed;         335 AA.
AC   Q8ISS3; D8L7A5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Acyl-CoA Delta(11) desaturase;
DE            EC=1.14.19.5 {ECO:0000269|PubMed:15455060};
DE   AltName: Full=Acyl-CoA Delta-11 desaturase;
DE            Short=Delta(11)-desaturase;
DE   AltName: Full=Acyl-CoA Z/E11 desaturase;
OS   Choristoneura rosaceana (Oblique banded leafroller).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tortricoidea;
OC   Tortricidae; Tortricinae; Choristoneura.
OX   NCBI_TaxID=27543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Pheromone gland;
RX   PubMed=15455060; DOI=10.1093/jis/2.1.26;
RA   Hao G., O'Connor M., Liu W., Roelofs W.L.;
RT   "Characterization of Z/E11- and Z9-desaturases from the obliquebanded
RT   leafroller moth, Choristoneura rosaceana.";
RL   J. Insect Sci. 2:26-26(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-335.
RA   Xue B., Roelofs W.L., Rooney A.P.;
RT   "Analysis of transcriptional profile and genomic organization of desaturase
RT   genes in moths.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of Delta(11) fatty acyl precursors in
CC       the pheromone gland, with a preference for myristic acid.
CC       {ECO:0000269|PubMed:15455060}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an 11,12-saturated fatty acyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC         2 H(+) + O2 = an (11Z)-Delta(11)-fatty acyl-CoA + 2 Fe(III)-
CC         [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:25852, Rhea:RHEA-COMP:10438,
CC         Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:84947, ChEBI:CHEBI:84948; EC=1.14.19.5;
CC         Evidence={ECO:0000269|PubMed:15455060};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in pheromone gland.
CC       {ECO:0000269|PubMed:15455060}.
CC   -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC       involved in metal ion binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF545481; AAN41250.1; -; mRNA.
DR   EMBL; FJ999625; ADC53485.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ISS3; -.
DR   SMR; Q8ISS3; -.
DR   BRENDA; 1.14.19.24; 7754.
DR   BRENDA; 1.14.19.5; 7754.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017105; F:acyl-CoA delta11-desaturase activity; IMP:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050601; F:myristoyl-CoA 11-(Z) desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0042811; P:pheromone biosynthetic process; IMP:UniProtKB.
DR   CDD; cd03505; Delta9-FADS-like; 1.
DR   InterPro; IPR015876; Acyl-CoA_DS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR001522; FADS-1_CS.
DR   PANTHER; PTHR11351; PTHR11351; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PRINTS; PR00075; FACDDSATRASE.
DR   PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE   1: Evidence at protein level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Metal-binding; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..335
FT                   /note="Acyl-CoA Delta(11) desaturase"
FT                   /id="PRO_0000418990"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          312..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           84..89
FT                   /note="Histidine box-1"
FT   MOTIF           121..125
FT                   /note="Histidine box-2"
FT   MOTIF           261..265
FT                   /note="Histidine box-3"
FT   COMPBIAS        320..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  38785 MW;  7DABB4EF770183F6 CRC64;
     MAPNVEDMES DLPESEEKLE KLVAPQAAPR KYQIIYTNLL TFGYWHIAGL YGLYLCFTSA
     KWQTIILALI LNEMAILGIT AGAHRLWAHR SYKATVPLQI ILIIFNSLSF QNSAIHWIRD
     HRMHHKYSDT DGDPHNASRG FFYSHVGWLL VKKHPEVKKR AKTIDMSDIY SNPILRFQKK
     YAIPFIGMIC FVLPTIIPMY FWGETLSNAW HITMLRYVFS LNSIFLVNSA AHLYGYRPYD
     KNILPAENKM TFIACLGENF HNYHHVFPWD YRASELGNIG MNWTAKFIDF FAWIGWAYDL
     KTASDENIKS RMKRTGDGTD VSGQKYSCES SEVLQ