ACO11_SPOLI
ID ACO11_SPOLI Reviewed; 338 AA.
AC Q6US81;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Acyl-CoA Delta(11) desaturase;
DE EC=1.14.19.5 {ECO:0000269|PubMed:15544945};
DE AltName: Full=Acyl-CoA Delta-11 desaturase;
DE Short=Delta(11)-desaturase;
DE AltName: Full=SlsZ/E11;
OS Spodoptera littoralis (Egyptian cotton leafworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7109;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pheromone gland;
RX PubMed=15544945; DOI=10.1016/j.ibmb.2004.09.003;
RA Rodriguez S., Hao G., Liu W., Pina B., Rooney A.P., Camps F., Roelofs W.L.,
RA Fabrias G.;
RT "Expression and evolution of delta9 and delta11 desaturase genes in the
RT moth Spodoptera littoralis.";
RL Insect Biochem. Mol. Biol. 34:1315-1328(2004).
CC -!- FUNCTION: Catalyzes the formation of delta(11) fatty acyl precursors in
CC the pheromone gland, and has high activity towards palmitic acid and
CC stearic acid. {ECO:0000269|PubMed:15544945}.
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:15544945};
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 the pheromone gland.
CC {ECO:0000269|PubMed:15544945}.
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; AY362879; AAQ74259.1; -; mRNA.
DR AlphaFoldDB; Q6US81; -.
DR SMR; Q6US81; -.
DR BRENDA; 1.14.19.5; 5837.
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..338
FT /note="Acyl-CoA Delta(11) desaturase"
FT /id="PRO_0000418991"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 318..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 83..88
FT /note="Histidine box-1"
FT MOTIF 120..124
FT /note="Histidine box-2"
FT MOTIF 260..264
FT /note="Histidine box-3"
SQ SEQUENCE 338 AA; 39085 MW; 29511BBC8A56F8F0 CRC64;
MAQCVQTTTI LEQKEEKTVT LLVPQAGKRK FEIVYFNIIT FAYWHIAGLY GLYLCFTSTK
WATVLFSFFL FVVAEVGVTA GSHRLWSHKT YKAKLPLQIL LMVMNSLAFQ NTVIDWVRDH
RLHHKYSDTD ADPHNASRGF FYSHVGWLLV RKHPDVKKRG KEIDISDIYN NPVLRFQKKY
AIPFIGAVCF VLPTLIPVYG WGETWTNAWH VAMLRYIMNL NVTFLVNSAA HIYGKRPYDK
KILPSQNIAV SIATFGEGFH NYHHVFPWDY RAAELGNNSL NFPTKFIDFF AWIGWAYDLK
TVSKEMIKQR SKRTGDGTNL WGLEDVDTPE DLKNTKGE
