DESAT_BOMMO
ID DESAT_BOMMO Reviewed; 330 AA.
AC Q75PL7; H9JPV8; Q9NDH3;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=(11Z)-hexadec-11-enoyl-CoA conjugase;
DE Short=Bmpgdesat1 {ECO:0000303|PubMed:15173596};
DE EC=1.14.19.15 {ECO:0000269|PubMed:15173596};
DE AltName: Full=Acyl-CoA Delta(11) desaturase;
DE EC=1.14.19.5 {ECO:0000269|PubMed:15173596};
DE AltName: Full=Acyl-CoA Z11/delta10,12 desaturase {ECO:0000312|EMBL:BAD18122.1};
GN Name=desat1 {ECO:0000303|PubMed:15173596};
GN ORFNames=BGIBMGA011563 {ECO:0000303|PubMed:19121390};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pheromone gland {ECO:0000312|EMBL:AAF80355.1};
RX PubMed=10767556; DOI=10.1016/s0378-1119(00)00047-0;
RA Yoshiga T., Okano K., Mita K., Shimada T., Matsumoto S.;
RT "cDNA cloning of acyl-CoA desaturase homologs in the silkworm, Bombyx
RT mori.";
RL Gene 246:339-345(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=p50T {ECO:0000312|EMBL:BAD18122.1};
RC TISSUE=Pheromone gland {ECO:0000312|EMBL:BAD18122.1};
RX PubMed=15173596; DOI=10.1073/pnas.0402056101;
RA Moto K., Suzuki M.G., Hull J.J., Kurata R., Takahashi S., Yamamoto M.,
RA Okano K., Imai K., Ando T., Matsumoto S.;
RT "Involvement of a bifunctional fatty-acyl desaturase in the biosynthesis of
RT the silkmoth, Bombyx mori, sex pheromone.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8631-8636(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
CC -!- FUNCTION: Fatty acid desaturase that catalyzes 2 consecutive steps in
CC the biosynthesis of bombykol, a sex pheromone produced by the moth.
CC First acts as an acyl-CoA Delta(11) desaturase (1) by catalyzing the
CC formation of Delta(11) fatty acyl precursors. Then acts as a (11Z)-
CC hexadec-11-enoyl-CoA conjugase (2) by converting a single cis double
CC bond at position 11 of (11Z)-hexadec-11-enoyl-CoA into conjugated 10
CC trans and 12 cis double bonds. {ECO:0000269|PubMed:15173596}.
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:15173596};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z)-hexadecenoyl-CoA + AH2 + O2 = (10E,12Z)-hexadecadienoyl-
CC CoA + A + 2 H2O; Xref=Rhea:RHEA:46444, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:86120, ChEBI:CHEBI:86122; EC=1.14.19.15;
CC Evidence={ECO:0000269|PubMed:15173596};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the pheromone gland.
CC {ECO:0000269|PubMed:15173596}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BABH01015400; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF157627; AAF80355.1; -; mRNA.
DR EMBL; AB166851; BAD18122.1; -; mRNA.
DR EMBL; BABH01015400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001037017.2; NM_001043552.2.
DR AlphaFoldDB; Q75PL7; -.
DR SMR; Q75PL7; -.
DR GeneID; 692567; -.
DR KEGG; bmor:692567; -.
DR CTD; 117369; -.
DR OrthoDB; 971318at2759; -.
DR BioCyc; MetaCyc:MON-18415; -.
DR BRENDA; 1.14.19.15; 890.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017105; F:acyl-CoA delta11-desaturase activity; IEA:UniProtKB-EC.
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:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042811; P:pheromone biosynthetic process; IDA: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;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..330
FT /note="(11Z)-hexadec-11-enoyl-CoA conjugase"
FT /id="PRO_0000434734"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 87..92
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 124..128
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 264..268
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="L -> I (in Ref. 1; AAF80355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 38077 MW; 1A56524DC6C88B1C CRC64;
MPPNSVDKTN ETEYLKDNHV DYEKLIAPQA SPIKHKIVVM NVIRFSYLHI AGLYGLYLCF
TSAKLATSVF AIVLFFLGNF GITAGAHRLW SHNGYKVKLP LEILLMVFNS IAFQNTIFTW
VRDHRLHHKY TDTDADPHNA TRGFFFSHIG WLLVRKHPMV KIAGKSLDMS DIYCNPLLRF
QKKYAIPFIG TICFIIPTLA PMYFWGESLN NAWHITVLRY IFSLNGTFLV NSAAHLWGYK
PYDKSLKATQ SGMANAFTFG EGFHNYHHVF PWDYRADELG DRYINLTTRF IDFFAWMGWA
YDLKTASTNI IEKRALRTGD GTYKRPNGMN
