FAD12_ACHDO
ID FAD12_ACHDO Reviewed; 357 AA.
AC B7SB91;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Acyl-CoA Delta12-desaturase {ECO:0000303|PubMed:19133076};
DE Short=AdD12Des {ECO:0000303|PubMed:19133076};
DE EC=1.14.19.6 {ECO:0000269|PubMed:21300802, ECO:0000305|PubMed:19133076};
DE AltName: Full=Delta-12/Delta9 desaturase {ECO:0000303|PubMed:21300802};
DE Short=AdD12/9des {ECO:0000303|PubMed:21300802};
GN Name=D12Des {ECO:0000312|EMBL:ABY26957.1};
OS Acheta domesticus (House cricket).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Ensifera; Gryllidea; Grylloidea;
OC Gryllidae; Gryllinae; Acheta.
OX NCBI_TaxID=6997;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19133076; DOI=10.1111/j.1365-2583.2008.00841.x;
RA Zhou X.-R., Horne I., Damcevski K., Haritos V., Green A., Singh S.;
RT "Isolation and functional characterization of two independently-evolved
RT fatty acid Delta12-desaturase genes from insects.";
RL Insect Mol. Biol. 17:667-676(2008).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21300802; DOI=10.1074/jbc.m110.191098;
RA Vanhercke T., Shrestha P., Green A.G., Singh S.P.;
RT "Mechanistic and structural insights into the regioselectivity of an acyl-
RT CoA fatty acid desaturase via directed molecular evolution.";
RL J. Biol. Chem. 286:12860-12869(2011).
CC -!- FUNCTION: Catalyzes the formation of a Delta12 double bond, acting on
CC monounsaturated fatty acyl subtrates like palmitoleoyl-CoA ((9Z)-
CC hexadecenoyl-CoA) and oleoyl-CoA ((9Z)-octadecenoyl-CoA) with higher
CC desaturation activity on (9Z)-octadecenoyl-CoA than (9Z)-hexadecenoyl-
CC CoA. Requires preexisting cis double bond at the Delta9 position of
CC fatty acyls to be able to insert the Delta12 double bond. Delta12-
CC desaturation of (9Z)-octadecenoyl-CoA in insects produces (9Z,12Z)-
CC octadecadienoyl-CoA (linoleoyl-CoA) which may be used to supply
CC precursors of crucial mediators of immunity and reproduction and other
CC essential functions (PubMed:19133076, PubMed:21300802). Can also
CC catalyze Delta9-desaturation on saturated fatty acyl substrates like
CC palmitoyl-CoA (hexadecanoyl-CoA) but with lower efficiency
CC (PubMed:21300802). {ECO:0000269|PubMed:19133076,
CC ECO:0000269|PubMed:21300802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:25856, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57387; EC=1.14.19.6;
CC Evidence={ECO:0000269|PubMed:21300802, ECO:0000305|PubMed:19133076};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25857;
CC Evidence={ECO:0000305|PubMed:19133076, ECO:0000305|PubMed:21300802};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:45096, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:61540,
CC ChEBI:CHEBI:76552; EC=1.14.19.6;
CC Evidence={ECO:0000305|PubMed:19133076};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45097;
CC Evidence={ECO:0000305|PubMed:19133076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36931, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:21300802};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932;
CC Evidence={ECO:0000305|PubMed:21300802};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:O00767};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000255|RuleBase:RU000581}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; EU159448; ABY26957.1; -; mRNA.
DR AlphaFoldDB; B7SB91; -.
DR SMR; B7SB91; -.
DR SwissLipids; SLP:000000456; -.
DR BRENDA; 1.14.19.6; 7760.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102985; F:delta12-fatty-acid desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
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..357
FT /note="Acyl-CoA Delta12-desaturase"
FT /id="PRO_0000452361"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 94..99
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:Q99PL7"
FT MOTIF 131..135
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:Q99PL7"
FT MOTIF 272..276
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:Q99PL7"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 276
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
SQ SEQUENCE 357 AA; 41113 MW; 7672A25D6932D709 CRC64;
MDLNEESAPS GVLFEEDVAE QEAKMANGGP KKGKKLEEPY RLEIVWFNVL WFVLLHAGAL
YGVYLIFASA KIYTTLYGFL LCELSLLSIT AGVHRLWAHR AYKAKWPLRL TLMVLNLLAY
QNSIYEWARD HRVHHKFSET NADPVNAKRG FFFSHVGWLL CRKHPEVRAK GGRIDLSDLE
RDPIVMFQKR HYYKLVPFVS FVIPTLIPMY FWGETLSNSW YVSTMFRYCL SLNLTWLVNS
AAHMWGNKPY DKNINPVENL AVAIGSLGEG WHNFHHVFPW DYKTSELGNY SLNFTNAFID
LAVLLGLAYD LKTVPVSMIK TRVGRTGDGS HDVWGWGDKD LPKELADQTM IENRKTE
