FAD9_ACHDO
ID FAD9_ACHDO Reviewed; 359 AA.
AC Q9BH41;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Acyl-CoA Delta-9 desaturase {ECO:0000303|PubMed:12429125};
DE Short=AdD9Des {ECO:0000303|PubMed:19133076};
DE EC=1.14.19.1 {ECO:0000269|PubMed:12429125, ECO:0000269|PubMed:19133076, ECO:0000269|PubMed:21300802};
DE AltName: Full=Delta-9 desaturase 1 {ECO:0000312|EMBL:AAK25796.1};
DE Short=Cricd9des1 {ECO:0000303|PubMed:12429125};
DE AltName: Full=Delta-9 desaturase 3 {ECO:0000312|EMBL:AAK25797.1};
DE Short=Cricd9des3 {ECO:0000303|PubMed:12429125};
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=12429125; DOI=10.1016/s0965-1748(02)00113-3;
RA Riddervold M.H., Tittiger C., Blomquist G.J., Borgeson C.E.;
RT "Biochemical and molecular characterizaton of house cricket (Acheta
RT domesticus, Orthoptera: Gryllidae) Delta9 desaturase.";
RL Insect Biochem. Mol. Biol. 32:1731-1740(2002).
RN [2]
RP 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 [3]
RP 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 Delta9 double bond, acting on
CC saturated fatty acyl subtrates like palmitoyl-CoA (hexadecanoyl-CoA)
CC and stearoyl-CoA (octadecanoyl-CoA) with higher desaturation activity
CC on octadecanoyl-CoA than hexadecanoyl-CoA.
CC {ECO:0000269|PubMed:12429125, ECO:0000269|PubMed:19133076,
CC ECO:0000269|PubMed:21300802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, 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:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000269|PubMed:12429125, ECO:0000269|PubMed:19133076,
CC ECO:0000269|PubMed:21300802};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19722;
CC Evidence={ECO:0000305|PubMed:12429125, ECO:0000305|PubMed:19133076,
CC ECO:0000305|PubMed:21300802};
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:12429125,
CC ECO:0000269|PubMed:19133076, ECO:0000269|PubMed:21300802};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932;
CC Evidence={ECO:0000305|PubMed:12429125, ECO:0000305|PubMed:19133076,
CC 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; AF338465; AAK25796.1; -; Transcribed_RNA.
DR EMBL; AF338466; AAK25797.1; -; mRNA.
DR AlphaFoldDB; Q9BH41; -.
DR SMR; Q9BH41; -.
DR SwissLipids; SLP:000000457; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR11351; PTHR11351; 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..359
FT /note="Acyl-CoA Delta-9 desaturase"
FT /id="PRO_0000452363"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 96..101
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:Q6US81"
FT MOTIF 133..137
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:Q6US81"
FT MOTIF 274..278
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:Q6US81"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 245
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 274
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 277
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 278
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
SQ SEQUENCE 359 AA; 41374 MW; C9CF7E4A6AF9C42D CRC64;
MAPNITSAPT GVLFEGDTIG PAAKDQQAEV NAPEAKKPRE PYRRQIVWRN VILFIYLHLA
ALYGAYLAFT SAKIATTIFA IILYQVSGVG ITGGAHRLWA HRSYKAKWPL RVILMLCNTL
AFQNHIYEWA RDHRVHHKFS ETDADPHNAT RGFFFSHVGW LLVRKHPDVK EKGKGIDMHD
LEQDKIVMFQ KKYYLILMPI VCFLIPTTIP VYMWNETWSN AWFVATLFRY TFTLNMTWLV
NSAAHMWGSQ PYDKYINPAE NLGVALGAMG EGWHNYHHVF PWDYKAAELG NYRANFTTAF
IDFFARIGWA YDLKTVPVSM IQRRVERTGD GSHEVWGWGD KDMPQEDIDG AVIEKRKTQ
