DES6_BOROF
ID DES6_BOROF Reviewed; 448 AA.
AC O04353;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Acyl-lipid (9-3)-desaturase {ECO:0000303|PubMed:9108131};
DE Short=BoDes6 {ECO:0000303|PubMed:9108131};
DE EC=1.14.19.47 {ECO:0000269|PubMed:9108131};
OS Borago officinalis (Bourrache) (Borage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Boraginales; Boraginaceae; Boraginoideae; Boragineae;
OC Boragininae; Borago.
OX NCBI_TaxID=13363 {ECO:0000312|EMBL:AAC49700.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=9108131; DOI=10.1073/pnas.94.8.4211;
RA Sayanova O., Smith M.A., Lapinskas P.A., Stobart K., Dobson G.,
RA Christie W.W., Shewry P.R., Napier J.A.;
RT "Expression of a borage desaturase cDNA containing an N-terminal cytochrome
RT b5 domain results in the accumulation of high levels of delta6-desaturated
RT fatty acids in transgenic tobacco.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4211-4216(1997).
CC -!- FUNCTION: Fatty acid desaturase able to introduce a delta(6)-double
CC bond into delta(9)-unsaturated fatty-acid substrates. Can use both
CC linoleic acid (18:2(9Z,12Z)) and alpha-linolenic acid
CC (18:3(9Z,12Z,15Z)) as substrates. {ECO:0000269|PubMed:9108131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-
CC octadecatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:46288, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:90078,
CC ChEBI:CHEBI:90079; EC=1.14.19.47;
CC Evidence={ECO:0000269|PubMed:9108131};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-
CC containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46284, 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:88351,
CC ChEBI:CHEBI:90081; EC=1.14.19.47;
CC Evidence={ECO:0000269|PubMed:9108131};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:9108131}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:9108131}; Multi-pass membrane protein
CC {ECO:0000255}.
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}.
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DR EMBL; U79010; AAC49700.1; -; mRNA.
DR AlphaFoldDB; O04353; -.
DR SMR; O04353; -.
DR KEGG; ag:AAC49700; -.
DR BioCyc; MetaCyc:MON-14126; -.
DR BRENDA; 1.14.19.3; 895.
DR BRENDA; 1.14.19.47; 895.
DR UniPathway; UPA00658; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..448
FT /note="Acyl-lipid (9-3)-desaturase"
FT /id="PRO_0000435460"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 6..90
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 159..163
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 196..200
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 373..377
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 41
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 64
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 448 AA; 51635 MW; B62EEE701680909F CRC64;
MAAQIKKYIT SDELKNHDKP GDLWISIQGK AYDVSDWVKD HPGGSFPLKS LAGQEVTDAF
VAFHPASTWK NLDKFFTGYY LKDYSVSEVS KDYRKLVFEF SKMGLYDKKG HIMFATLCFI
AMLFAMSVYG VLFCEGVLVH LFSGCLMGFL WIQSGWIGHD AGHYMVVSDS RLNKFMGIFA
ANCLSGISIG WWKWNHNAHH IACNSLEYDP DLQYIPFLVV SSKFFGSLTS HFYEKRLTFD
SLSRFFVSYQ HWTFYPIMCA ARLNMYVQSL IMLLTKRNVS YRAHELLGCL VFSIWYPLLV
SCLPNWGERI MFVIASLSVT GMQQVQFSLN HFSSSVYVGK PKGNNWFEKQ TDGTLDISCP
PWMDWFHGGL QFQIEHHLFP KMPRCNLRKI SPYVIELCKK HNLPYNYASF SKANEMTLRT
LRNTALQARD ITKPLPKNLV WEALHTHG
