DES_CHLRE
ID DES_CHLRE Reviewed; 476 AA.
AC Q2HWK7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acyl-lipid omega-13 desaturase {ECO:0000303|PubMed:16267098};
DE Short=CrDES {ECO:0000303|PubMed:16267098};
DE EC=1.14.19.12 {ECO:0000269|PubMed:16267098};
DE AltName: Full=Omega13 fatty acid desaturase {ECO:0000303|PubMed:16267098};
GN Name=DES {ECO:0000303|PubMed:16267098};
GN ORFNames=CHLREDRAFT_182572 {ECO:0000312|EMBL:EDP08027.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000312|EMBL:BAE79427.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=C9;
RX PubMed=16267098; DOI=10.1093/pcp/pci224;
RA Kajikawa M., Yamato K.T., Kohzu Y., Shoji S., Matsui K., Tanaka Y.,
RA Sakai Y., Fukuzawa H.;
RT "A front-end desaturase from Chlamydomonas reinhardtii produces pinolenic
RT and coniferonic acids by omega13 desaturation in methylotrophic yeast and
RT tobacco.";
RL Plant Cell Physiol. 47:64-73(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
CC -!- FUNCTION: Front-end desaturase having a omega-13 desaturase activity
CC for omega-9 unsaturated C18/C20 fatty acids. Strong substrate
CC preferences for linoleic acid and alpha-linolenic acid for the
CC production of pinolenic and coniferonic acids respectively. No
CC desaturase activity for dihomo gamma-linolenic acid and
CC eicosatertraenoic acid. {ECO:0000269|PubMed:16267098}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a (5Z,9Z,12Z)-octadecatrienoyl-
CC containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46236, 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:88238,
CC ChEBI:CHEBI:88351; EC=1.14.19.12;
CC Evidence={ECO:0000269|PubMed:16267098};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (5Z,9Z,12Z,15Z)-
CC octadecatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:38039, 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:88239,
CC ChEBI:CHEBI:90078; EC=1.14.19.12;
CC Evidence={ECO:0000269|PubMed:16267098};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB239770; BAE79428.1; -; mRNA.
DR EMBL; AB239769; BAE79427.1; -; Genomic_DNA.
DR EMBL; DS496111; EDP08027.1; -; Genomic_DNA.
DR RefSeq; XP_001698534.1; XM_001698482.1.
DR AlphaFoldDB; Q2HWK7; -.
DR SMR; Q2HWK7; -.
DR STRING; 3055.EDP08027; -.
DR PaxDb; Q2HWK7; -.
DR EnsemblPlants; PNW77828; PNW77828; CHLRE_10g453600v5.
DR EnsemblPlants; PNW77829; PNW77829; CHLRE_10g453600v5.
DR GeneID; 5723905; -.
DR Gramene; PNW77828; PNW77828; CHLRE_10g453600v5.
DR Gramene; PNW77829; PNW77829; CHLRE_10g453600v5.
DR KEGG; cre:CHLRE_10g453600v5; -.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_030320_1_0_1; -.
DR InParanoid; Q2HWK7; -.
DR OMA; YHEHVIG; -.
DR OrthoDB; 1060606at2759; -.
DR BioCyc; MetaCyc:MON-17794; -.
DR BRENDA; 1.14.19.12; 1318.
DR UniPathway; UPA00658; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102431; F:acyl-lipid omega-(9-4) desaturase; IDA:UniProtKB.
DR GO; GO:0102430; F:alpha-linolenate delta5 desaturase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0043651; P:linoleic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033559; P:unsaturated fatty acid metabolic process; IDA:UniProtKB.
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; IPR018506; Cyt_B5_heme-BS.
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 SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..476
FT /note="Acyl-lipid omega-13 desaturase"
FT /id="PRO_0000434400"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 10..75
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 189..193
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 224..229
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 410..414
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 37
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 60
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 476 AA; 53622 MW; 0CF734A34FE739C8 CRC64;
MCRPTDSDSG PALPSIPHQY WIIHGATYDL ASYIKSHPGG DEAILLGRGR DCTELFEQYH
VLNNKHLRVL ERFRVTLPAA KVATNNLKED MVSTISAFEG EEADAAAVVG IQQPAAPARV
AHQSDPFYED IKAMVRAHGN TKMSAPFVIL HCLHVVGLIW SMKLWWQGAF ISAFILPYFL
WVLCAAMVHD GGHFAHSKRP LVNKLLTHTG ALFTNSVGCW YLQHNILHHS YTNLVGKDGD
LDSHHPYMRI HPEQSMLPAN IHHAVRFFSH LIMYNFAHIG LTMISPLSYF RGVAAQKKGT
ADAKQAQDAQ TVAQYHSTVM LQLVTVGAFY ITPFLRFDFS RALLLTLLPT FMMSVAFMVI
AQVSHIQMDA EAPSADLEKL HWARRMALTS VDYSQESTLW AYLTIGLNMQ SLHHIVPGVS
YSQLPRLYPA YRAICEKHGI KLLERRNLAH AFWTHLQTLW VLSKTHSFVE VARKLA
