DES6_PHYPA
ID DES6_PHYPA Reviewed; 525 AA.
AC Q9ZNW2; A9SC29; E1C9Y0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Acyl-lipid (9-3)-desaturase {ECO:0000303|PubMed:9744093};
DE EC=1.14.19.47 {ECO:0000269|PubMed:9744093};
GN Name=DES6 {ECO:0000303|PubMed:9744093};
GN ORFNames=PHYPADRAFT_164045 {ECO:0000312|EMBL:EDQ71334.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000312|EMBL:CAA11033.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=9744093; DOI=10.1046/j.1365-313x.1998.00178.x;
RA Girke T., Schmidt H., Zahringer U., Reski R., Heinz E.;
RT "Identification of a novel delta 6-acyl-group desaturase by targeted gene
RT disruption in Physcomitrella patens.";
RL Plant J. 15:39-48(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
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. Required for the biosynthesis of
CC arachidonic acid (20:4(5z,8Z,11Z,14Z)). {ECO:0000269|PubMed:9744093}.
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:9744093};
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:9744093};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:9744093}.
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 -!- DISRUPTION PHENOTYPE: Increased content in linoleic acid and
CC disappearance of gamma-linolenic and arachidonic acid.
CC {ECO:0000269|PubMed:9744093}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AJ222980; CAA11032.1; -; mRNA.
DR EMBL; AJ222981; CAA11033.1; -; Genomic_DNA.
DR EMBL; DS544953; EDQ71334.1; -; Genomic_DNA.
DR RefSeq; XP_001763930.1; XM_001763878.1.
DR AlphaFoldDB; Q9ZNW2; -.
DR SMR; Q9ZNW2; -.
DR STRING; 3218.PP1S64_155V6.2; -.
DR EnsemblPlants; Pp3c5_9590V3.2; Pp3c5_9590V3.2; Pp3c5_9590.
DR EnsemblPlants; Pp3c5_9590V3.3; Pp3c5_9590V3.3; Pp3c5_9590.
DR EnsemblPlants; Pp3c5_9590V3.4; Pp3c5_9590V3.4; Pp3c5_9590.
DR EnsemblPlants; Pp3c5_9590V3.5; Pp3c5_9590V3.5; Pp3c5_9590.
DR Gramene; Pp3c5_9590V3.2; Pp3c5_9590V3.2; Pp3c5_9590.
DR Gramene; Pp3c5_9590V3.3; Pp3c5_9590V3.3; Pp3c5_9590.
DR Gramene; Pp3c5_9590V3.4; Pp3c5_9590V3.4; Pp3c5_9590.
DR Gramene; Pp3c5_9590V3.5; Pp3c5_9590V3.5; Pp3c5_9590.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_016265_1_1_1; -.
DR OMA; CWIVIND; -.
DR BioCyc; MetaCyc:MON-12524; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000006727; Chromosome 5.
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 Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..525
FT /note="Acyl-lipid (9-3)-desaturase"
FT /id="PRO_0000435461"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 102..176
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 254..258
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 291..295
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 462..466
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 137
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 159
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 525 AA; 59369 MW; 530F158B0C97C83F CRC64;
MVFAGGGLQQ GSLEENIDVE HIASMSLFSD FFSYVSSTVG SWSVHSIQPL KRLTSKKRVS
ESAAVQCISA EVQRNSSTQG TAEALAESVV KPTRRRSSQW KKSTHPLSEV AVHNKPSDCW
IVVKNKVYDV SNFADEHPGG SVISTYFGRD GTDVFSSFHA ASTWKILQDF YIGDVERVEP
TPELLKDFRE MRALFLREQL FKSSKLYYVM KLLTNVAIFA ASIAIICWSK TISAVLASAC
MMALCFQQCG WLSHDFLHNQ VFETRWLNEV VGYVIGNAVL GFSTGWWKEK HNLHHAAPNE
CDQTYQPIDE DIDTLPLIAW SKDILATVEN KTFLRILQYQ HLFFMGLLFF ARGSWLFWSW
RYTSTAVLSP VDRLLEKGTV LFHYFWFVGT ACYLLPGWKP LVWMAVTELM SGMLLGFVFV
LSHNGMEVYN SSKEFVSAQI VSTRDIKGNI FNDWFTGGLN RQIEHHLFPT MPRHNLNKIA
PRVEVFCKKH GLVYEDVSIA TGTCKVLKAL KEVAEAAAEQ HATTS
