D5FAD_PHYPA
ID D5FAD_PHYPA Reviewed; 480 AA.
AC A9SIZ6;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Acyl-lipid (8-3)-desaturase {ECO:0000305};
DE EC=1.14.19.30 {ECO:0000305|PubMed:16728405};
DE AltName: Full=AN Delta(5)-fatty-acid desaturase {ECO:0000305};
DE AltName: Full=Acyl-lipid 5-desaturase {ECO:0000305};
DE AltName: Full=Delta-5 desaturase {ECO:0000305};
DE Short=PPDES5 {ECO:0000303|PubMed:16728405};
GN Name=DES5 {ECO:0000305};
GN ORFNames=PHYPADRAFT_165175 {ECO:0000312|EMBL:EDQ68896.1};
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;
RN [1]
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16728405; DOI=10.1074/jbc.m603022200;
RA Kaewsuwan S., Cahoon E.B., Perroud P.F., Wiwat C., Panvisavas N.,
RA Quatrano R.S., Cove D.J., Bunyapraphatsara N.;
RT "Identification and functional characterization of the moss Physcomitrella
RT patens delta5-desaturase gene involved in arachidonic and eicosapentaenoic
RT acid biosynthesis.";
RL J. Biol. Chem. 281:21988-21997(2006).
CC -!- FUNCTION: Fatty acid desaturase that introduces a cis double bond at
CC the 5-position in 20-carbon polyunsaturated fatty acids incorporated in
CC a glycerolipid that contain a Delta(8) double bond.
CC {ECO:0000269|PubMed:16728405}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (8Z,11Z,14Z)-icosatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46260, 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:90076,
CC ChEBI:CHEBI:90077; EC=1.14.19.30;
CC Evidence={ECO:0000305|PubMed:16728405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (8Z,11Z,14Z,17Z)-eicosatetraenoyl-containing glycerolipid +
CC 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46264, 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:90082,
CC ChEBI:CHEBI:90083; EC=1.14.19.30;
CC Evidence={ECO:0000305|PubMed:16728405};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain acts as the direct
CC electron donor to the active site of the desaturase, and does not
CC require an external cytochrome. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Defects in the fatty acid composition.
CC {ECO:0000269|PubMed:16728405}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; DS544972; EDQ68896.1; -; Genomic_DNA.
DR RefSeq; XP_001766264.1; XM_001766212.1.
DR AlphaFoldDB; A9SIZ6; -.
DR SMR; A9SIZ6; -.
DR STRING; 3218.PP1S83_225V6.2; -.
DR EnsemblPlants; Pp3c15_5610V3.1; Pp3c15_5610V3.1; Pp3c15_5610.
DR EnsemblPlants; Pp3c15_5610V3.2; Pp3c15_5610V3.2; Pp3c15_5610.
DR EnsemblPlants; Pp3c15_5610V3.3; Pp3c15_5610V3.3; Pp3c15_5610.
DR Gramene; Pp3c15_5610V3.1; Pp3c15_5610V3.1; Pp3c15_5610.
DR Gramene; Pp3c15_5610V3.2; Pp3c15_5610V3.2; Pp3c15_5610.
DR Gramene; Pp3c15_5610V3.3; Pp3c15_5610V3.3; Pp3c15_5610.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_030320_1_0_1; -.
DR InParanoid; A9SIZ6; -.
DR OMA; NGRECTA; -.
DR OrthoDB; 1060606at2759; -.
DR Proteomes; UP000006727; Chromosome 15.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102866; F:di-homo-gamma-linolenate delta5 desaturase activity; IEA:RHEA.
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:0042759; P:long-chain fatty acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic 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; 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 Electron transport; Fatty acid biosynthesis; Fatty acid metabolism; Heme;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..480
FT /note="Acyl-lipid (8-3)-desaturase"
FT /id="PRO_0000434761"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 33..107
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 203..207
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:Q8S3C0"
FT MOTIF 238..243
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:Q8S3C0"
FT MOTIF 419..423
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:Q8S3C0"
FT BINDING 68
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 90
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 480 AA; 54267 MW; 8098F54ECA0C7D11 CRC64;
MAPHSADTAG LVPSDELRLR TSNSKGPEQE QTLKKYTLED VSRHNTPADC WLVIWGKVYD
VTSWIPNHPG GSLIHVKAGQ DSTQLFDSYH PLYVRKMLAK YCIGELVPSA GDDKFKKATL
EYADAENEDF YLVVKQRVES YFKSNKINPQ IHPHMILKSL FILGGYFASY YLAFFWSSSV
LVSLFFALWM GFFAAEVGVS IQHDGNHGSY TKWRGFGYIM GASLDLVGAS SFMWRQQHVV
GHHSFTNVDN YDPDIRVKDP DVRRVATTQP RQWYHAYQHI YLAVLYGTLA LKSIFLDDFL
AYFTGSIGPV KVAKMTPLEF NIFFQGKLLY AFYMFVLPSV YGVHSGGTFL ALYVASQLIT
GWMLAFLFQV AHVVDDVAFP TPEGGKVKGG WAAMQVATTT DFSPRSWFWG HVSGGLNNQI
EHHLFPGVCH VHYPAIQPIV EKTCKEFDVP YVAYPTFWTA LRAHFAHLKK VGLTEFRLDG
