DES6_CERPU
ID DES6_CERPU Reviewed; 520 AA.
AC Q9LEM9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Acyl-lipid (9-3)-desaturase {ECO:0000303|PubMed:10848999};
DE EC=1.14.19.47 {ECO:0000269|PubMed:10848999};
DE AltName: Full=Delta 6-fatty acid desaturase {ECO:0000303|PubMed:10848999};
DE Short=CpDES6 {ECO:0000303|PubMed:10848999};
OS Ceratodon purpureus (Fire moss) (Dicranum purpureum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Dicranidae; Pseudoditrichales; Ditrichaceae;
OC Ceratodon.
OX NCBI_TaxID=3225 {ECO:0000312|EMBL:CAB94993.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=10848999; DOI=10.1046/j.1432-1327.2000.01418.x;
RA Sperling P., Lee M., Girke T., Zahringer U., Stymne S., Heinz E.;
RT "A bifunctional delta-fatty acyl acetylenase/desaturase from the moss
RT Ceratodon purpureus. A new member of the cytochrome b5 superfamily.";
RL Eur. J. Biochem. 267:3801-3811(2000).
CC -!- FUNCTION: Fatty acid desaturase able to introduce a delta(6)-double
CC bond into delta(9)-unsaturated fatty-acid substrates. Has a strong
CC preference for linoleic acid (18:2(9Z,12Z)).
CC {ECO:0000269|PubMed:10848999}.
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:10848999};
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:10848999};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:10848999}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ250735; CAB94993.1; -; mRNA.
DR AlphaFoldDB; Q9LEM9; -.
DR SMR; Q9LEM9; -.
DR BioCyc; MetaCyc:MON-15861; -.
DR UniPathway; UPA00658; -.
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; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Acyl-lipid (9-3)-desaturase"
FT /id="PRO_0000435459"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 97..171
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 249..253
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 286..290
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 457..461
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 132
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 154
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 520 AA; 59160 MW; 5A9332EECC153439 CRC64;
MVSQGGGLSQ GSIEENIDVE HLATMPLVSD FLNVLGTTLG QWSLSTTFAF KRLTTKKHSS
DISVEAQKES VARGPVENIS QSVAQPIRRR WVQDKKPVTY SLKDVASHDM PQDCWIIIKE
KVYDVSTFAE QHPGGTVINT YFGRDATDVF STFHASTSWK ILQNFYIGNL VREEPTLELL
KEYRELRALF LREQLFKSSK SYYLFKTLIN VSIVATSIAI ISLYKSYRAV LLSASLMGLF
IQQCGWLSHD FLHHQVFETR WLNDVVGYVV GNVVLGFSVS WWKTKHNLHH AAPNECDQKY
TPIDEDIDTL PIIAWSKDLL ATVESKTMLR VLQYQHLFFL VLLTFARASW LFWSAAFTLR
PELTLGEKLL ERGTMALHYI WFNSVAFYLL PGWKPVVWMV VSELMSGFLL GYVFVLSHNG
MEVYNTSKDF VNAQIASTRD IKAGVFNDWF TGGLNRQIEH HLFPTMPRHN LNKISPHVET
LCKKHGLVYE DVSMASGTYR VLKTLKDVAD AASHQQLAAS
