D4FAD_CHLRE
ID D4FAD_CHLRE Reviewed; 516 AA.
AC I2CYZ4; A8HMA4;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Acyl-lipid (7-3)-desaturase, chloroplastic {ECO:0000305};
DE EC=1.14.19.31 {ECO:0000305|PubMed:22562471};
DE AltName: Full=Acyl-lipid 4-desaturase {ECO:0000305};
DE AltName: Full=Fatty acyl delta4 desaturase {ECO:0000303|PubMed:22562471};
DE Flags: Precursor;
GN ORFNames=CHLREDRAFT_32523 {ECO:0000312|EMBL:AFJ74144.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Dw15-1 {ECO:0000312|EMBL:AFJ74144.1};
RX PubMed=22562471; DOI=10.1128/ec.00079-12;
RA Zaeuner S., Jochum W., Bigorowski T., Benning C.;
RT "A cytochrome b5-containing plastid-located fatty acid desaturase from
RT Chlamydomonas reinhardtii.";
RL Eukaryot. Cell 11:856-863(2012).
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: Fatty acid desaturase that introduces a cis double bond at
CC the 4-position in 16-carbon polyunsaturated fatty acids that contain a
CC Delta(7) double bond, resulting in the production of 16 carbon fatty
CC acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate.
CC {ECO:0000269|PubMed:22562471}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-containing
CC glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-containing glycerolipid + 2
CC Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46252, Rhea:RHEA-
CC COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:88266, ChEBI:CHEBI:88267;
CC EC=1.14.19.31; Evidence={ECO:0000305|PubMed:22562471};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (7Z,10Z,13Z,16Z)-docosatetraenoyl-containing glycerolipid +
CC 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (4Z,7Z,10Z,13Z,16Z)-
CC docosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46256, 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:88264,
CC ChEBI:CHEBI:88265; EC=1.14.19.31;
CC Evidence={ECO:0000305|PubMed:22562471};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000305|PubMed:22562471}; Multi-pass membrane protein
CC {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|PubMed:22562471}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP09855.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JN089704; AFJ74144.1; -; Genomic_DNA.
DR EMBL; DS496108; EDP09855.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001690117.1; XM_001690065.1.
DR AlphaFoldDB; I2CYZ4; -.
DR SMR; I2CYZ4; -.
DR STRING; 3055.EDP09855; -.
DR PaxDb; I2CYZ4; -.
DR EnsemblPlants; PNW88628; PNW88628; CHLRE_01g037700v5.
DR GeneID; 5715503; -.
DR Gramene; PNW88628; PNW88628; CHLRE_01g037700v5.
DR KEGG; ag:AFJ74144; -.
DR KEGG; cre:CHLRE_01g037700v5; -.
DR eggNOG; KOG4232; Eukaryota.
DR OMA; HHIHCND; -.
DR OrthoDB; 1447181at2759; -.
DR BRENDA; 1.14.19.31; 1318.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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; 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 PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SMART; SM01117; Cyt-b5; 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 Chloroplast; Electron transport; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Oxidoreductase; Plastid; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..516
FT /note="Acyl-lipid (7-3)-desaturase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434758"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 83..148
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 227..231
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 262..267
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 444..448
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
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 123
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 516 AA; 56877 MW; F934BC722B7327BD CRC64;
MNATMQRSAV AGRTSGKVAT TARASSMARP RLPIAGRVAR RSAVTVRAVA EPVVVDKAVE
APAKPVPSGG DPWEDEKWTK YKWTVYRGVA YDLTPYLDRH PGGRWLLNLA IGRDATALFE
SYHLRPEVAA SMLKRLPVLA DFPVDAVPPS PRPNDSELYN AIRERVRKEV FKGTEIKGAH
RSGSEGAAFA VLGYAAAMYA LYTYDANPLT GALLGLGGAW IGLTIQHCGN HGAMSTNPVV
NNLMGLTNDL AGGSSLMWRY HHQVSHHIHC NDDALDEDVF SAFPMLRFDD RLPKAWYHQF
QHVYMWALFP FLQLVFQIGD WQALLTNRTV GATLYGASNF ERQTLIAGKL AHYFLLYGLP
AFLHGPTAML GGAAGYLFTQ SIVLAATFAV SHNVPETKPL DPGPTRENLD ESAVTRDWGV
QQVLTSANWG GVIGNFFTGG LNLQIEHHLF PAISFMHYPA ISKIVADECK QRGIPYSHYD
TLPEILGRFV RYMKEVGAAP QKPVKRDGEM LMLSKF
