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sn-2 acyl-lipid omega-3 desaturase (ferredoxin), chloroplastic (EC 1.14.19.35) (Omega-3 fatty acid desaturase 7, chloroplastic)

 FAD3C_ARATH             Reviewed;         446 AA.
P46310;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-APR-2018, entry version 136.
RecName: Full=sn-2 acyl-lipid omega-3 desaturase (ferredoxin), chloroplastic {ECO:0000303|PubMed:8226956};
EC=1.14.19.35 {ECO:0000269|PubMed:8226956};
AltName: Full=Omega-3 fatty acid desaturase 7, chloroplastic {ECO:0000303|PubMed:8226956};
Flags: Precursor;
Name=FAD7 {ECO:0000303|PubMed:8226956};
Synonyms=FADD {ECO:0000303|PubMed:8029334};
OrderedLocusNames=At3g11170 {ECO:0000312|Araport:AT3G11170};
ORFNames=F11B9.10 {ECO:0000312|EMBL:AAG50977.1},
F9F8.4 {ECO:0000312|EMBL:AAF01508.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Hypocotyl;
PubMed=8029334; DOI=10.1104/pp.103.2.467;
Yadav N.S., Wierzbicki A., Aegerter M., Caster C.S., Perez-Grau L.,
Kinney A.J., Hitz W.D., Booth J.R. Jr., Schweiger B., Stecca K.L.,
Allen S.M., Blackwell M., Reiter R.S., Carlson T.J., Russell S.H.,
Feldmann K.A., Pierce J., Browse J.;
"Cloning of higher plant omega-3 fatty acid desaturases.";
Plant Physiol. 103:467-476(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
PATHWAY, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Aerial part;
PubMed=8226956;
Iba K., Gibson S., Nishiuchi T., Fuse T., Nishimura M., Arondel V.,
Hugly S., Somerville C.R.;
"A gene encoding a chloroplast omega-3 fatty acid desaturase
complements alterations in fatty acid desaturation and chloroplast
copy number of the fad7 mutant of Arabidopsis thaliana.";
J. Biol. Chem. 268:24099-24105(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Hypocotyl;
Watahiki M., Yamamoto K.;
"cDNA cloning of fatty acid desaturase from Arabidopsis thaliana.";
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Wassilewskija;
PubMed=12766230; DOI=10.1074/mcp.M300030-MCP200;
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
Garin J., Joyard J., Rolland N.;
"Proteomics of the chloroplast envelope membranes from Arabidopsis
thaliana.";
Mol. Cell. Proteomics 2:325-345(2003).
-!- FUNCTION: Chloroplast omega-3 fatty acid desaturase introduces the
third double bond in the biosynthesis of 16:3 and 18:3 fatty
acids, important constituents of plant membranes. It is thought to
use ferredoxin as an electron donor and to act on fatty acids
esterified to galactolipids, sulfolipids and phosphatidylglycerol.
{ECO:0000269|PubMed:8226956}.
-!- CATALYTIC ACTIVITY: A (7Z,10Z)-hexadeca-7,10-dienoyl-
[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O(2)
+ 2 H(+) = a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid]
+ 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O.
{ECO:0000269|PubMed:8226956}.
-!- CATALYTIC ACTIVITY: A linoleoyl-[glycerolipid] + 2 reduced
ferredoxin [iron-sulfur] cluster + O(2) + 2 H(+) = an alpha-
linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur]
cluster + 2 H(2)O. {ECO:0000269|PubMed:8226956}.
-!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid
biosynthesis. {ECO:0000269|PubMed:8226956}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
{ECO:0000269|PubMed:12766230}; Multi-pass membrane protein
{ECO:0000269|PubMed:12766230}.
-!- TISSUE SPECIFICITY: Most abundant in leaves and seedlings.
{ECO:0000269|PubMed:8226956}.
-!- DOMAIN: The histidine box domains may contain the active site
and/or be involved in metal ion binding. {ECO:0000305}.
-!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
{ECO:0000305}.
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EMBL; L22961; AAA61773.1; -; mRNA.
EMBL; D14007; BAA03106.1; -; Genomic_DNA.
EMBL; D26019; BAA05040.1; -; mRNA.
EMBL; AC009991; AAF01508.1; -; Genomic_DNA.
EMBL; AC073395; AAG50977.1; -; Genomic_DNA.
EMBL; CP002686; AEE75009.1; -; Genomic_DNA.
PIR; JQ2336; JQ2336.
RefSeq; NP_187727.1; NM_111953.3.
UniGene; At.272; -.
ProteinModelPortal; P46310; -.
BioGrid; 5622; 2.
STRING; 3702.AT3G11170.1; -.
PaxDb; P46310; -.
EnsemblPlants; AT3G11170.1; AT3G11170.1; AT3G11170.
GeneID; 820288; -.
Gramene; AT3G11170.1; AT3G11170.1; AT3G11170.
KEGG; ath:AT3G11170; -.
Araport; AT3G11170; -.
TAIR; locus:2074628; AT3G11170.
eggNOG; ENOG410IGZD; Eukaryota.
eggNOG; COG3239; LUCA.
HOGENOM; HOG000201904; -.
InParanoid; P46310; -.
KO; K10257; -.
OMA; INRMSHH; -.
OrthoDB; EOG09360BAK; -.
PhylomeDB; P46310; -.
BioCyc; ARA:AT3G11170-MONOMER; -.
BioCyc; MetaCyc:AT3G11170-MONOMER; -.
UniPathway; UPA00658; -.
PRO; PR:P46310; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P46310; baseline and differential.
Genevisible; P46310; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042170; C:plastid membrane; TAS:TAIR.
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; IEA:InterPro.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
GO; GO:0009409; P:response to cold; IMP:TAIR.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR005804; FA_desaturase_dom.
InterPro; IPR021863; FAS_N.
Pfam; PF11960; DUF3474; 1.
Pfam; PF00487; FA_desaturase; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
Oxidoreductase; Plastid; Plastid inner membrane; Reference proteome;
Transit peptide; Transmembrane; Transmembrane helix.
TRANSIT 1 65 Chloroplast. {ECO:0000305}.
CHAIN 66 446 sn-2 acyl-lipid omega-3 desaturase
(ferredoxin), chloroplastic.
{ECO:0000255}.
/FTId=PRO_0000007117.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TRANSMEM 141 161 Helical. {ECO:0000255}.
TRANSMEM 231 250 Helical. {ECO:0000255}.
TRANSMEM 279 299 Helical. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
MOTIF 163 167 Histidine box-1. {ECO:0000305}.
MOTIF 199 203 Histidine box-2. {ECO:0000305}.
MOTIF 366 370 Histidine box-3. {ECO:0000305}.
COMPBIAS 182 208 His-rich. {ECO:0000255|PROSITE-
ProRule:PRU00009}.
COMPBIAS 360 379 His-rich. {ECO:0000255|PROSITE-
ProRule:PRU00009}.
SEQUENCE 446 AA; 51174 MW; 121125F634553D35 CRC64;
MANLVLSECG IRPLPRIYTT PRSNFLSNNN KFRPSLSSSS YKTSSSPLSF GLNSRDGFTR
NWALNVSTPL TTPIFEESPL EEDNKQRFDP GAPPPFNLAD IRAAIPKHCW VKNPWKSLSY
VVRDVAIVFA LAAGAAYLNN WIVWPLYWLA QGTMFWALFV LGHDCGHGSF SNDPKLNSVV
GHLLHSSILV PYHGWRISHR THHQNHGHVE NDESWHPMSE KIYNTLDKPT RFFRFTLPLV
MLAYPFYLWA RSPGKKGSHY HPDSDLFLPK ERKDVLTSTA CWTAMAALLV CLNFTIGPIQ
MLKLYGIPYW INVMWLDFVT YLHHHGHEDK LPWYRGKEWS YLRGGLTTLD RDYGLINNIH
HDIGTHVIHH LFPQIPHYHL VEATEAAKPV LGKYYREPDK SGPLPLHLLE ILAKSIKEDH
YVSDEGEVVY YKADPNLYGE VKVRAD


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