DESA_ARTPT
ID DESA_ARTPT Reviewed; 351 AA.
AC Q54794;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Delta(12)-fatty-acid desaturase;
DE EC=1.14.19.6 {ECO:0000269|PubMed:15560373};
GN Name=desA;
OS Arthrospira platensis (Spirulina platensis).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Arthrospira.
OX NCBI_TaxID=118562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Murata N., Deshnium P., Tasaka Y.;
RT "Biosynthesis of gamma-linolenic acid in the cyanobacterium Spirulina
RT platensis.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16233567; DOI=10.1016/s1389-1723(04)70143-7;
RA Hongsthong A., Deshnium P., Paithoonrangsarid K., Cheevadhanarak S.,
RA Tanticharoen M.;
RT "Differential responses of three acyl-lipid desaturases to immediate
RT temperature reduction occurring in two lipid membranes of Spirulina
RT platensis strain C1.";
RL J. Biosci. Bioeng. 96:519-524(2003).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=15560373; DOI=10.1023/b:mole.0000043571.78809.40;
RA Apiradee H., Kalyanee P., Pongsathon P., Patcharaporn D., Matura S.,
RA Sanjukta S., Supapon C., Morakot T.;
RT "The expression of three desaturase genes of Spirulina platensis in
RT Escherichia coli DH5alpha. Heterologous expression of Spirulina-desaturase
RT genes.";
RL Mol. Biol. Rep. 31:177-189(2004).
RN [4]
RP INDUCTION.
RX PubMed=18336550; DOI=10.1111/j.1574-6968.2008.01100.x;
RA Jeamton W., Mungpakdee S., Sirijuntarut M., Prommeenate P.,
RA Cheevadhanarak S., Tanticharoen M., Hongsthong A.;
RT "A combined stress response analysis of Spirulina platensis in terms of
RT global differentially expressed proteins, and mRNA levels and stability of
RT fatty acid biosynthesis genes.";
RL FEMS Microbiol. Lett. 281:121-131(2008).
CC -!- FUNCTION: Can introduce a second cis double bond at the Delta(12)
CC position of fatty acid bound to membranes glycerolipids. This enzyme is
CC involved in chilling tolerance because the phase transition temperature
CC of lipids of cellular membranes depends on the degree of unsaturation
CC of fatty acids of the membrane lipids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:25856, 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:57383,
CC ChEBI:CHEBI:57387; EC=1.14.19.6;
CC Evidence={ECO:0000269|PubMed:15560373};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:45096, 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:61540,
CC ChEBI:CHEBI:76552; EC=1.14.19.6;
CC Evidence={ECO:0000250|UniProtKB:P20388};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16233567};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16233567}. Thylakoid
CC {ECO:0000269|PubMed:16233567}.
CC -!- INDUCTION: Expression is light and temperature-dependent with a
CC decrease with decreased light conditions or lower temperatures.
CC {ECO:0000269|PubMed:16233567, ECO:0000269|PubMed:18336550}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X86736; CAA60415.1; -; Genomic_DNA.
DR PIR; S54259; S54259.
DR AlphaFoldDB; Q54794; -.
DR UniPathway; UPA00658; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009579; C:thylakoid; IEA:UniProtKB-SubCell.
DR GO; GO:0102985; F:delta12-fatty-acid desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102987; F:palmitoleic acid delta 12 desaturase activity; IEA:RHEA.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005804; FA_desaturase_dom.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="Delta(12)-fatty-acid desaturase"
FT /id="PRO_0000185416"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 89..93
FT /note="Histidine box-1"
FT MOTIF 125..129
FT /note="Histidine box-2"
FT MOTIF 286..290
FT /note="Histidine box-3"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 40928 MW; 125A9F1E07E5EE97 CRC64;
MTLSIVKSED SSSRPSAVPS DLPLEEDIIN TLPSGVFVQD RYKAWMTVII NVVMVGLGWL
GIAIAPWFLL PVVWVFTGTA LTGFFVIGHD CGHRSFSRNV WVNDWVGHIL FLPIIYPFHS
WRIGHNQHHK YTNRMELDNA WQPWRKEEYQ NAGKFMQVTY DLFRGRAWWI GSILHWASIH
FDWTKFEGKQ RQQVKFSSLL VIGAAAIAFP TMILTIGVWG FVKFWVIPWL VFHFWMSTFT
LLHHTIADIP FREPEQWHEA ESQLSGTVHC NYSRWGEFLC HDINVHIPHH VTTAIPWYNL
RTPTPVYRKI GGEYLYPECD FSWGLMKQVV DHAICMMRIT IISQSLTTKR V
