DES_BACSU
ID DES_BACSU Reviewed; 352 AA.
AC O34653; Q796C9;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Fatty acid desaturase;
DE EC=1.14.19.-;
DE AltName: Full=Delta(5) acyl-lipid desaturase;
DE AltName: Full=Delta(5) desaturase;
GN Name=des; Synonyms=desA, yocE; OrderedLocusNames=BSU19180;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION BY COLD SHOCK.
RX PubMed=9555904; DOI=10.1128/jb.180.8.2194-2200.1998;
RA Aguilar P.S., Cronan J.E. Jr., de Mendoza D.;
RT "A Bacillus subtilis gene induced by cold shock encodes a membrane
RT phospholipid desaturase.";
RL J. Bacteriol. 180:2194-2200(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION BY COLD SHOCK.
RX PubMed=8326865; DOI=10.1111/j.1365-2958.1993.tb01598.x;
RA Grau R., de Mendoza D.;
RT "Regulation of the synthesis of unsaturated fatty acids by growth
RT temperature in Bacillus subtilis.";
RL Mol. Microbiol. 8:535-542(1993).
RN [5]
RP SUBSTRATE SPECIFICITY.
RX PubMed=16105701; DOI=10.1016/j.jbiotec.2005.07.008;
RA Bonamore A., Macone A., Colotti G., Matarese R.M., Boffi A.;
RT "The desaturase from Bacillus subtilis, a promising tool for the selective
RT olefination of phospholipids.";
RL J. Biotechnol. 121:49-53(2006).
CC -!- FUNCTION: Catalyzes the introduction of a cis-double bond at the
CC delta(5) position of existing saturated fatty acids attached to
CC membrane phospholipids. It is not strictly specific for palmitic acid
CC (C16) but can also accept C14 as well as C18 species to yield
CC unsaturated fatty acids. {ECO:0000269|PubMed:9555904}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Transcriptionally regulated by DesR/DesK in response to cold
CC shock. {ECO:0000269|PubMed:8326865, ECO:0000269|PubMed:9555904}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF027868; AAB84436.1; -; Genomic_DNA.
DR EMBL; AF037430; AAC38355.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13810.1; -; Genomic_DNA.
DR PIR; B69901; B69901.
DR RefSeq; NP_389799.1; NC_000964.3.
DR RefSeq; WP_004399588.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34653; -.
DR STRING; 224308.BSU19180; -.
DR PaxDb; O34653; -.
DR EnsemblBacteria; CAB13810; CAB13810; BSU_19180.
DR GeneID; 939668; -.
DR KEGG; bsu:BSU19180; -.
DR PATRIC; fig|224308.179.peg.2096; -.
DR eggNOG; COG3239; Bacteria.
DR InParanoid; O34653; -.
DR OMA; PYDCWRR; -.
DR PhylomeDB; O34653; -.
DR BioCyc; BSUB:BSU19180-MON; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001570; Chromosome.
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: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; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="Fatty acid desaturase"
FT /id="PRO_0000390566"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 76..80
FT /note="Histidine box-1"
FT /evidence="ECO:0000255"
FT MOTIF 112..116
FT /note="Histidine box-2"
FT /evidence="ECO:0000255"
FT MOTIF 274..278
FT /note="Histidine box-3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 40708 MW; 80F5ECD62346B635 CRC64;
MTEQTIAHKQ KQLTKQVAAF AQPETKNSLI QLLNTFIPFF GLWFLAYLSL DVSYLLTLAL
TVIAAGFLTR IFIIFHDCCH QSFFKQKRYN HILGFLTGVL TLFPYLQWQH SHSIHHATSS
NLDKRGTGDI WMLTVNEYKA ASRRTKLAYR LYRNPFIMFI LGPIYVFLIT NRFNKKGARR
KERVNTYLTN LAIVALAAAC CLIFGWQSFL LVQGPIFLIS GSIGVWLFYV QHTFEDSYFE
ADENWSYVQA AVEGSSFYKL PKLLQWLTGN IGYHHVHHLS PKVPNYKLEV AHEHHEPLKN
VPTITLKTSL QSLAFRLWDE DNKQFVSFRA IKHIPVSLPP DSPEKQKLRK NA
