(data stored in ACNUC7421 zone)

SWISSPROT: B4SR46_STRM5

ID   B4SR46_STRM5            Unreviewed;       400 AA.
AC   B4SR46;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 49.
DE   SubName: Full=Fatty acid desaturase {ECO:0000313|EMBL:ACF49747.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0042 {ECO:0000313|EMBL:ACF49747.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49747.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49747.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49747.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF49747.1; -; Genomic_DNA.
DR   RefSeq; WP_004133312.1; NC_011071.1.
DR   STRING; 391008.Smal_0042; -.
DR   EnsemblBacteria; ACF49747; ACF49747; Smal_0042.
DR   KEGG; smt:Smal_0042; -.
DR   eggNOG; ENOG410637N; Bacteria.
DR   eggNOG; COG1398; LUCA.
DR   HOGENOM; HOG000220383; -.
DR   KO; K00507; -.
DR   OMA; AQNTREW; -.
DR   OrthoDB; 797871at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00210-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; 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; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd03505; Delta9-FADS-like; 1.
DR   InterPro; IPR015876; Acyl-CoA_DS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   PANTHER; PTHR11351; PTHR11351; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
PE   4: Predicted;
DR   PRODOM; B4SR46.
DR   SWISS-2DPAGE; B4SR46.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     16     40       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    143    165       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       18    229       FA_desaturase. {ECO:0000259|Pfam:
FT                                PF00487}.
SQ   SEQUENCE   400 AA;  45558 MW;  1A6BED25157E311F CRC64;
     MPDALMSLLT GGVLGLGWWA MLAVLLVFTQ ITIFSVTLYL HRSQAHRGVD FHPALAHVFR
     FWLWLTTSMI TREWVAIHRK HHAKVETEDD PHSPVTRGIG KVFWHGVELY REARGQRADI
     EQYGRGTPDD AIERRLYTPH ATLGPVLLFA INTVLFGLPG VALWAIQMAW IPFWAAGVVN
     GLGHWWGYRN YESADTSTNL TPWGFWIGGE ELHNNHHAFP SSARFAMRRW EFDIGWSAIR
     LLQALRLAKV LRVVPAMDVR PNIAVPDAET LKALLSHRFQ AMTDYQRNVF MPALREEAVQ
     AGAKLRRLLP RRLRRGLVND GRWLKPDSRA QLSEWVAQRP RIRTLVEYRG RLAALLEARG
     HDAAERLHQL QAWCREAEES GIAALQAYAA RLKGYSLVGA
//

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