(data stored in SCRATCH zone)

SWISSPROT: B6HD77_PENRW

ID   B6HD77_PENRW            Unreviewed;       455 AA.
AC   B6HD77;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Acyl-CoA desaturase {ECO:0000256|PIRNR:PIRNR000345};
DE            EC=1.14.19.1 {ECO:0000256|PIRNR:PIRNR000345};
GN   ORFNames=Pc20g01400 {ECO:0000313|EMBL:CAP85469.1}, PCH_Pc20g01400
GN   {ECO:0000313|EMBL:CAP85469.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85469.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85469.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons
CC       from reduced cytochrome b5 to introduce the first double bond into
CC       saturated fatty acyl-CoA substrates.
CC       {ECO:0000256|PIRNR:PIRNR000345}.
CC   -!- CATALYTIC ACTIVITY: Stearoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2
CC       H(+) = oleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR000345}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000345};
CC       Note=Expected to bind 2 Fe(2+) ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000345};
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|PIRNR:PIRNR000345}.
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DR   EMBL; AM920435; CAP85469.1; -; Genomic_DNA.
DR   RefSeq; XP_002562699.1; XM_002562653.1.
DR   ProteinModelPortal; B6HD77; -.
DR   STRING; 500485.XP_002562699.1; -.
DR   EnsemblFungi; CAP85469; CAP85469; PCH_Pc20g01400.
DR   GeneID; 8312277; -.
DR   KEGG; pcs:Pc20g01400; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   eggNOG; KOG1600; Eukaryota.
DR   eggNOG; COG1398; LUCA.
DR   eggNOG; COG5274; LUCA.
DR   HOGENOM; HOG000270353; -.
DR   KO; K00507; -.
DR   OMA; FNGGVYF; -.
DR   OrthoDB; EOG092C2CE8; -.
DR   BioCyc; PCHR:PC20G01400-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
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-UniRule.
DR   GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03505; Delta9-FADS-like; 1.
DR   Gene3D; 3.10.120.10; -; 1.
DR   InterPro; IPR009160; Acyl-CoA_deSatase_haem/ster-bd.
DR   InterPro; IPR015876; Acyl-CoA_DS.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR001522; FADS-1_CS.
DR   PANTHER; PTHR11351; PTHR11351; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PIRSF; PIRSF000345; OLE1; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   PRINTS; PR00075; FACDDSATRASE.
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.
DR   PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HD77.
DR   SWISS-2DPAGE; B6HD77.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000345};
KW   Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000345};
KW   Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000345};
KW   Heme {ECO:0000256|PIRNR:PIRNR000345, ECO:0000256|SAAS:SAAS00499898};
KW   Iron {ECO:0000256|PIRNR:PIRNR000345, ECO:0000256|SAAS:SAAS00499917};
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000345};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000345};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000345,
KW   ECO:0000256|SAAS:SAAS00499892};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000345,
KW   ECO:0000256|SAAS:SAAS00734536, ECO:0000313|EMBL:CAP85469.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|PIRNR:PIRNR000345}.
FT   TRANSMEM     36     56       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     63     84       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    177    198       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      330    408       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
SQ   SEQUENCE   455 AA;  51879 MW;  4048822ED5DE3B47 CRC64;
     MSSKPDATRP RAADTKKVHI ADTQMTRQNW YKHVNWLNVT FIIGVPISGC IQAFFVPLQL
     KTAIWAVIYY FFTGLGITAG YHRLWAHCSY SATLPMRIWL ALVGGGAVEG SIRWWARDHR
     AHHRYTDTDK DPYSVRKGLL YSHLGWMVMK QNPKRIGRTD ITDLNEDPVV VWQHRNYIKV
     VITMGLIVPM LVAGLGWGDW YGGFVYAGIL RIFFVQQATF CVNSLAHWLG DQPFDDRNSP
     RDHIITALVT LGEGYHNFHH EFPSDYRNAI EWHQYDPTKW TIWTCKQLGL AYDLKQFRSN
     EIEKGRVQQL QKKIDQKRAK LDWGTPLDQL PVMEWDDYVE QAKNGRGLIS IAGVVHDVTD
     FIKDHPGGKA MIKSGLGKDA TAMFNGGVYY HSNGAHNLLS TMRVGVIRGG GEVEIWKRAQ
     KENSEYVRDE TGQRIIRAGQ QVTKMPEPIP TADAA
//

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