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Database: UniProt
Entry: B0D8R3
LinkDB: B0D8R3
Original site: B0D8R3 
ID   MKAR_LACBS              Reviewed;         338 AA.
AC   B0D8R3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   29-OCT-2014, entry version 42.
DE   RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_03107};
DE            EC=1.1.1.330 {ECO:0000255|HAMAP-Rule:MF_03107};
DE   AltName: Full=3-ketoacyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_03107};
DE            Short=3-ketoreductase {ECO:0000255|HAMAP-Rule:MF_03107};
DE            Short=KAR {ECO:0000255|HAMAP-Rule:MF_03107};
DE   AltName: Full=Microsomal beta-keto-reductase {ECO:0000255|HAMAP-Rule:MF_03107};
GN   ORFNames=LACBIDRAFT_192627;
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured
OS   deceiver) (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Tricholomataceae;
OC   Laccaria.
OX   NCBI_TaxID=486041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686;
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A.,
RA   Shapiro H.J., Wuyts J., Blaudez D., Buee M., Brokstein P.,
RA   Canbaeck B., Cohen D., Courty P.E., Coutinho P.M., Delaruelle C.,
RA   Detter J.C., Deveau A., DiFazio S., Duplessis S.,
RA   Fraissinet-Tachet L., Lucic E., Frey-Klett P., Fourrey C.,
RA   Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P., Kilaru S.,
RA   Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R., Melayah D.,
RA   Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
CC   -!- FUNCTION: Component of the microsomal membrane bound fatty acid
CC       elongation system, which produces the 26-carbon very long-chain
CC       fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the
CC       3-ketoacyl-CoA intermediate that is formed in each cycle of fatty
CC       acid elongation. VLCFAs serve as precursors for ceramide and
CC       sphingolipids. {ECO:0000255|HAMAP-Rule:MF_03107}.
CC   -!- CATALYTIC ACTIVITY: A very-long-chain (3R)-3-hydroxyacyl-CoA +
CC       NADP(+) = a very-long-chain 3-oxoacyl-CoA + NADPH.
CC       {ECO:0000255|HAMAP-Rule:MF_03107}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03107}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03107}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. {ECO:0000255|HAMAP-Rule:MF_03107}.
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DR   EMBL; DS547100; EDR09116.1; -; Genomic_DNA.
DR   RefSeq; XP_001880429.1; XM_001880394.1.
DR   ProteinModelPortal; B0D8R3; -.
DR   STRING; 29883.JGI192627; -.
DR   GeneID; 6076163; -.
DR   KEGG; lbc:LACBIDRAFT_192627; -.
DR   eggNOG; COG0300; -.
DR   InParanoid; B0D8R3; -.
DR   KO; K10251; -.
DR   OrthoDB; EOG7NPG46; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045703; F:ketoreductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030497; P:fatty acid elongation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_03107; 3_ketoreductase; 1.
DR   InterPro; IPR027533; 3_ketoreductase_fungal.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   Pfam; PF00106; adh_short; 1.
DR   PIRSF; PIRSF000126; 11-beta-HSD1; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Endoplasmic reticulum; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    338       Very-long-chain 3-oxoacyl-CoA reductase.
FT                                /FTId=PRO_0000357311.
FT   TRANSMEM     20     40       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03107}.
FT   ACT_SITE    214    214       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03107}.
FT   BINDING     201    201       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03107}.
SQ   SEQUENCE   338 AA;  36601 MW;  63859EE86F225A41 CRC64;
     MDVFNVQELS FSLVRDQPYL SAFLLVMGSI GVGRVIYQTL SVFLQTFILP GTNLRKFGAK
     KGAWAVVTGA TDGIGREFSL QLAKAGFHVF LVARNEALLA STAAEIEQKY GVSTATHSID
     FSKADKSAYN SLGSSLGSVD VGVLVNNVGK SHAMPAYFVD TPEEEMSDIV SINVQATLQV
     THSVLPGMVQ RKRGLILNVG SFAGAVPSPM LATYSGTKAF LTTFSSALGE EVRKDNITVE
     HLNTYFVVSK LSKIRKASAL IPKPDAYVRS VLSKIGLPCG ASYSGRPNTS TPFWSHALLD
     YGLTLIGLQS AFISYTHGLH KDIRRRALRK MERDAKLQ
//
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