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MKAR_USTMA
ID   MKAR_USTMA              Reviewed;         350 AA.
AC   Q4P622; A0A0D1DSL9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=UMAG_04441;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the microsomal membrane bound fatty acid
CC       elongation system, which produces the 26-carbon very long-chain fatty
CC       acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-
CC       ketoacyl-CoA intermediate that is formed in each cycle of fatty acid
CC       elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
CC       {ECO:0000255|HAMAP-Rule:MF_03107}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-
CC         long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03107};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P38286}.
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 (SDR)
CC       family. {ECO:0000255|HAMAP-Rule:MF_03107}.
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DR   EMBL; CM003153; KIS67339.1; -; Genomic_DNA.
DR   RefSeq; XP_011391124.1; XM_011392822.1.
DR   AlphaFoldDB; Q4P622; -.
DR   SMR; Q4P622; -.
DR   STRING; 5270.UM04441P0; -.
DR   EnsemblFungi; KIS67339; KIS67339; UMAG_04441.
DR   GeneID; 23564623; -.
DR   KEGG; uma:UMAG_04441; -.
DR   VEuPathDB; FungiDB:UMAG_04441; -.
DR   eggNOG; KOG1014; Eukaryota.
DR   HOGENOM; CLU_010194_38_0_1; -.
DR   InParanoid; Q4P622; -.
DR   OMA; FLQHWSS; -.
DR   OrthoDB; 895581at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000561; Chromosome 14.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045703; F:ketoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR   HAMAP; MF_03107; 3_ketoreductase; 1.
DR   InterPro; IPR027533; 3_ketoreductase_fungal.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..350
FT                   /note="Very-long-chain 3-oxoacyl-CoA reductase"
FT                   /id="PRO_0000357323"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT   ACT_SITE        228
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
SQ   SEQUENCE   350 AA;  37725 MW;  90436BAEE9C7ACD1 CRC64;
     MAIEQHIDGL LRHVGLRVDH GLTPVSASLV LLAGIGALSV GTFALRLVRL FADVYILPGN
     SVSKYGANKK DLTRASWAVV TGATDGIGRE FALQLARKGF NIVLVSRSPE KLGSVAAEIE
     AATPGVRTKT QAIDFALGDE RQYEGLEHTV KGLNVGVLVN NVGKSHNMPV TFTETSEEEM
     EDIIEINVVS VLRVSKMIIP GMVDRKRGLV LNLGSFAGQV TTPMLATYAG SKAFLSGWSQ
     ALGEEVKRSN VDVSLLNTYF VVSNLSKIRK SSAMIPTPKQ YVTQVLKTLG RNGGAVGRPY
     TATPWPGHAL VDWATTFVLP RGWLLSYTYG QQVATRKRAL NKAHKAVKSA
 
 
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