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ILV5_NEUCR
ID   ILV5_NEUCR              Reviewed;         402 AA.
AC   P38674; Q7RVD5; Q8X0I9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Ketol-acid reductoisomerase, mitochondrial;
DE            EC=1.1.1.86;
DE   AltName: Full=Acetohydroxy-acid reductoisomerase;
DE   AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase;
DE   Flags: Precursor;
GN   Name=ilv-2; ORFNames=B11H24.150, NCU03608;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1398116; DOI=10.1016/0378-1119(92)90018-k;
RA   Sista H., Bowman B.;
RT   "Characterization of the ilv-2 gene from Neurospora crassa encoding alpha-
RT   keto-beta-hydroxylacyl reductoisomerase.";
RL   Gene 120:115-118(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC         acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58476; EC=1.1.1.86;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-
CC         ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 2/4.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000305}.
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DR   EMBL; M84189; AAB00797.1; -; Genomic_DNA.
DR   EMBL; AL670005; CAD21284.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32099.1; -; Genomic_DNA.
DR   PIR; JC1428; JC1428.
DR   RefSeq; XP_961335.1; XM_956242.3.
DR   AlphaFoldDB; P38674; -.
DR   SMR; P38674; -.
DR   STRING; 5141.EFNCRP00000003426; -.
DR   PRIDE; P38674; -.
DR   EnsemblFungi; EAA32099; EAA32099; NCU03608.
DR   GeneID; 3877517; -.
DR   KEGG; ncr:NCU03608; -.
DR   VEuPathDB; FungiDB:NCU03608; -.
DR   HOGENOM; CLU_033821_1_2_1; -.
DR   InParanoid; P38674; -.
DR   OMA; RAMFSWL; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR   GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.10.1040.10; -; 3.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013023; KARI.
DR   InterPro; IPR000506; KARI_C.
DR   InterPro; IPR013116; KARI_N.
DR   InterPro; IPR016207; KetolA_reductoisomerase_fun.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR21371; PTHR21371; 1.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   PIRSF; PIRSF000119; Ilv5_fungal; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
DR   PROSITE; PS51851; KARI_C; 1.
DR   PROSITE; PS51850; KARI_N; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Magnesium;
KW   Metal-binding; Mitochondrion; NADP; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..402
FT                   /note="Ketol-acid reductoisomerase, mitochondrial"
FT                   /id="PRO_0000015632"
FT   DOMAIN          63..252
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT   DOMAIN          253..400
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000255"
FT   BINDING         90..99
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
FT   BINDING         114..119
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..156
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   CONFLICT        358
FT                   /note="T -> R (in Ref. 1; AAB00797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392..393
FT                   /note="Missing (in Ref. 1; AAB00797)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   402 AA;  44623 MW;  246F795898D2A174 CRC64;
     MAARNCTKAL RPLARQLATP AVQRRTFVAA ASAVRASVAV KAVAAPARQQ VRGVKTMDFA
     GHKEEVHERA DWPAEKLLDY FKNDTLALIG YGSQGHGQGL NLRDNGLNVI VGVRKNGKSW
     EDAIQDGWVP GKNLFDVDEA ISRGTIVMNL LSDAAQSETW PHIKPQITKG KTLYFSHGFS
     PVFKDLTKVE VPTDVDVILV APKGSGRTVR SLFREGRGIN SSFAVYQDVT GKAKEKAVAL
     GVAVGSGYLY ETTFEKEVYS DLYGERGCLM GGIHGMFLAQ YEVLRERGHS PSEAFNETVE
     EATQSLYPLI GAHGMDWMFD ACSTTARRGA IDWTPKFKDA LKPVFNNLYD SVKNGDETKR
     SLEYNSQPDY RERYEAELDE IRNLEIWRAG KAVRSLRPEN QK
 
 
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