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LEU3_LEPIN
ID   LEU3_LEPIN              Reviewed;         358 AA.
AC   P24015;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=3-isopropylmalate dehydrogenase;
DE            EC=1.1.1.85;
DE   AltName: Full=3-IPM-DH;
DE   AltName: Full=Beta-IPM dehydrogenase;
DE            Short=IMDH;
GN   Name=leuB; OrderedLocusNames=LA_2152;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Kenniwicki / Serogroup Pomona / Serovar pomona;
RX   PubMed=8336106; DOI=10.1099/00221287-139-5-1093;
RA   Ding M., Yelton D.B.;
RT   "Cloning and analysis of the leuB gene of Leptospira interrogans serovar
RT   pomona.";
RL   J. Gen. Microbiol. 139:1093-1103(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
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DR   EMBL; M59431; AAA72088.1; -; Unassigned_DNA.
DR   EMBL; AE010300; AAN49351.1; -; Genomic_DNA.
DR   RefSeq; NP_712333.1; NC_004342.2.
DR   RefSeq; WP_000799846.1; NC_004342.2.
DR   AlphaFoldDB; P24015; -.
DR   SMR; P24015; -.
DR   STRING; 189518.LA_2152; -.
DR   EnsemblBacteria; AAN49351; AAN49351; LA_2152.
DR   GeneID; 61141667; -.
DR   KEGG; lil:LA_2152; -.
DR   PATRIC; fig|189518.3.peg.2144; -.
DR   HOGENOM; CLU_031953_0_3_12; -.
DR   InParanoid; P24015; -.
DR   OMA; EYDLGAR; -.
DR   BioCyc; MetaCyc:MON-11898; -.
DR   BRENDA; 1.1.1.85; 2986.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   PANTHER; PTHR42979; PTHR42979; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00169; leuB; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW   Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..358
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083702"
FT   BINDING         75..88
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         283..295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            142
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            192
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  38871 MW;  E64192745EB9C370 CRC64;
     MKNVAVLSGD GIGPEVMEIA ISVLKKALGA KVSEFQFKEG FVGGIAIDKT GHPLPPETLK
     LCEESSAILF GSVGGPKWET LPPEKQPERG ALLPLRKHFD LFANLRPAII YPELKNASPV
     RSDIIGNGLD ILILRELTGG IYFGQPKGRE GSGQEEFAYD TMKYSRREIE RIAKVAFQAA
     RKRNNKVTSI DKANVLTTSV FWKEVVIELH KKEFSDVQLN HLYVDNAAMQ LIVNPKQFDV
     VLCENMFGDI LSDEASIITG SIGMLPSASL SESGFGLYEP SGGSAPDIAG KGVANPIAQV
     LSAALMLRYS FSMEEEANKI ETAVRKTIAS GKRTRDIAEV GSTIVGTKEI GQLIESFL
 
 
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