(data stored in ACNUC7421 zone)

HOGENOM: FRASU_1_PE1008

ID   FRASU_1_PE1008                       STANDARD;      PRT;   343 AA.
AC   FRASU_1_PE1008; E3IYV8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=3-isopropylmalate dehydrogenase; EC=1.1.1 85;AltName:
DE   Full=3-IPM-DH;AltName: Full=Beta-IPM dehydrogenase; (FRASU_1.PE1008).
GN   Name=leuB; OrderedLocusNames=FraEuI1c_1023;
OS   FRANKIA SP. EUI1C.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Frankineae;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=298654;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FRASU_1.PE1008.
CC       Frankia sp. EuI1c chromosome, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E3IYV8_FRASU
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
CC       oxopentanoate (By similarity).
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
CC       2-oxopentanoate + CO(2) + NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 2 subfamily.
CC   -!- GENE_FAMILY: HOG000021111 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E3IYV8; -.
DR   EMBL; CP002299; ADP79096.1; -; Genomic_DNA.
DR   RefSeq; YP_004014966.1; NC_014666.1.
DR   GeneID; 9971446; -.
DR   GenomeReviews; CP002299_GR; FraEuI1c_1023.
DR   KEGG; fri:FraEuI1c_1023; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:HAMAP.
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; IEA:HAMAP.
DR   HAMAP; MF_01035; LeuB_type2; 1; -.
DR   InterPro; IPR023698; 3-isopropylmalate_DH_LeuB.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
DR   HOGENOMDNA; FRASU_1.PE1008; -.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW   Manganese; Metal-binding; NAD; Oxidoreductase.
SQ   SEQUENCE   343 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKLAVIGGDG IGPEVVAEGL RVLRAVHDKV ETTDYDLGAR RWHETGETLP DTVLDELRGH
     DAILLGAVGD PNVPSGVLER GLLLRLRFEL DHHVNLRPVK LYPGVTSPLA GDPTIDMIVV
     REGTEGPYAG AGGVLRKGTP HEIATEESIN TRFGVERVVR DAFARAQRRP RRKLTLVHKN
     NVLTKAGDLW SRTVTEVAAE FPEITVEYQH ADAASMFFIT DPGRFDVVVT DNLFGDIITD
     IGAAVTGGIG LAASGNLDPS GAHPSMFEPV HGSAPDIAGK GVADPTATVA SVAMLLDHLG
     LTAEAAKVEK AVAGSLAARA ASAGQPLSTR EVGEDLAQRA VAN
//

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