ID C8W662_DESAS Unreviewed; 523 AA.
AC C8W662;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 31.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE EC=1.1.1.85;
GN OrderedLocusNames=Dtox_0597;
OS Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS B-1644).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=485916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644;
RX PubMed=21304664; DOI=10.4056/sigs.39508;;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
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).
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DR EMBL; CP001720; ACV61517.1; -; Genomic_DNA.
DR RefSeq; YP_003190140.1; NC_013216.1.
DR ProteinModelPortal; C8W662; -.
DR STRING; 485916.Dtox_0597; -.
DR EnsemblBacteria; ACV61517; ACV61517; Dtox_0597.
DR GeneID; 8427532; -.
DR KEGG; dae:Dtox_0597; -.
DR PATRIC; 21717897; VBIDesAce42372_0604.
DR eggNOG; COG0473; -.
DR HOGENOM; HOG000021112; -.
DR KO; K00052; -.
DR OMA; VDTMRYS; -.
DR BioCyc; DACE485916:GHUF-613-MONOMER; -.
DR UniPathway; UPA00048; UER00072.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:InterPro.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:EC.
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:UniProtKB-UniPathway.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.40.718.10; -; 1.
DR HAMAP; MF_01032; LeuD_type2; 1; -.
DR HAMAP; MF_01033; LeuB_type1; 1; -.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR011827; IsopropMal_deHydtase_ssu.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR PANTHER; PTHR11835; PTHR11835; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 1.
DR TIGRFAMs; TIGR00169; leuB; 1.
DR TIGRFAMs; TIGR02087; LEUD_arch; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW Manganese; Metal-binding; NAD; Oxidoreductase.
SQ SEQUENCE 523 AA; 56813 MW; 3A6884E2350A6254 CRC64;
MGLKGKAWKF GADIDTDAII PARYLNTSDP VELAKHCMED ADTSFAQKVQ PGDVIVADKN
FGCGSSREHA PISIKYAGVS CVIAKSFARI FYRNAFNIGL PILESTEAVE GIDEGNEVSV
NAETGTITNV TKGETYQATV VPPFMQQIIA AGGLINYVAE RMKVKKMYKI AVLPGDGIGP
EITEQALKAL KAVAEHFGHE FQFTEALVGG AAYDAVGHPL PKETLDLCYS SDAILLGAVG
GDKWADLPPE LTPERGALLP LRKLLGLYAN LRPAVVFPAL ANASTLKPEV VEGLDIMVVR
ELTGGLYFGE KKREDLPDGT VRVTDTLVYT TEEIVRIARL AFELAAKRRK KVTLVDKANV
LESSRYWREV VANMAAEYPD IEFNTMYVDN AAMQLVKMPK QFDVIVTDNM FGDILSDQAS
QLTGSLGMLA SASIGGKIGL YEPSHGSAPK YAGLKRANPI ATVMSGAMLL RYSFDMEKEA
KAIEDAVTEV LKKYRTRDIM EEGLQLVNTD EMGDRIAEQI LAG
//
