(data stored in ACNUC7421 zone)

SWISSPROT: LEU3_RUEPO

ID   LEU3_RUEPO              Reviewed;         367 AA.
AC   Q5LWZ5;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033};
DE            EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01033};
DE   AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01033};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033};
DE            Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01033};
GN   Name=leuB {ECO:0000255|HAMAP-Rule:MF_01033};
GN   OrderedLocusNames=SPO0210;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-
CC         oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01033};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01033}.
DR   EMBL; CP000031; AAV93535.1; -; Genomic_DNA.
DR   RefSeq; WP_011045978.1; NC_003911.12.
DR   SMR; Q5LWZ5; -.
DR   STRING; 246200.SPO0210; -.
DR   EnsemblBacteria; AAV93535; AAV93535; SPO0210.
DR   KEGG; sil:SPO0210; -.
DR   eggNOG; ENOG4105C0C; Bacteria.
DR   eggNOG; COG0473; LUCA.
DR   HOGENOM; HOG000021112; -.
DR   KO; K00052; -.
DR   OMA; EYDLGAR; -.
DR   OrthoDB; 1551125at2; -.
DR   BioCyc; RPOM246200:G1G48-214-MONOMER; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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;
DR   PRODOM; Q5LWZ5.
DR   SWISS-2DPAGE; Q5LWZ5.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW   Manganese; Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    367       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083749.
FT   NP_BIND      77     90       NAD. {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   NP_BIND     287    299       NAD. {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       224    224       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       248    248       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       252    252       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   BINDING      97     97       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     107    107       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     135    135       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     224    224       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   SITE        142    142       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   SITE        192    192       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
SQ   SEQUENCE   367 AA;  39481 MW;  5C6FED0D71E5CBD5 CRC64;
     MSNPSLLILP GDGIGPEVMA EVRKIIGWFG DKRGLNFDVS EDLVGGAAYD VHGVPLADET
     MAKAQEADAV LLGAVGGPKY DDLDFSVKPE RGLLRLRKEM DLFSNLRPAQ CFDALADFSS
     LKKDIVAGLD IMIVRELTSG VYFGEPRGIF EEGNERVGIN TQRYTESEIE RVARSAFELA
     MRRSKKLCSM EKANVMESGI LWREVVTRVA KDYPEVELSH MYADNGAMQL VRAPKQFDVI
     LTDNLFGDIL SDCAAMLTGS LGMLPSASLG APMANGRPKA LYEPVHGSAP DIAGQGKANP
     IACILSFAMA LRYSFDQGAE ADRLEAAVEQ VLADGVRTAD LLGTEGVTPV STTEMGAAIL
     AKLDASL
//

If you have problems or comments...

PBIL Back to PBIL home page