(data stored in SCRATCH zone)

SWISSPROT: B7UIC3_ECO27

ID   B7UIC3_ECO27            Unreviewed;       363 AA.
AC   B7UIC3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   16-JAN-2019, entry version 70.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE            EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01033};
DE   AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01033};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE            Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01033};
GN   Name=leuB {ECO:0000256|HAMAP-Rule:MF_01033,
GN   ECO:0000313|EMBL:CAS07626.1};
GN   OrderedLocusNames=E2348C_0078 {ECO:0000313|EMBL:CAS07626.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07626.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07626.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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. {ECO:0000256|HAMAP-Rule:MF_01033,
CC       ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571560}.
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:0000256|HAMAP-Rule:MF_01033,
CC         ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS01118041};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00611795};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
CC       ECO:0000256|SAAS:SAAS00571573}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01033,
CC       ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571561}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01033}.
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DR   EMBL; FM180568; CAS07626.1; -; Genomic_DNA.
DR   RefSeq; WP_000042356.1; NC_011601.1.
DR   EnsemblBacteria; CAS07626; CAS07626; E2348C_0078.
DR   KEGG; ecg:E2348C_0078; -.
DR   HOGENOM; HOG000021112; -.
DR   KO; K00052; -.
DR   OMA; EYDLGAR; -.
DR   BioCyc; ECOL574521:E2348C_RS00405-MONOMER; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000008205; 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; B7UIC3.
DR   SWISS-2DPAGE; B7UIC3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571577};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
KW   ECO:0000256|SAAS:SAAS00571571};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571574};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571572};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571566};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571558};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
KW   ECO:0000256|SAAS:SAAS00571565};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571564}.
FT   DOMAIN        6    355       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      78     91       NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   NP_BIND     285    297       NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       227    227       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       251    251       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       255    255       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   BINDING      99     99       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     109    109       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     138    138       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     227    227       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   SITE        145    145       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   SITE        195    195       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
SQ   SEQUENCE   363 AA;  39501 MW;  125EC1165BB0F3B5 CRC64;
     MSKNYHIAVL PGDGIGPEVM TQALKVLDAV RNRFAMRITT SHYDVGGAAI DNHGQPLPPA
     TVEGCEQADA VLFGSVGGPK WEHLPPDQQP ERGALLPLRK HFKLFSNLRP AKLYQGLEAF
     CPLRADIAAN GFDILCVREL TGGIYFGQPK GREGSGQYEK AFDTEVYHRF EIERIARIAF
     ESARKRRHKV TSIDKANVLQ SSILWREIVN EIATEYPDVE LAHMYIDNAT MQLIKDPSQF
     DVLLCSNLFG DILSDECAMI TGSMGMLPSA SLNEQGFGLY EPAGGSAPDI AGKNIANPIA
     QILSLALLLR YSLDADDAAS AIERAINRAL EEGIRTGDLA RGAAAVSTDE MGDIIARYVA
     EGV
//

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