(data stored in ACNUC7421 zone)

SWISSPROT: A1AZ60_PARDP

ID   A1AZ60_PARDP            Unreviewed;       373 AA.
AC   A1AZ60;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 98.
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   OrderedLocusNames=Pden_0440 {ECO:0000313|EMBL:ABL68554.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68554.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000489; ABL68554.1; -; Genomic_DNA.
DR   RefSeq; WP_011746787.1; NC_008686.1.
DR   STRING; 318586.Pden_0440; -.
DR   PRIDE; A1AZ60; -.
DR   EnsemblBacteria; ABL68554; ABL68554; Pden_0440.
DR   KEGG; pde:Pden_0440; -.
DR   eggNOG; ENOG4105C0C; Bacteria.
DR   eggNOG; COG0473; LUCA.
DR   HOGENOM; HOG000021112; -.
DR   KO; K00052; -.
DR   OMA; EYDLGAR; -.
DR   BioCyc; PDEN318586:G1GW1-440-MONOMER; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AZ60.
DR   SWISS-2DPAGE; A1AZ60.
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:UP000000361};
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, ECO:0000313|EMBL:ABL68554.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT   DOMAIN        5    366       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      77     90       NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   NP_BIND     294    306       NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       231    231       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   METAL       259    259       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   BINDING      97     97       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     107    107       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     231    231       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   SITE        142    142       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   SITE        198    198       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
SQ   SEQUENCE   373 AA;  40200 MW;  94851545CEDF304D CRC64;
     MTTYSLLILP GDGIGPEVMA EVRKVIGWFE KSRGLSFDVS EDLVGGAAYD KYGKPLADET
     MAKAQAVDAV LLGAVGGPKY DNLDFSVKPE RGLLRLRKEM DLFANLRPAQ CFDALADFSS
     LKREVVAGLD ILIVRELTSG VYFGEPRGIH ADDNNPDNEG GRVGVNTQRY TSGEIRRVAR
     SAFELARKRS NRVCSMEKAN VMESGILWRE EVQWVHDNEY PDVELSHMYA DNGAMQLVRN
     PRQFDVIVTD NLFGDILSDA AAMLTGSLGM LPSASLGAPM ANGRPKALYE PVHGSAPDIA
     GQGKANPIAC ILSFAMCLRY SFGLGAEADL LEKAVERVLA DGVRTGDLMG AEGGKPVSTA
     EMGDHIVAAL SAL
//

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