(data stored in SCRATCH zone)

SWISSPROT: Q13S31_PARXL

ID   Q13S31_PARXL            Unreviewed;       355 AA.
AC   Q13S31;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 93.
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   ORFNames=Bxe_B2887 {ECO:0000313|EMBL:ABE33108.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33108.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33108.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33108.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
CC       2-oxopentanoate + CO(2) + NADH. {ECO:0000256|HAMAP-Rule:MF_01033,
CC       ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571562}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU004445};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU004445};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {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       ECO:0000256|SAAS:SAAS00571576}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01033}.
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DR   EMBL; CP000271; ABE33108.1; -; Genomic_DNA.
DR   RefSeq; WP_011490491.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13S31; -.
DR   STRING; 266265.Bxe_B2887; -.
DR   EnsemblBacteria; ABE33108; ABE33108; Bxe_B2887.
DR   GeneID; 4006748; -.
DR   KEGG; bxb:DR64_5216; -.
DR   KEGG; bxe:Bxe_B2887; -.
DR   PATRIC; fig|266265.5.peg.4802; -.
DR   eggNOG; ENOG4105C0C; Bacteria.
DR   eggNOG; COG0473; LUCA.
DR   HOGENOM; HOG000021112; -.
DR   KO; K00052; -.
DR   OMA; EYDLGAR; -.
DR   OrthoDB; POG091H01YH; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-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:UniProtKB-HAMAP.
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   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; Q13S31.
DR   SWISS-2DPAGE; Q13S31.
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:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571563};
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:ABE33108.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        2    351       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     280    292       NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       222    222       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       246    246       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       250    250       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   BINDING      90     90       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     100    100       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     128    128       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     222    222       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   SITE        135    135       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   SITE        190    190       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
SQ   SEQUENCE   355 AA;  38109 MW;  C293F8BFD0614236 CRC64;
     MKIAVLPGDG IGPEIVKEAV KVLNVLGEKF ELEEAPVGGA GYEAKGHPLP DSTLALAKEA
     DAILFGAVGD WKYDSLERAL RPEQAILGLR KHLQLFANFR PAICYPQLTG ASSLKEEIVS
     GLDILIVREL NGDIYFGSPR GVREAPDGLF AGSKEGFDTM RYSEPEVRRI AHVAFQAAQK
     RGKKLTSVDK ANVLETSQFW KDVMIDVSKE YADVELSHMY VDNAAMQLVK APKSFDVIVT
     GNMFGDILSD EAAMLTGSIG MLPSASLDKN NKGLYEPSHG SAPDIAGKGV ANPLATILSA
     AMMLRYSLNK AEQADRIENA VKKVLEQGYR TGDIVTPGCK QVGTVAMGDA VVAAL
//

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