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Database: UniProt/SWISS-PROT
Entry: IDH_BACSU
LinkDB: IDH_BACSU
Original site: IDH_BACSU 
ID   IDH_BACSU               Reviewed;         423 AA.
AC   P39126;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   05-DEC-2018, entry version 145.
DE   RecName: Full=Isocitrate dehydrogenase [NADP];
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=IDP;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=Oxalosuccinate decarboxylase;
GN   Name=icd; Synonyms=citC; OrderedLocusNames=BSU29130;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / SMY;
RX   PubMed=8045898; DOI=10.1128/jb.176.15.4669-4679.1994;
RA   Jin S., Sonenshein A.L.;
RT   "Identification of two distinct Bacillus subtilis citrate synthase
RT   genes.";
RL   J. Bacteriol. 176:4669-4679(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes
RT   in the 200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PHOSPHORYLATION.
RX   PubMed=11751849; DOI=10.1074/jbc.M107908200;
RA   Singh S.K., Miller S.P., Dean A., Banaszak L.J., LaPorte D.C.;
RT   "Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for
RT   Escherichia coli isocitrate dehydrogenase kinase/phosphatase.";
RL   J. Biol. Chem. 277:7567-7573(2002).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH CITRATE, AND
RP   SUBUNIT.
RX   PubMed=11290745; DOI=10.1074/jbc.M101191200;
RA   Singh S.K., Matsuno K., LaPorte D.C., Banaszak L.J.;
RT   "Crystal structure of Bacillus subtilis isocitrate dehydrogenase at
RT   1.55 A. Insights into the nature of substrate specificity exhibited by
RT   Escherichia coli isocitrate dehydrogenase kinase/phosphatase.";
RL   J. Biol. Chem. 276:26154-26163(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC         Xref=Rhea:RHEA:19629, ChEBI:CHEBI:16087, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.42;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11290745}.
CC   -!- INTERACTION:
CC       P49814:mdh; NbExp=3; IntAct=EBI-7829570, EBI-7827708;
CC   -!- MISCELLANEOUS: The enzyme can be phosphorylated in vitro by the
CC       E.coli isocitrate dehydrogenase kinase/phosphatase, but B.subtilis
CC       lacks such an enzyme.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
DR   EMBL; U05257; AAA96342.1; -; Genomic_DNA.
DR   EMBL; AF008220; AAC00346.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14873.1; -; Genomic_DNA.
DR   PIR; I40382; I40382.
DR   RefSeq; NP_390791.1; NC_000964.3.
DR   RefSeq; WP_003229433.1; NZ_JNCM01000036.1.
DR   PDB; 1HQS; X-ray; 1.55 A; A/B=1-423.
DR   PDBsum; 1HQS; -.
DR   ProteinModelPortal; P39126; -.
DR   SMR; P39126; -.
DR   IntAct; P39126; 2.
DR   MINT; P39126; -.
DR   STRING; 224308.Bsubs1_010100015896; -.
DR   DrugBank; DB02159; (R)-Propylene glycol.
DR   DrugBank; DB04272; Citric Acid.
DR   PaxDb; P39126; -.
DR   PRIDE; P39126; -.
DR   EnsemblBacteria; CAB14873; CAB14873; BSU29130.
DR   GeneID; 938183; -.
DR   KEGG; bsu:BSU29130; -.
DR   PATRIC; fig|224308.179.peg.3163; -.
DR   eggNOG; ENOG4108HMX; Bacteria.
DR   eggNOG; COG0538; LUCA.
DR   HOGENOM; HOG000021113; -.
DR   InParanoid; P39126; -.
DR   KO; K00031; -.
DR   OMA; HGTAPKH; -.
DR   PhylomeDB; P39126; -.
DR   BioCyc; BSUB:BSU29130-MONOMER; -.
DR   SABIO-RK; P39126; -.
DR   EvolutionaryTrace; P39126; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR43504; PTHR43504; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00183; prok_nadp_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Glyoxylate bypass; Magnesium;
KW   Manganese; Metal-binding; NADP; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    423       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083549.
FT   NP_BIND     345    351       NADP. {ECO:0000250}.
FT   METAL       311    311       Magnesium or manganese. {ECO:0000250}.
FT   BINDING      95     95       NADP. {ECO:0000250}.
FT   BINDING      96     96       Substrate.
FT   BINDING     104    104       Substrate.
FT   BINDING     106    106       Substrate.
FT   BINDING     110    110       Substrate.
FT   BINDING     120    120       Substrate. {ECO:0000250}.
FT   BINDING     144    144       Substrate.
FT   BINDING     358    358       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING     397    397       NADP. {ECO:0000250}.
FT   BINDING     401    401       NADP. {ECO:0000250}.
FT   SITE        151    151       Critical for catalysis. {ECO:0000250}.
FT   SITE        221    221       Critical for catalysis. {ECO:0000250}.
FT   STRAND        3      5       {ECO:0000244|PDB:1HQS}.
FT   STRAND        8     10       {ECO:0000244|PDB:1HQS}.
FT   STRAND       13     15       {ECO:0000244|PDB:1HQS}.
FT   STRAND       18     25       {ECO:0000244|PDB:1HQS}.
FT   HELIX        31     50       {ECO:0000244|PDB:1HQS}.
FT   STRAND       57     60       {ECO:0000244|PDB:1HQS}.
FT   HELIX        65     71       {ECO:0000244|PDB:1HQS}.
FT   HELIX        77     86       {ECO:0000244|PDB:1HQS}.
FT   STRAND       88     91       {ECO:0000244|PDB:1HQS}.
FT   STRAND       98    102       {ECO:0000244|PDB:1HQS}.
FT   HELIX       105    112       {ECO:0000244|PDB:1HQS}.
FT   STRAND      117    123       {ECO:0000244|PDB:1HQS}.
FT   STRAND      131    133       {ECO:0000244|PDB:1HQS}.
FT   HELIX       135    137       {ECO:0000244|PDB:1HQS}.
FT   STRAND      139    145       {ECO:0000244|PDB:1HQS}.
FT   HELIX       149    152       {ECO:0000244|PDB:1HQS}.
FT   HELIX       161    173       {ECO:0000244|PDB:1HQS}.
FT   HELIX       182    184       {ECO:0000244|PDB:1HQS}.
FT   STRAND      185    193       {ECO:0000244|PDB:1HQS}.
FT   HELIX       194    211       {ECO:0000244|PDB:1HQS}.
FT   STRAND      214    220       {ECO:0000244|PDB:1HQS}.
FT   TURN        222    224       {ECO:0000244|PDB:1HQS}.
FT   TURN        226    228       {ECO:0000244|PDB:1HQS}.
FT   HELIX       229    244       {ECO:0000244|PDB:1HQS}.
FT   HELIX       245    247       {ECO:0000244|PDB:1HQS}.
FT   STRAND      248    250       {ECO:0000244|PDB:1HQS}.
FT   HELIX       251    275       {ECO:0000244|PDB:1HQS}.
FT   STRAND      279    285       {ECO:0000244|PDB:1HQS}.
FT   HELIX       286    295       {ECO:0000244|PDB:1HQS}.
FT   HELIX       297    299       {ECO:0000244|PDB:1HQS}.
FT   STRAND      301    305       {ECO:0000244|PDB:1HQS}.
FT   HELIX       307    320       {ECO:0000244|PDB:1HQS}.
FT   TURN        324    326       {ECO:0000244|PDB:1HQS}.
FT   STRAND      328    332       {ECO:0000244|PDB:1HQS}.
FT   TURN        334    336       {ECO:0000244|PDB:1HQS}.
FT   STRAND      339    344       {ECO:0000244|PDB:1HQS}.
FT   HELIX       349    351       {ECO:0000244|PDB:1HQS}.
FT   TURN        352    355       {ECO:0000244|PDB:1HQS}.
FT   HELIX       360    373       {ECO:0000244|PDB:1HQS}.
FT   HELIX       376    391       {ECO:0000244|PDB:1HQS}.
FT   HELIX       397    400       {ECO:0000244|PDB:1HQS}.
FT   STRAND      403    405       {ECO:0000244|PDB:1HQS}.
FT   HELIX       411    420       {ECO:0000244|PDB:1HQS}.
SQ   SEQUENCE   423 AA;  46418 MW;  CC69E694EB66D0D8 CRC64;
     MAQGEKITVS NGVLNVPNNP IIPFIEGDGT GPDIWNAASK VLEAAVEKAY KGEKKITWKE
     VYAGEKAYNK TGEWLPAETL DVIREYFIAI KGPLTTPVGG GIRSLNVALR QELDLFVCLR
     PVRYFTGVPS PVKRPEDTDM VIFRENTEDI YAGIEYAKGS EEVQKLISFL QNELNVNKIR
     FPETSGIGIK PVSEEGTSRL VRAAIDYAIE HGRKSVTLVH KGNIMKFTEG AFKNWGYELA
     EKEYGDKVFT WAQYDRIAEE QGKDAANKAQ SEAEAAGKII IKDSIADIFL QQILTRPNEF
     DVVATMNLNG DYISDALAAQ VGGIGIAPGA NINYETGHAI FEATHGTAPK YAGLDKVNPS
     SVILSGVLLL EHLGWNEAAD LVIKSMEKTI ASKVVTYDFA RLMDGATEVK CSEFGEELIK
     NMD
//
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