Reviewed,
UniProtKB/Swiss-Prot P65097 (IDH_MYCTU)
Last modified
February 9, 2010.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Isocitrate dehydrogenase [NADP] Short name=IDH EC=1.1.1.42 Alternative name(s): Oxalosuccinate decarboxylase NADP(+)-specific ICDH IDP | ||||||
| Gene names |
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| Organism | Mycobacterium tuberculosis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 409 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH. Oxalosuccinate + NADP+ = 2-oxoglutarate + CO2 + NADPH. |
| Cofactor | Binds 1 magnesium or manganese ion per subunit By similarity. |
| Sequence similarities | Belongs to the isocitrate and isopropylmalate dehydrogenases family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glyoxylate bypass Tricarboxylic acid cycle |
| Ligand | Magnesium Manganese Metal-binding NADP |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic processInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NADP+) activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 409 | 409 | Isocitrate dehydrogenase [NADP] | PRO_0000083555 | |||||
Regions | |||||||||
| Nucleotide binding | 78 – 80 | 3 | NADP By similarity | ||||||
| Nucleotide binding | 313 – 318 | 6 | NADP By similarity | ||||||
| Region | 97 – 103 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 255 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 278 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 80 | 1 | Substrate By similarity | ||||||
| Binding site | 85 | 1 | NADP By similarity | ||||||
| Binding site | 112 | 1 | Substrate By similarity | ||||||
| Binding site | 135 | 1 | Substrate By similarity | ||||||
| Binding site | 263 | 1 | NADP By similarity | ||||||
| Binding site | 331 | 1 | NADP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Site | 142 | 1 | Critical for catalysis By similarity | ||||||
| Site | 215 | 1 | Critical for catalysis By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 97 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842582 Genomic DNA. Translation: CAA17111.1. AE000516 Genomic DNA. Translation: AAK47786.1. |
| PIR | B70846. |
| RefSeq | NP_217856.1. NP_337972.1. |
3D structure databases | |
| SMR | P65097. Positions 6-408. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 888013. 926429. |
| GenomeReviews | Gene locus MT3442 in contig AE000516_GR. |
| KEGG | mtc:MT3442. mtu:Rv3339c. |
| TIGR | MT3442. |
Organism-specific databases | |
| TubercuList | Rv3339c. |
Phylogenomic databases | |
| HOGENOM | HBG596047. |
| OMA | KLITPFL. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-11946. |
| BRENDA | 1.1.1.42. 809. |
Family and domain databases | |
| InterPro | IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004790. Isocitrate_DH_NADP-dep_euk. [Graphical view] |
| Gene3D | G3DSA:3.40.718.10. IDH_IMDH. 1 hit. |
| PANTHER | PTHR11822. IDH_NADP_euk. 1 hit. |
| Pfam | PF00180. Iso_dh. 1 hit. [Graphical view] |
| PIRSF | PIRSF000108. IDH_NADP. 1 hit. |
| TIGRFAMs | TIGR00127. nadp_idh_euk. 1 hit. |
| PROSITE | PS00470. IDH_IMDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IDH_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P65097 Secondary accession number(s): O53389 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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