SMART: Iso_dh domain annotation

The domain within your query sequence starts at position 33 and ends at position 358; the E-value for the Iso_dh domain shown below is 1.37e-169.

TVTLIPGDGIGPEISASVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKESMDKNK
MGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGE
YSGIEHVIVDGVVQSIKLITEEASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFL
QKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGV
TPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAAKIEAACF
ATIKDGKSLTKDLGGNAKCSDFTEEI

Iso_dh Isocitrate/isopropylmalate dehydrogenase

SMART accession number:	SM01329
Description:	Isocitrate dehydrogenase (IDH), is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate.
Interpro abstract (IPR024084):	This entry represents a structural domain found in all types of isocitrate dehydrogenase, and in isopropylmalate dehydrogenase and tartrate dehydrogenase. The crystal structure of Escherichia coli isopropylmalate dehydrogenase has been described [ (PUBMED:9086278) ]. The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate dehydrogenase (IMDH) and tartrate dehydrogenase. IDH is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate [ (PUBMED:2682654) (PUBMED:1939242) ]. IDH is either dependent on NAD ⁺ ( EC 1.1.1.41 ) or on NADP ⁺ ( EC 1.1.1.42 ). In eukaryotes there are at least three isozymes of IDH: two are located in the mitochondrial matrix (one NAD ⁺ -dependent, the other NADP ⁺ -dependent), while the third one (also NADP ⁺ -dependent) is cytoplasmic. In Escherichia coli, the activity of a NADP ⁺ -dependent form of the enzyme is controlled by the phosphorylation of a serine residue; the phosphorylated form of IDH is completely inactivated. IMDH ( EC 1.1.1.85 ) catalyses the third step in the biosynthesis of leucine in bacteria and fungi, the oxidative decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate [ (PUBMED:1748999) (PUBMED:7773180) ]. Tartrate dehydrogenase ( EC 1.1.1.93 ) shows strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser extent, isocitrate dehydrogenase [ (PUBMED:8053675) ]. It catalyses the reduction of tartrate to oxaloglycolate [ (PUBMED:8053675) ].
GO process:	oxidation-reduction process (GO:0055114)
GO function:	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)
Family alignment:	View or

There are 52899 Iso_dh domains in 52895 proteins in SMART's nrdb database.

Click on the following links for more information.

Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Iso_dh domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Iso_dh domain is also avaliable.

Click on the protein counts, or double click on taxonomic names to display all proteins containing Iso_dh domain in the selected taxonomic class.
Cellular role (predicted cellular role)
Cellular role: metabolism
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Cupp JR, McAlister-Henn L
- NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, anddisruption of the IDH2 gene from Saccharomyces cerevisiae.
- J Biol Chem. 1991; 266: 22199-205
- Display abstract
- NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae iscomposed of two nonidentical subunits, designated IDH1 (Mr approximately 40,000) and IDH2 (Mr approximately 39,000). We have isolated and characterized a yeastgenomic clone containing the IDH2 gene. The amino acid sequence deduced from the gene indicates that IDH2 is synthesized as a precursor of 369 amino acids (Mr39,694) and is processed upon mitochondrial import to yield a mature protein of354 amino acids (Mr 37,755). Amino acid sequence comparison between S. cerevisiaeIDH2 and S. cerevisiae NADP(+)-dependent isocitrate dehydrogenase shows nosignificant sequence identity, whereas comparison of IDH2 and Escherichia coliNADP(+)-dependent isocitrate dehydrogenase reveals a 33% sequence identity. Toconfirm the identity of the IDH2 gene and examine the relationship between IDH1and IDH2, the IDH2 gene was disrupted by genomic replacement in a haploid yeaststrain. The disruption strain expressed no detectable IDH2, as determined byWestern blot analysis, and was found to lack NAD(+)-dependent isocitratedehydrogenase activity, indicating that IDH2 is essential for a functionalenzyme. Overexpression of IDH2, however, did not result in increasedNAD(+)-dependent isocitrate dehydrogenase activity, suggesting that both IDH1 andIDH2 subunits are required for catalytic activity. The disruption strain wasunable to utilize acetate as a carbon source and exhibited a 2-fold slower growthrate than wild type strains on glycerol or lactate. This growth phenotype isconsistent with NAD(+)-dependent isocitrate dehydrogenase performing an essentialrole in the oxidative function of the citric acid cycle.
- Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM
- Structure of a bacterial enzyme regulated by phosphorylation, isocitratedehydrogenase.
- Proc Natl Acad Sci U S A. 1989; 86: 8635-9
- Display abstract
- The structure of isocitrate dehydrogenase [threo-DS-isocitrate: NADP+oxidoreductase (decarboxylating), EC 1.1.1.42] from Escherichia coli has beensolved and refined at 2.5 A resolution and is topologically different from thatof any other dehydrogenase. This enzyme, a dimer of identical 416-residuesubunits, is inactivated by phosphorylation at Ser-113, which lies at the edge ofan interdomain pocket that also contains many residues conserved betweenisocitrate dehydrogenase and isopropylmalate dehydrogenase. Isocitratedehydrogenase contains an unusual clasp-like domain in which both polypeptidechains in the dimer interlock. Based on the structure of isocitrate dehydrogenaseand conservation with isopropylmalate dehydrogenase, we suggest that the activesite lies in an interdomain pocket close to the phosphorylation site.
Structure (3D structures containing this domain)

3D Structures of Iso_dh domains in PDB

PDB code	Main view	Title
1a05		CRYSTAL STRUCTURE OF THE COMPLEX OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THIOBACILLUS FERROOXIDANS WITH 3-ISOPROPYLMALATE
1ai2		ISOCITRATE DEHYDROGENASE COMPLEXED WITH ISOCITRATE, NADP+, AND CALCIUM (FLASH-COOLED)
1ai3		ORBITAL STEERING IN THE CATALYTIC POWER OF ENZYMES: SMALL STRUCTURAL CHANGES WITH LARGE CATALYTIC CONSEQUENCES
1bl5		ISOCITRATE DEHYDROGENASE FROM E. COLI SINGLE TURNOVER LAUE STRUCTURE OF RATE-LIMITED PRODUCT COMPLEX, 10 MSEC TIME RESOLUTION
1cm7		3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI
1cnz		3-ISOPROPYLMALATE DEHYDROGENASE (IPMDH) FROM SALMONELLA TYPHIMURIUM
1cw1		CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE MUTANT K230M BOUND TO ISOCITRATE AND MN2+
1cw4		CRYSTAL STRUCTURE OF K230M ISOCITRATE DEHYDROGENASE IN COMPLEX WITH ALPHA-KETOGLUTARATE
1cw7		LOW TEMPERATURE STRUCTURE OF WILD-TYPE IDH COMPLEXED WITH MG-ISOCITRATE
1dpz		STUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD711
1dr0		STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD708
1dr8		STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177
1g2u		THE STRUCTURE OF THE MUTANT, A172V, OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THERMUS THERMOPHILUS HB8 : ITS THERMOSTABILITY AND STRUCTURE.
1gc8		THE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS 3-ISOPROPYLMALATE DEHYDROGENASE MUTATED AT 172TH FROM ALA TO PHE
1gc9		THE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS 3-ISOPROPYLMALATE DEHYDROGENASE MUTATED AT 172TH FROM ALA TO GLY
1gro		REGULATORY AND CATALYTIC MECHANISMS IN ESCHERICHIA COLI ISOCITRATE DEHYDROGENASE: MULTIPLE ROLES FOR N115
1grp		REGULATORY AND CATALYTIC MECHANISMS IN ESCHERICHIA COLI ISOCITRATE DEHYDROGENASE: MULTIPLE ROLES FOR N115
1hex		STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE IN COMPLEX WITH NAD+: LIGAND-INDUCED LOOP-CLOSING AND MECHANISM FOR COFACTOR SPECIFICITY
1hj6		ISOCITRATE DEHYDROGENASE S113E MUTANT COMPLEXED WITH ISOPROPYLMALATE, NADP+ AND MAGNESIUM (FLASH-COOLED)
1hqs		CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE FROM BACILLUS SUBTILIS
1idc		ISOCITRATE DEHYDROGENASE FROM E.COLI (MUTANT K230M), STEADY-STATE INTERMEDIATE COMPLEX DETERMINED BY LAUE CRYSTALLOGRAPHY
1idd		ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME
1ide		ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)
1idf		ISOCITRATE DEHYDROGENASE K230M MUTANT APO ENZYME
1idm		3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA
1ika		STRUCTURE OF ISOCITRATE DEHYDROGENASE WITH ALPHA-KETOGLUTARATE AT 2.7 ANGSTROMS RESOLUTION: CONFORMATIONAL CHANGES INDUCED BY DECARBOXYLATION OF ISOCITRATE
1ipd		THREE-DIMENSIONAL STRUCTURE OF A HIGHLY THERMOSTABLE ENZYME, 3-ISOPROPYLMALATE DEHYDROGENASE OF THERMUS THERMOPHILUS AT 2.2 ANGSTROMS RESOLUTION
1iso		ISOCITRATE DEHYDROGENASE: STRUCTURE OF AN ENGINEERED NADP+--> NAD+ SPECIFICITY-REVERSAL MUTANT
1lwd		CRYSTAL STRUCTURE OF NADP-DEPENDENT ISOCITRATE DEHYDROGENASE FROM PORCINE HEART MITOCHONDRIA
1osi		STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE
1osj		STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE
1p8f		A four location model to explain the stereospecificity of proteins.
1pb1		A four location model to explain the stereospecificity of proteins.
1pb3		Sites of binding and orientation in a four location model for protein stereospecificity.
1sjs		ACCESS TO PHOSPHORYLATION IN ISOCITRATE DEHYDROGENASE MAY OCCUR BY DOMAIN SHIFTING
1t09		Crystal structure of human cytosolic NADP(+)-dependent isocitrate dehydrogenase in complex NADP
1t0l		Crystal structure of human cytosolic NADP(+)-dependent isocitrate dehydrogenase in complex with NADP, isocitrate, and calcium(2+)
1tyo		Isocitrate Dehydrogenase from the hyperthermophile Aeropyrum pernix in complex with etheno-NADP
1v53		The crystal structure of 3-isopropylmalate dehydrogenase from Bacillus coagulans
1v5b		The Structure Of The Mutant, S225A and E251L, Of 3-Isopropylmalate Dehydrogenase From Bacillus Coagulans
1v94		Crystal structure of isocitrate dehydrogenase from Aeropyrum pernix
1vlc		Crystal structure of 3-isopropylmalate dehydrogenase (TM0556) from Thermotoga maritima at 1.90 A resolution
1w0d		The high resolution structure of Mycobacterium tuberculosis LeuB (Rv2995c)
1wal		3-ISOPROPYLMALATE DEHYDROGENASE (IPMDH) MUTANT (M219A)FROM THERMUS THERMOPHILUS
1wpw		Crystal Structure of IPMDH from Sulfolobus tokodaii
1x0l		Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus
1xaa		3-ISOPROPYLMALATE DEHYDROGENASE, LOW TEMPERATURE (100K) STRUCTURE
1xab		3-ISOPROPYLMALATE DEHYDROGENASE, LOW TEMPERATURE (150K) STRUCTURE
1xac		CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE.
1xad		CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (150K) STRUCTURE.
1xgv		Isocitrate Dehydrogenase from the hyperthermophile Aeropyrum pernix
1xkd		Ternary complex of Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix
1zor		Isocitrate dehydrogenase from the hyperthermophile Thermotoga maritima
2ayq		3-ISOPROPYLMALATE DEHYDROGENASE FROM THE MODERATE FACULTATIVE THERMOPHILE, BACILLUS COAGULANS
2cmj		Crystal Structure of Mouse Cytosolic Isocitrate Dehydrogenase
2cmv		Crystal Structure of Mouse Cytosolic Isocitrate Dehydrogenase complexed with Cadmium and citrate
2d1c		Crystal Structure Of TT0538 protein from Thermus thermophilus HB8
2d4v		Crystal structure of NAD dependent isocitrate dehydrogenase from Acidithiobacillus thiooxidans
2dht		Crystal structure of isocitrate dehydrogenase from Sulfolobus tokodaii strain7
2e0c		crystal structure of isocitrate dehydrogenase from Sulfolobus tokodaii strain7 at 2.0 A resolution
2e5m		Crystal structure of isocitrate dehydrogenase from Sulfolobus tokodaii strain 7
2g4o		anomalous substructure of 3-ISOPROPYLMALATE DEHYDROGENASE
2iv0		Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers.
2qfv		Crystal structure of Saccharomyces cerevesiae mitochondrial NADP(+)-dependent isocitrate dehydrogenase in complex with NADP(+)
2qfw		Crystal structure of Saccharomyces cerevesiae mitochondrial NADP(+)-dependent isocitrate dehydrogenase in complex with isocitrate
2qfx		Crystal structure of Saccharomyces cerevesiae mitochondrial NADP(+)-dependent isocitrate dehydrogenase in complex with NADPH, a-ketoglutarate and Ca(2+)
2qfy		Crystal structure of Saccharomyces cerevesiae mitochondrial NADP(+)-dependent isocitrate dehydrogenase in complex with a-ketoglutarate
2uxq		Isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila: biochemical properties and crystal structure analysis
2uxr		Complex with isocitrate and the protein isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila
2y3z		Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - apo enzyme
2y40		Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - complex with Mn
2y41		Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - complex with IPM and MN
2y42		Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - complex with NADH and Mn
2ztw		Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+
3ah3		Crystal structure of LR5-1, 3-isopropylmalate dehydrogenase created by directed evolution
3asj		Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor
3blv		Yeast Isocitrate Dehydrogenase with Citrate Bound in the Regulatory Subunits
3blw		Yeast Isocitrate Dehydrogenase with Citrate and AMP Bound in the Regulatory Subunits
3blx		Yeast Isocitrate Dehydrogenase (Apo Form)
3dms		1.65A crystal structure of isocitrate dehydrogenase from Burkholderia pseudomallei
3flk		Crystal Structure of Tartrate Dehydrogenase from Pseudomonas putida in complex with NADH, oxalate and metal ion
3fmx		Crystal structure of Tartrate dehydrogenase from Pseudomonas putida complexed with NADH
3icd		STRUCTURE OF A BACTERIAL ENZYME REGULATED BY PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE
3inm		Crystal structure of human cytosolic NADP(+)-dependent isocitrate dehydrogenase R132H mutant in complex with NADPH, ALPHA-KETOGLUTARATE and CALCIUM(2+)
3lcb		The crystal structure of isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli.
3map		Crystal structure of homodimeric R132H mutant of human cytosolic NADP(+)-dependent isocitrate dehydrogenase in complex with NADP and isocitrate
3mar		Crystal structure of homodimeric R132H mutant of human cytosolic NADP(+)-dependent isocitrate dehydrogenase in complex with NADP
3mas		Crystal structure of heterodimeric R132H mutant of human cytosolic NADP(+)-dependent isocitrate dehydrogenase in complex with NADP and isocitrate
3r8w		Structure of 3-isopropylmalate dehydrogenase isoform 2 from Arabidopsis thaliana at 2.2 angstrom resolution
3ty3		Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe bound to glycyl-glycyl-glycine
3ty4		Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe
3u1h		Crystal structure of IPMDH from the last common ancestor of Bacillus
3udo		Crystal structure of putative isopropylamlate dehydrogenase from Campylobacter jejuni
3udu		Crystal structure of putative 3-isopropylmalate dehydrogenase from Campylobacter jejuni
3us8		Crystal Structure of an isocitrate dehydrogenase from Sinorhizobium meliloti 1021
3vkz		3-isopropylmalate dehydrogenase from Shewanella oneidensis MR-1 at atmospheric pressure
3vl2		3-isopropylmalate dehydrogenase from Shewanella oneidensis MR-1 at 160 MPa
3vl3		3-isopropylmalate dehydrogenase from Shewanella oneidensis MR-1 at 340 MPa
3vl4		3-isopropylmalate dehydrogenase from Shewanella oneidensis MR-1 at 410 MPa
3vl6		3-isopropylmalate dehydrogenase from Shewanella oneidensis MR-1 at 580 MPa
3vl7		3-isopropylmalate dehydrogenase from Shewanella oneidensis MR-1 at 650 MPa
3vmj		3-isopropylmalate dehydrogenase from Shewanella oneidensis MR-1
3vmk		3-isopropylmalate dehydrogenase from Shewanella benthica DB21 MT-2
3vml		Chimera 3-isopropylmalate dehydrogenase between Shewanella oneidensis MR-1 (O) and Shewanella benthica DB21 MT-2 (M) from N-terminal: 20% O middle 70% M residual 10% O
3wzv		3WZV
3wzw		3WZW
3wzx		3WZX
3wzy		3WZY
4aj3		3D structure of E. coli Isocitrate Dehydrogenase in complex with Isocitrate, calcium(II) and NADP - The pseudo-Michaelis complex
4aja		3D structure of E. coli Isocitrate Dehydrogenase in complex with Isocitrate, calcium(II) and thioNADP
4ajb		3D structure of E. coli Isocitrate Dehydrogenase K100M mutant in complex with Isocitrate, calcium(II) and thioNADP
4ajc		3D structure of E. coli Isocitrate Dehydrogenase K100M mutant in complex with alpha-ketoglutarate, calcium(II) and adenine nucleotide phosphate
4ajr		3D structure of E. coli Isocitrate Dehydrogenase K100M mutant in complex with alpha-ketoglutarate, magnesium(II) and NADPH - The product complex
4ajs		3D structure of E. coli Isocitrate Dehydrogenase K100M mutant in complex with isocitrate, magnesium(II), Adenosine 2',5'-biphosphate and ribosylnicotinamide-5'-phosphate
4aou		CtIDH bound to NADP. The complex structures of Isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila, support a new active site locking mechanism
4aov		DpIDH-NADP. The complex structures of Isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila, support a new active site locking mechanism
4aoy		Open CtIDH. The complex structures of Isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila, support a new active site locking mechanism
4bnp		3D structure of E. coli Isocitrate Dehydrogenase K100M mutant in complex with isocitrate and magnesium(II)
4f7i		Structure of Isopropylmalate dehydrogenase from Thermus thermophilus in complex with IPM, Mn and NADH
4hcx		Structure of ICDH-1 from M.tuberculosis complexed with NADPH & Mn2+
4i3k		Crystal structure of a metabolic reductase with 1-hydroxy-6-(4-hydroxybenzyl)-4-methylpyridin-2(1H)-one
4i3l		Crystal structure of a metabolic reductase with 6-benzyl-1-hydroxy-4-methylpyridin-2(1H)-one
4icd		REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME
4iwh		Crystal structure of a 3-isopropylmalate dehydrogenase from Burkholderia pseudomallei
4ja8		Complex of Mitochondrial Isocitrate Dehydrogenase R140Q Mutant with AGI-6780 Inhibitor
4kzo		Crystal Structure Analysis of human IDH1 mutants in complex with NADP+ and Ca2+/alpha-Ketoglutarate
4l03		Crystal Structure Analysis of human IDH1 mutants in complex with NADP+ and Ca2+/alpha-Ketoglutarate
4l04		Crystal Structure Analysis of human IDH1 mutants in complex with NADP+ and Ca2+/alpha-Ketoglutarate
4l06		Crystal Structure Analysis of human IDH1 mutants in complex with NADP+ and Ca2+/alpha-Ketoglutarate
4p69		4P69
4umx		4UMX
4umy		4UMY
4wuo		4WUO
4xrx		4XRX
4xs3		4XS3
4xxv		4XXV
4y1p		4Y1P
4yb4		4YB4
5de1		5DE1
5icd		REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE
5j32		5J32
5j33		5J33
5j34		5J34
5k10		5K10
5k11		5K11
6icd		REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE
7icd		REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE
8icd		REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE
9icd		CATALYTIC MECHANISM OF NADP+-DEPENDENT ISOCITRATE DEHYDROGENASE: IMPLICATIONS FROM THE STRUCTURES OF MAGNESIUM-ISOCITRATE AND NADP+ COMPLEXES

Links (links to other resources describing this domain)
PFAM Iso_dh
INTERPRO IPR024084

PFAM	Iso_dh
INTERPRO	IPR024084

The domain within your query sequence starts at position 33 and ends at position 358; the E-value for the Iso_dh domain shown below is 1.37e-169.

Iso_dh

Taxonomic distribution of proteins containing Iso_dh domain.

3D Structures of Iso_dh domains in PDB