Skip Header

Contribute Send feedback
Read comments (?) or add your own

P50216 (IDH_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP]
Short name=IDH
EC=1.1.1.42
Alternative name(s):
Oxalosuccinate decarboxylase
Gene names
Name:icd
Ordered Locus Names:Cgl0664, cg0766
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length738 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

Cofactor

Binds 1 magnesium or manganese ion per subunit.

Enzyme regulation

Weakly inhibited by oxaloacetate, 2-oxoglutarate, and citrate. Severely inhibited by oxaloacetate plus glyoxylate.

Subunit structure

Monomer. Ref.4

Sequence similarities

Belongs to the monomeric-type IDH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 738738Isocitrate dehydrogenase [NADP]
PRO_0000083595

Regions

Nucleotide binding80 – 856NADP By similarity
Nucleotide binding580 – 5812NADP By similarity
Nucleotide binding596 – 5983NADP By similarity
Region130 – 1378Substrate binding By similarity

Sites

Metal binding3461Magnesium or manganese
Metal binding5441Magnesium or manganese
Metal binding5481Magnesium or manganese
Binding site1331NADP By similarity
Binding site1431Substrate By similarity
Binding site5431Substrate By similarity
Binding site5851NADP By similarity
Binding site6451NADP By similarity
Site2531Critical for catalysis By similarity
Site4161Critical for catalysis By similarity

Secondary structure

1 .......................................................................................................................... 738
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50216 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EAC4C5FA38C33F63

FASTA73880,081
        10         20         30         40         50         60 
MAKIIWTRTD EAPLLATYSL KPVVEAFAAT AGIEVETRDI SLAGRILAQF PERLTEDQKV 

        70         80         90        100        110        120 
GNALAELGEL AKTPEANIIK LPNISASVPQ LKAAIKELQD QGYDIPELPD NATTDEEKDI 

       130        140        150        160        170        180 
LARYNAVKGS AVNPVLREGN SDRRAPIAVK NFVKKFPHRM GEWSADSKTN VATMDANDFR 

       190        200        210        220        230        240 
HNEKSIILDA ADEVQIKHIA ADGTETILKD SLKLLEGEVL DGTVLSAKAL DAFLLEQVAR 

       250        260        270        280        290        300 
AKAEGILFSA HLKATMMKVS DPIIFGHVVR AYFADVFAQY GEQLLAAGLN GENGLAAILS 

       310        320        330        340        350        360 
GLESLDNGEE IKAAFEKGLE DGPDLAMVNS ARGITNLHVP SDVIVDASMP AMIRTSGHMW 

       370        380        390        400        410        420 
NKDDQEQDTL AIIPDSSYAG VYQTVIEDCR KNGAFDPTTM GTVPNVGLMA QKAEEYGSHD 

       430        440        450        460        470        480 
KTFRIEADGV VQVVSSNGDV LIEHDVEAND IWRACQVKDA PIQDWVKLAV TRSRLSGMPA 

       490        500        510        520        530        540 
VFWLDPERAH DRNLASLVEK YLADHDTEGL DIQILSPVEA TQLSIDRIRR GEDTISVTGN 

       550        560        570        580        590        600 
VLRDYNTDLF PILELGTSAK MLSVVPLMAG GGLFETGAGG SAPKHVQQVQ EENHLRWDSL 

       610        620        630        640        650        660 
GEFLALAESF RHELNNNGNT KAGVLADALD KATEKLLNEE KSPSRKVGEI DNRGSHFWLT 

       670        680        690        700        710        720 
KFWADELAAQ TEDADLAATF APVAEALNTG AADIDAALLA VQGGATDLGG YYSPNEEKLT 

       730 
NIMRPVAQFN EIVDALKK

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence analysis, expression, and inactivation of the Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and biochemical characterization of the enzyme."
Eikmanns B.J., Rittmann D., Sahm H.
J. Bacteriol. 177:774-782(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"Substrate-free structure of a monomeric NADP isocitrate dehydrogenase: an open conformation phylogenetic relationship of isocitrate dehydrogenase."
Imabayashi F., Aich S., Prasad L., Delbaere L.T.
Proteins 63:100-112(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X71489 Genomic DNA. Translation: CAA50590.1.
BA000036 Genomic DNA. Translation: BAB98057.1.
BX927149 Genomic DNA. Translation: CAF19369.1.
PIRI40719.
RefSeqNP_599896.1. NC_003450.3.
YP_224955.1. NC_006958.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B0TX-ray1.75A1-738[»]
3MBCX-ray1.90A/B1-738[»]
ProteinModelPortalP50216.
SMRP50216. Positions 2-736.
ModBaseSearch...

Protein-protein interaction databases

STRING196627.cg0766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98057; BAB98057; BAB98057.
CAF19369; CAF19369; cg0766.
GeneID1018663.
3345662.
KEGGcgb:cg0766.
cgl:NCgl0634.
PATRIC21493369. VBICorGlu203724_0650.

Phylogenomic databases

eggNOGCOG2838.
HOGENOMHOG000240860.
KOK00031.
OMAPRTMGTV.
ProtClustDBCLSK867411.

Family and domain databases

Gene3D3.40.718.10. 3 hits.
InterProIPR004436. Isocitrate_DH_NADP_mono.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PfamPF03971. IDH. 1 hit.
[Graphical view]
PIRSFPIRSF009407. IDH_monmr. 1 hit.
TIGRFAMsTIGR00178. monomer_idh. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP50216.

Entry information

Entry nameIDH_CORGL
AccessionPrimary (citable) accession number: P50216
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 29, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents