Skip Header

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

A3DC45 (A3DC45_CLOTH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 47. Feed History...

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

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP] PIRNR PIRNR000108

EC=1.1.1.42 PIRNR PIRNR000108
Gene names
Ordered Locus Names:Cthe_0285
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP] EMBL ABN51524.1
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH. PIRNR PIRNR000108

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity. PIRNR PIRNR000108 PIRSR PIRSR000108-3

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family. PIRNR PIRNR000108 RuleBase RU004443

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region94 – 1007Substrate binding By similarity PIRSR PIRSR000108-2

Sites

Metal binding2501Magnesium or manganese By similarity PIRSR PIRSR000108-3
Metal binding2731Magnesium or manganese By similarity PIRSR PIRSR000108-3
Binding site771Substrate By similarity PIRSR PIRSR000108-2
Binding site1091Substrate By similarity PIRSR PIRSR000108-2
Binding site1321Substrate By similarity PIRSR PIRSR000108-2
Site1391Critical for catalysis By similarity PIRSR PIRSR000108-1
Site2101Critical for catalysis By similarity PIRSR PIRSR000108-1

Sequences

Sequence LengthMass (Da)Tools
A3DC45 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 5A55781A7AC5B42E

FASTA40245,782
        10         20         30         40         50         60 
MSKIKMKVPL VEMDGDEMTR IIWRLIKENL LEPYIELNTE YYDLGLENRD KTEDQVTIDA 

        70         80         90        100        110        120 
ARAIQKYGVG VKCATITPNA QRVEEYNLKK MWKSPNGTIR AILDGTVFRA PIVVNSIKPF 

       130        140        150        160        170        180 
VKGWKKPISI ARHAYGDVYK NVEYYVPSAG KAELVFTSEN GEVSRQTIHE FDGPGVIMGM 

       190        200        210        220        230        240 
HNTDKSIRSF ARACFNYALD MNQDLWFSTK DTISKTYDHR FKDIFQEIYE NEYKEKFEAK 

       250        260        270        280        290        300 
NLQYFYTLID DAVARIIRSE GGMVWACKNY DGDVMSDMVA SAFGSLAMMT SVLVSPDGKY 

       310        320        330        340        350        360 
EFEAAHGTVT RHYYKHLKGE ETSTNSMATI FAWTGALKKR GELDGIKELV DFATKLEQAS 

       370        380        390        400 
VQTIENGVMT KDLASLSEVP EKKIVNTEDF LKEIRKTFEG MA 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of Clostridium thermocellum ATCC 27405."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27405 / DSM 1237.
[2]"The Complex Structures of Isocitrate Dehydrogenase from Clostridium Thermocellum and Desulfotalea Psychrophila, Support a New Active Site Locking Mechanism."
Leiros H.-K.S., Fedoy A.-E., Leiros I., Steen I.H.
Submitted (MAR-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000568 Genomic DNA. Translation: ABN51524.1.
RefSeqYP_001036717.1. NC_009012.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AOUX-ray2.50A1-402[»]
ProteinModelPortalA3DC45.
SMRA3DC45. Positions 3-401.
ModBaseSearch...

Protein-protein interaction databases

STRING203119.Cthe_0285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN51524; ABN51524; Cthe_0285.
GeneID4808568.
KEGGcth:Cthe_0285.
PATRIC19514209. VBICloThe47081_0302.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0538.
HOGENOMHOG000019858.
KOK00031.
OMAQHQQGKP.
ProtClustDBPRK08299.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-293-MONOMER.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11822. PTHR11822. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA3DC45_CLOTH
AccessionPrimary (citable) accession number: A3DC45
Entry history
Integrated into UniProtKB/TrEMBL: March 20, 2007
Last sequence update: March 20, 2007
Last modified: May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)