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E6ULW2

- E6ULW2_CLOTL

UniProt

E6ULW2 - E6ULW2_CLOTL

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Protein
Isocitrate dehydrogenase [NADP]
Gene
Clo1313_1944
Organism
Clostridium thermocellum (strain DSM 1313 / LMG 6656 / LQ8)
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 magnesium or manganese ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771Substrate By similarityUniRule annotation
Binding sitei109 – 1091Substrate By similarityUniRule annotation
Binding sitei132 – 1321Substrate By similarityUniRule annotation
Sitei139 – 1391Critical for catalysis By similarityUniRule annotation
Sitei210 – 2101Critical for catalysis By similarityUniRule annotation
Metal bindingi250 – 2501Magnesium or manganese By similarityUniRule annotation
Metal bindingi273 – 2731Magnesium or manganese By similarityUniRule annotation

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB-EC
  3. magnesium ion binding Source: InterPro

GO - Biological processi

  1. isocitrate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, ManganeseUniRule annotation, Metal-bindingUniRule annotation, NADPUniRule annotation

Enzyme and pathway databases

BioCyciCTHE637887:GLBN-1992-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NADP]UniRule annotation (EC:1.1.1.42UniRule annotation)
Gene namesi
Ordered Locus Names:Clo1313_1944Imported
OrganismiClostridium thermocellum (strain DSM 1313 / LMG 6656 / LQ8)Imported
Taxonomic identifieri637887 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000008083: Chromosome

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AOYX-ray2.35A/B/C/D1-402[»]
ProteinModelPortaliE6ULW2.
SMRiE6ULW2. Positions 3-401.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 1007Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK00031.
OMAiKNTIMKV.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11822. PTHR11822. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E6ULW2-1 [UniParc]FASTAAdd to Basket

« Hide

MSKIKMKVPL VEMDGDEMTR IIWRLIKENL LEPYIELNTE YYDLGLENRD    50
KTEDQVTIDA ARAIQKYGVG VKCATITPNA QRVEEYNLKK MWKSPNGTIR 100
AILDGTVFRA PIVVNSIKPF VKGWKKPISI ARHAYGDVYK NVEYYVPSAG 150
KAELVFTSEN GEVSRQTIHE FDGPGVIMGM HNTDKSIRSF ARACFNYALD 200
MNQDLWFSTK DTISKTYDHR FKDIFQEIYE NEYKEKFEAK NLQYFYTLID 250
DAVARIIRSE GGMVWACKNY DGDVMSDMVA SAFGSLAMMT SVLVSPDGKY 300
EFEAAHGTVT RHYYKHLKGE ETSTNSMATI FAWTGALKKR GELDGIKELV 350
DFATKLEQAS VQTIENGVMT KDLASLSEVP EKKIVNTEDF LKEIRKTFEG 400
MA 402
Length:402
Mass (Da):45,782
Last modified:March 8, 2011 - v1
Checksum:i5A55781A7AC5B42E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002416 Genomic DNA. Translation: ADU74991.1.
RefSeqiYP_005688442.1. NC_017304.1.

Genome annotation databases

EnsemblBacteriaiADU74991; ADU74991; Clo1313_1944.
GeneIDi12421679.
KEGGictx:Clo1313_1944.
PATRICi45478813. VBICloThe140364_2116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002416 Genomic DNA. Translation: ADU74991.1 .
RefSeqi YP_005688442.1. NC_017304.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AOY X-ray 2.35 A/B/C/D 1-402 [» ]
ProteinModelPortali E6ULW2.
SMRi E6ULW2. Positions 3-401.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADU74991 ; ADU74991 ; Clo1313_1944 .
GeneIDi 12421679.
KEGGi ctx:Clo1313_1944.
PATRICi 45478813. VBICloThe140364_2116.

Phylogenomic databases

KOi K00031.
OMAi KNTIMKV.

Enzyme and pathway databases

BioCyci CTHE637887:GLBN-1992-MONOMER.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view ]
PANTHERi PTHR11822. PTHR11822. 1 hit.
Pfami PF00180. Iso_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsi TIGR00127. nadp_idh_euk. 1 hit.
PROSITEi PS00470. IDH_IMDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 1313 / LMG 6656 / LQ8.
  2. "The complex structures of isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila suggest a new active site locking mechanism."
    Leiros H.K., Fedoy A.E., Leiros I., Steen I.H.
    FEBS Open Bio 2:159-172(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).

Entry informationi

Entry nameiE6ULW2_CLOTL
AccessioniPrimary (citable) accession number: E6ULW2
Entry historyi
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: September 3, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome

External Data

Dasty 3

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