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UniProtKB/Swiss-Prot entry Q68XA5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IDH_RICTY
Primary accession number Q68XA5
Secondary accession numbers None
Integrated into Swiss-Prot on June 21, 2005
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 30)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP]
Synonyms IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
Gene name
Name: icd
OrderedLocusNames: RT0256
From
Rickettsia typhi [TaxID: 785] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-144 / Wilmington;
DOI=10.1128/JB.186.17.5842-5855.2004; PubMed=15317790 [NCBI, ExPASy, EBI, Israel, Japan]
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.;
"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae.";
J. Bacteriol. 186:5842-5855(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE017197; AAU03737.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_067219.1; -.
3D structure databases
ModBase Q68XA5.
Enzyme and pathway databases
BioCyc RTYP257363:RT0256-MON; -.
Ontologies
GO
GO:0004450; Molecular function: isocitrate dehydrogenase (NADP+) activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006097; Biological process: glyoxylate cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001804; IsoCit_IM_DHase.
IPR014273; Isocitrate_DH_bac.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02924; ICDH_alpha; 1.
PROSITE PS00470; IDH_IMDH; 1.
Genome annotation databases
GeneID 2958917; -.
GenomeReviews AE017197_GR; RT0256.
KEGG rty:RT0256; -.
Phylogenomic databases
HOGENOM Q68XA5; -.
Genome annotation databases
CMR Q68XA5; RT0256.
Other
ProtoNet Q68XA5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   483  483     Isocitrate dehydrogenase [NADP]. PRO_0000083558
METAL   208   208        Magnesium or manganese (By similarity). 
METAL   232   232        Magnesium or manganese (By similarity). 
METAL   236   236        Magnesium or manganese (By similarity). 
BINDING   89    89        Substrate (By similarity). 
BINDING   99    99        Substrate (By similarity). 
BINDING   121   121        Substrate (By similarity). 
BINDING   208   208        Substrate (By similarity). 
SITE   128   128  1     Critical for catalysis (By similarity). 
SITE   175   175  1     Critical for catalysis (By similarity). 
MOD_RES   83    83        Phosphoserine (By similarity). 
Sequence information
Length: 483 AA [This is the length of the unprocessed precursor] Molecular weight: 54161 Da [This is the MW of the unprocessed precursor] CRC64: D6AAA410411169AF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAEFTPITIA YGDGIGPEIM DAVLYILRQA EARISLETIE VGEKLYKKHY TSGISEESWN 

        70         80         90        100        110        120 
VIQRTGIILK APITTPQSGG YKSLNVTIRK TLQLFANIRP AVSFHPFTRT LHPNLNLTII 

       130        140        150        160        170        180 
RENEEDLYSG IEYRQTHNMY ESLKLISHTG CKKIIRYAFE YAVKNNRKKV TCLSKDNIMK 

       190        200        210        220        230        240 
FSDGIFHRVF NEIAKEYPQI DNEHYIIDIG TAKLATTPEI FDIIVTSNLY GDIISDVAAE 

       250        260        270        280        290        300 
ISGSVGLAGS ANIGQHYAMF EAVHGSAPDI AGKGIANPSG LLNAAIMMLV HIGQGDIASL 

       310        320        330        340        350        360 
IENAWKKTIE DGVHTFDIYS EHSSSKKVCT KEFAEEVIKR LGQLPMTLPK ASYPLIVKKQ 

       370        380        390        400        410        420 
ESKIEYKIDT TEVKKLVGTD IFINIHVFSA HDIADKINKL DIGNFELKTI SSKGLKLWPH 

       430        440        450        460        470        480 
DLRFEIISDH WCCRFMNKDG TEIKHLDIII LLQALSKANI DFIKVENLFE FDGVACYSLA 


QGE
Q68XA5 in FASTA format

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