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UniProtKB/Swiss-Prot entry O13285

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

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Entry information
Entry name IDH1_CANTR
Primary accession number O13285
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 52)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP], mitochondrial [Precursor]
Synonyms IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
CtIDP1
Gene name
Name: IDP1
From
Candida tropicalis (Yeast) [TaxID: 5482] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 20336 / pK233 / NCYC 997;
DOI=10.1007/s002030050513; PubMed=9325427 [NCBI, ExPASy, EBI, Israel, Japan]
Imajo T., Kawachi H., Atomi H., Sanuki S., Yamamoto S., Ueda M., Tanaka A.;
"Immunochemically distinct NADP-linked isocitrate dehydrogenase isozymes in mitochondria and peroxisomes of Candida tropicalis.";
Arch. Microbiol. 168:389-395(1997).
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
AB004556; BAA22945.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P33198; 1LWD. [HSSP ENTRY / PDB]
SMR O13285; 29-430.
ModBase O13285.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
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:0006102; Biological process: isocitrate metabolic process (inferred from electronic annotation from InterPro).
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 IPR004790; IsoCit_DHase_NADP-dep_euk.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11822; IDH_NADP_euk; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000108; IDH_NADP; 1.
TIGRFAMs TIGR00127; nadp_idh_euk; 1.
PROSITE PS00470; IDH_IMDH; 1.
Other
ProtoNet O13285.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    27  27     Mitochondrion (By similarity). 
CHAIN   28   430  403     Isocitrate dehydrogenase [NADP], mitochondrial. PRO_0000014424
NP_BIND   101   103  3     NADP (By similarity). 
NP_BIND   335   340  6     NADP (By similarity). 
REGION   120   126  7     Substrate binding (By similarity). 
METAL   277   277        Magnesium or manganese (By similarity). 
METAL   300   300        Magnesium or manganese (By similarity). 
BINDING   103   103        Substrate (By similarity). 
BINDING   108   108        NADP (By similarity). 
BINDING   135   135        Substrate (By similarity). 
BINDING   158   158        Substrate (By similarity). 
BINDING   285   285        NADP (By similarity). 
BINDING   353   353        NADP; via amide nitrogen and carbonyl oxygen (By similarity). 
SITE   165   165  1     Critical for catalysis (By similarity). 
SITE   237   237  1     Critical for catalysis (By similarity). 
Sequence information
Length: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 48009 Da [This is the MW of the unprocessed precursor] CRC64: 205A319496F0CCEB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIRASAIQRT AMLLRQLRGF STSATLADKI KVKNPIVELD GDEMTRIIWQ KIKDQLILPY 

        70         80         90        100        110        120 
LDVDLKYYDL GIESRDATDD QITIDAANAI KEYGVGVKCA TITPDEARVK EFHLKKMWLS 

       130        140        150        160        170        180 
PNGTIRNILG GTVFRESIII PCIPRLIPGW EKPIVIGRHA FGDQYKATDL VINEPGRLEL 

       190        200        210        220        230        240 
RFTPASGGEA QTQKVYDYTG PGVGLAMYNT DESITGFAHA SFKMALAKGL PLYMSTKNTI 

       250        260        270        280        290        300 
LKKYDGRFKD IFQQIYEQDY AAEFEKQGLW YEHRLIDDMV AQMIKSKGGF VMALKNYDGD 

       310        320        330        340        350        360 
VQSDIVAQGF GSLGLMTSAL MTPDGKAYEA EAAHGTVTRH YRQHQQGKET STNSIASIFA 

       370        380        390        400        410        420 
WTRGLAQRGK LDETPDVVDF ASKLEQATID TVEVDRIMTK DLALAMGKTD RSAYVTTTEF 

       430 
LDAVADRLKK
O13285 in FASTA format

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