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UniProtKB/Swiss-Prot entry Q9ZH99


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

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Entry information
Entry name IDH_COXBU
Primary accession number Q9ZH99
Secondary accession numbers Q7C3F6 Q9RG62 Q9RG63 Q9RG64 Q9RG65 Q9RG66 Q9RG67 Q9RG68 Q9RG69 Q9RG70 Q9RG71 Q9RG72
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 58)
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: CBU_1200
From
Coxiella burnetii [TaxID: 777] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae; Coxiella.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPTIMAL PH.
STRAIN=Nine Mile I;
DOI=10.1111/j.1574-6968.1999.tb13607.x; PubMed=10361714 [NCBI, ExPASy, EBI, Israel, Japan]
Van Nguyen S., To H., Yamaguchi T., Fukushi H., Hirai K.;
"Molecular cloning of an immunogenic and acid-induced isocitrate dehydrogenase gene from Coxiella burnetii.";
FEMS Microbiol. Lett. 175:101-106(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1M, 27M, 307, 3M, 605, 60M, 82M, Bangui VR 730, El Tayeb RSA 342, GQ212, KoQ229, MAN, ME, Ohio 314 VR 542, Priscilla, SQ217, and TK-1;
DOI=10.1111/j.1574-6968.1999.tb08803.x; PubMed=10556719 [NCBI, ExPASy, EBI, Israel, Japan]
Nguyen S.V., Hirai K.;
"Differentiation of Coxiella burnetii isolates by sequence determination and PCR-restriction fragment length polymorphism analysis of isocitrate dehydrogenase gene.";
FEMS Microbiol. Lett. 180:249-254(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nine Mile phase I / RSA 493;
DOI=10.1073/pnas.0931379100; PubMed=12704232 [NCBI, ExPASy, EBI, Israel, Japan]
Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.;
"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
STRAIN=Nine Mile Crazy / RSA 514;
DOI=10.1128/IAI.00883-06; PubMed=17088354 [NCBI, ExPASy, EBI, Israel, Japan]
Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J., Samuel J.E., Heinzen R.A.;
"Proteome and antigen profiling of Coxiella burnetii developmental forms.";
Infect. Immun. 75:290-298(2007).
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
AF069035; AAC68600.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146284; AAF16725.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146285; AAF16726.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146286; AAF16727.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146287; AAF16728.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146288; AAF16729.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146289; AAF16730.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146290; AAF16731.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146291; AAF16732.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146292; AAF16733.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146293; AAF16734.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146294; AAF16735.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146295; AAF16736.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146296; AAF16737.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146297; AAF16738.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146298; AAF16739.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146299; AAF16740.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146300; AAF16741.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146301; AAF16742.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE016828; AAO90709.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_820195.1; -.
3D structure databases
HSSP P08200; 1PB1. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR Q9ZH99; 15-426.
ModBase Q9ZH99.
Enzyme and pathway databases
BioCyc CBUR227377:CBU_1200-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 InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004439; IsoCit_DHase_NADP_prok.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF1; NADP_IDH_prok; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00183; prok_nadp_idh; 1.
PROSITE PS00470; IDH_IMDH; 1.
ProtoNet Q9ZH99.
Genome annotation databases
GeneID 1209104; -.
GenomeReviews AE016828_GR; CBU_1200.
KEGG cbu:CBU_1200; -.
NMPDR fig|227377.1.peg.1139; -.
TIGR CBU_1200; -.
Phylogenomic databases
HOGENOM Q9ZH99; -.
Other
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   427  427     Isocitrate dehydrogenase [NADP]. PRO_0000323713
NP_BIND   349   355  7     NADP (By similarity). 
METAL   317   317        Magnesium or manganese (By similarity). 
BINDING   114   114        NADP (By similarity). 
BINDING   123   123        Substrate (By similarity). 
BINDING   125   125        Substrate (By similarity). 
BINDING   129   129        Substrate (By similarity). 
BINDING   139   139        Substrate (By similarity). 
BINDING   163   163        Substrate (By similarity). 
BINDING   362   362        NADP; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   401   401        NADP (By similarity). 
BINDING   405   405        NADP (By similarity). 
SITE   170   170  1     Critical for catalysis (By similarity). 
SITE   240   240  1     Critical for catalysis (By similarity). 
MOD_RES   123   123        Phosphoserine (By similarity). 
VARIANT   20    20  1     Q -> E (in strain: GQ212, KoQ229, SQ217). 
VARIANT   32    32  1     E -> V (in strain: TK-1). 
VARIANT   33    33  1     V -> A (in strain: GQ212). 
VARIANT   52    52  1     A -> T (in strain: GQ212, KoQ229, MAN, ME, Priscilla, SQ217). 
VARIANT   63    63  1     V -> A (in strain: ME). 
VARIANT   87    87  1     V -> A (in strain: SQ217). 
VARIANT   100   100  1     E -> G (in strain: California 76 VR 614). 
VARIANT   104   104  1     E -> G (in strain: 605). 
VARIANT   183   183  1     V -> M (in strain: Priscilla). 
VARIANT   271   271  1     G -> R (in strain: Bangui VR 730). 
VARIANT   306   306  1     Y -> C (in strain: Bangui VR 730). 
VARIANT   379   379  1     W -> R (in strain: El Tayeb RSA 342). 
VARIANT   415   415  1     T -> A (in strain: GQ212, KoQ229, SQ217). 
VARIANT   419   419  1     G -> A (in strain: GQ212, KoQ229, SQ217). 
Sequence information
Length: 427 AA [This is the length of the unprocessed precursor] Molecular weight: 46636 Da [This is the MW of the unprocessed precursor] CRC64: E23462962C26C138 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTELTGVSIV TYQHIKVPSQ GEKITVNKAV LEVPDRPIIP FIEGDGIGID IAPVMKNVVD 

        70         80         90        100        110        120 
AAVEKSYAGK RKIEWMEIYA GEKATKVYGK DNWLPDETLE AIKEYQVAIK GPLTTPVGGG 

       130        140        150        160        170        180 
IRSLNVALRQ QLDLYVCLRP VRYFTGVPSP VKTPEKVNMV IFRENSEDIY AGIEWPAGSP 

       190        200        210        220        230        240 
EAVKLINFLQ NEMGVKKIRF PETAGIGIKP VSKEGTSRLV RRAIQYAIDN DRDSVTLVHK 

       250        260        270        280        290        300 
GNIMKFTEGA FKDWGYEVAV KEFGAKPLDG GPWHVFENPK TGQKITIKDV IADAFLQQIL 

       310        320        330        340        350        360 
LRPAEYSVIA TLNLNGDYIS DALAAEVGGI GIAPGANLSD TVGLFEATHG TAPKYAGQDK 

       370        380        390        400        410        420 
VNPGSLILSA EMMLRYLGWK EAADLVVQGI EGAIESKTVT YDFARLMTGA KEVSTSQFGK 


AIIKHIL 

Q9ZH99 in FASTA format

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