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Q9ZH99 (IDH_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP]

Short name=IDH
EC=1.1.1.42
Alternative name(s):
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:icd
Ordered Locus Names:CBU_1200
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Developmental stage

Detected in both the small cell variant (SCV) and in the large cell variant (LCV) stage (at protein level). LCVs are more metabolically active than SCVs. Ref.4

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5-7.7.

Sequence caution

The sequence AAO90709.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Isocitrate dehydrogenase [NADP]
PRO_0000323713

Regions

Nucleotide binding349 – 3557NADP By similarity

Sites

Metal binding3171Magnesium or manganese By similarity
Binding site1141NADP By similarity
Binding site1231Substrate By similarity
Binding site1251Substrate By similarity
Binding site1291Substrate By similarity
Binding site1391Substrate By similarity
Binding site1631Substrate By similarity
Binding site3621NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site4011NADP By similarity
Binding site4051NADP By similarity
Site1701Critical for catalysis By similarity
Site2401Critical for catalysis By similarity

Amino acid modifications

Modified residue1231Phosphoserine By similarity

Natural variations

Natural variant201Q → E in strain: GQ212, KoQ229, SQ217.
Natural variant321E → V in strain: TK-1.
Natural variant331V → A in strain: GQ212.
Natural variant521A → T in strain: GQ212, KoQ229, MAN, ME, Priscilla, SQ217.
Natural variant631V → A in strain: ME.
Natural variant871V → A in strain: SQ217.
Natural variant1001E → G in strain: California 76 VR 614.
Natural variant1041E → G in strain: 605.
Natural variant1831V → M in strain: Priscilla.
Natural variant2711G → R in strain: Bangui VR 730.
Natural variant3061Y → C in strain: Bangui VR 730.
Natural variant3791W → R in strain: El Tayeb RSA 342.
Natural variant4151T → A in strain: GQ212, KoQ229, SQ217.
Natural variant4191G → A in strain: GQ212, KoQ229, SQ217.

Sequences

Sequence LengthMass (Da)Tools
Q9ZH99 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E23462962C26C138

FASTA42746,636
        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 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of an immunogenic and acid-induced isocitrate dehydrogenase gene from Coxiella burnetii."
Van Nguyen S., To H., Yamaguchi T., Fukushi H., Hirai K.
FEMS Microbiol. Lett. 175:101-106(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPTIMAL PH.
Strain: Nine Mile I.
[2]"Differentiation of Coxiella burnetii isolates by sequence determination and PCR-restriction fragment length polymorphism analysis of isocitrate dehydrogenase gene."
Nguyen S.V., Hirai K.
FEMS Microbiol. Lett. 180:249-254(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[3]"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."
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. expand/collapse author list , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.
Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RSA 493 / Nine Mile phase I.
[4]"Proteome and antigen profiling of Coxiella burnetii developmental forms."
Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J., Samuel J.E., Heinzen R.A.
Infect. Immun. 75:290-298(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, DEVELOPMENTAL STAGE.
Strain: Nine Mile Crazy / RSA 514.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF069035 Genomic DNA. Translation: AAC68600.1.
AF146284 Genomic DNA. Translation: AAF16725.1.
AF146285 Genomic DNA. Translation: AAF16726.1.
AF146286 Genomic DNA. Translation: AAF16727.1.
AF146287 Genomic DNA. Translation: AAF16728.1.
AF146288 Genomic DNA. Translation: AAF16729.1.
AF146289 Genomic DNA. Translation: AAF16730.1.
AF146290 Genomic DNA. Translation: AAF16731.1.
AF146291 Genomic DNA. Translation: AAF16732.1.
AF146292 Genomic DNA. Translation: AAF16733.1.
AF146293 Genomic DNA. Translation: AAF16734.1.
AF146294 Genomic DNA. Translation: AAF16735.1.
AF146295 Genomic DNA. Translation: AAF16736.1.
AF146296 Genomic DNA. Translation: AAF16737.1.
AF146297 Genomic DNA. Translation: AAF16738.1.
AF146298 Genomic DNA. Translation: AAF16739.1.
AF146299 Genomic DNA. Translation: AAF16740.1.
AF146300 Genomic DNA. Translation: AAF16741.1.
AF146301 Genomic DNA. Translation: AAF16742.1.
AE016828 Genomic DNA. Translation: AAO90709.2. Different initiation.
RefSeqNP_820195.2. NC_002971.3.

3D structure databases

ProteinModelPortalQ9ZH99.
SMRQ9ZH99. Positions 12-426.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9ZH99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO90709; AAO90709; CBU_1200.
GeneID1209104.
KEGGcbu:CBU_1200.
PATRIC17931139. VBICoxBur82552_1195.

Phylogenomic databases

KOK00031.
OMAFRDWGYE.
OrthoDBEOG6SNDTP.
ProtClustDBCLSK914608.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1188-MONOMER.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004439. Isocitrate_DH_NADP_dimer_prok.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00183. prok_nadp_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIDH_COXBU
AccessionPrimary (citable) accession number: Q9ZH99
Secondary accession number(s): Q7C3F6 expand/collapse secondary AC list , Q9RG62, Q9RG63, Q9RG64, Q9RG65, Q9RG66, Q9RG67, Q9RG68, Q9RG69, Q9RG70, Q9RG71, Q9RG72
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 1, 1999
Last modified: November 13, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names