Isocitrate dehydrogenase [NADP]

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Q9ZH99 (IDH_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Coxiella burnetii

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Ligand	Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 427

427

Isocitrate dehydrogenase [NADP]

PRO_0000323713

Regions

Nucleotide binding

349 – 355

NADP By similarity

Sites

Metal binding

317

Magnesium or manganese By similarity

Binding site

114

NADP By similarity

Binding site

123

Substrate By similarity

Binding site

125

Substrate By similarity

Binding site

129

Substrate By similarity

Binding site

139

Substrate By similarity

Binding site

163

Substrate By similarity

Binding site

362

NADP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

401

NADP By similarity

Binding site

405

NADP By similarity

Site

170

Critical for catalysis By similarity

Site

240

Critical for catalysis By similarity

Amino acid modifications

Modified residue

123

Phosphoserine By similarity

Natural variations

Natural variant

Q → E in strain: GQ212, KoQ229, SQ217.

Natural variant

E → V in strain: TK-1.

Natural variant

V → A in strain: GQ212.

Natural variant

A → T in strain: GQ212, KoQ229, MAN, ME, Priscilla, SQ217.

Natural variant

V → A in strain: ME.

Natural variant

V → A in strain: SQ217.

Natural variant

100

E → G in strain: California 76 VR 614.

Natural variant

104

E → G in strain: 605.

Natural variant

183

V → M in strain: Priscilla.

Natural variant

271

G → R in strain: Bangui VR 730.

Natural variant

306

Y → C in strain: Bangui VR 730.

Natural variant

379

W → R in strain: El Tayeb RSA 342.

Natural variant

415

T → A in strain: GQ212, KoQ229, SQ217.

Natural variant

419

G → A in strain: GQ212, KoQ229, SQ217.

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ZH99 [UniParc].

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

FASTA

427

46,636

        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' referencesShow '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: 10361714] [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: 10556719] [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. Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.
[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: 17088354] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, DEVELOPMENTAL STAGE. Strain: Nine Mile Crazy / RSA 514.
+	Additional computationally mapped references.

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.
RefSeq	NP_820195.2. NC_002971.3.
3D structure databases
HSSP	HSSP built from PDB template 1PB1 based on UniProtKB P08200.
ProteinModelPortal	Q9ZH99.
SMR	Q9ZH99. Positions 12-426.
ModBase	Search...
Proteomic databases
PRIDE	Q9ZH99.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1209104.
GenomeReviews	Gene locus CBU_1200 in contig AE016828_GR.
KEGG	cbu:CBU_1200.
NMPDR	fig\|227377.1.peg.1139.
PATRIC	17931139. VBICoxBur82552_1195.
TIGR	CBU_1200.
Phylogenomic databases
OMA	FQQIQTR.
PhylomeDB	Q9ZH99.
ProtClustDB	CLSK914608.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_1200-MONOMER.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004439. Isocitrate_DH_NADP_dimer_prok. IPR024084. IsoPropMal-DH-like_dom. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
KO	K00031.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00183. Prok_nadp_idh. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IDH_COXBU

Accession

Primary (citable) accession number: Q9ZH99
Secondary accession number(s): Q7C3F6

Q9RG72

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Coxiella burnetii

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents