[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1016/S0140-6736(00)04403-2; PubMed=11418146 [NCBI, ExPASy, EBI, Israel, Japan] Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.; "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; Lancet 357:1225-1240(2001).
[2]	IDENTIFICATION BY MASS SPECTROMETRY. DOI=10.1016/j.mimet.2004.09.017; PubMed=15590099 [NCBI, ExPASy, EBI, Israel, Japan] Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.; "Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."; J. Microbiol. Methods 60:247-257(2005).
[3]	IDENTIFICATION BY MASS SPECTROMETRY. Vaezzadeh A.R., Deshusses J., Lescuye P., Hochstrasser D.F.; "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."; Submitted (OCT-2007) to UniProtKB.

Comments

CATALYTIC ACTIVITY: Isocitrate + NADP⁺ = 2-oxoglutarate + CO₂ + NADPH.
CATALYTIC ACTIVITY: Oxalosuccinate + NADP⁺ = 2-oxoglutarate + CO₂ + NADPH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

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

BA000018; BAB42784.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C89953; C89953.

RefSeq

NP_374805.1; -.

3D structure databases

HSSP

P39126; 1HQS. [HSSP ENTRY / PDB]

SMR

P99167; 3-421.

ModBase

P99167.

Enzyme and pathway databases

BioCyc

SAUR158879:SA1517-MON; -.

2D gel databases

SWISS-2DPAGE

P99167; -.

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.

BLOCKS

P99167.

Genome annotation databases

GeneID

1124362; -.

GenomeReviews

BA000018_GR; SA1517.

KEGG

sau:SA1517; -.

Phylogenomic databases

HOGENOM

P99167; -.

Genome annotation databases

CMR

P99167; SA1517.

Other

ProtoNet

P99167.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 422`	`422`	`Isocitrate dehydrogenase [NADP].`	`PRO_0000083561`
`NP_BIND`	`344 350`	`7`	`NADP (By similarity).`
`METAL`	`310 310`		`Magnesium or manganese (By similarity).`
`BINDING`	`94 94`		`NADP (By similarity).`
`BINDING`	`103 103`		`Substrate (By similarity).`
`BINDING`	`105 105`		`Substrate (By similarity).`
`BINDING`	`109 109`		`Substrate (By similarity).`
`BINDING`	`119 119`		`Substrate (By similarity).`
`BINDING`	`143 143`		`Substrate (By similarity).`
`BINDING`	`357 357`		`NADP; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`396 396`		`NADP (By similarity).`
`BINDING`	`400 400`		`NADP (By similarity).`
`SITE`	`150 150`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`220 220`	`1`	`Critical for catalysis (By similarity).`

Sequence information

Length: 422 AA [This is the length of the unprocessed precursor]

Molecular weight: 46423 Da [This is the MW of the unprocessed precursor]

CRC64: 50AA94DF122F0DB7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAEKITQGT EGLNVPNEPI IPFIIGDGIG PDIWKAASRV IDAAVEKAYN GEKRIEWKEV 

        70         80         90        100        110        120 
LAGQKAFDTT GEWLPQETLD TIKEYLIAVK GPLTTPIGGG IRSLNVALRQ ELDLFTCLRP 

       130        140        150        160        170        180 
VRWFKGVPSP VKRPQDVDMV IFRENTEDIY AGIEFKEGTT EVKKVIDFLQ NEMGATNIRF 

       190        200        210        220        230        240 
PETSGIGIKP VSKEGTERLV RAAIQYAIDN NRKSVTLVHK GNIMKFTEGS FKQWGYDLAL 

       250        260        270        280        290        300 
SEFGDQVFTW QQYDEIVENE GRDAANAAQE KAEKEGKIII KDSIADIFLQ QILTRPAEHD 

       310        320        330        340        350        360 
VVATMNLNGD YISDALAAQV GGIGIAPGAN INYETGHAIF EATHGTAPKY AGLNKVNPSS 

       370        380        390        400        410        420 
VILSSVLMLE HLGWQEAADK ITDSIEDTIA SKVVTYDFAR LMDGAEEVST SAFADELIKN 


LK

P99167 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools