[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8226630 [NCBI, ExPASy, EBI, Israel, Japan] Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., Fukunaga N.; "Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium, Vibrio sp. strain ABE-1."; J. Bacteriol. 175:6873-6880(1993).
[2]	PROTEIN SEQUENCE OF 2-41. PubMed=1295895 [NCBI, ExPASy, EBI, Israel, Japan] Fukunaga N., Imagawa S., Sahara T., Ishii A., Suzuki M.; "Purification and characterization of monomeric isocitrate dehydrogenase with NADP(+)-specificity from Vibrio parahaemolyticus Y-4."; J. Biochem. 112:849-855(1992).

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.
INDUCTION: By acetate.
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

D14047; BAA03135.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B49341; B49341.

3D structure databases

HSSP

P08200; 1PB1. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

P41560; 1-415.

ModBase

P41560.

Ontologies

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

P41560.

Other

UniRef

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

Keywords

Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 415`	`414`	`Isocitrate dehydrogenase [NADP] 1.`	`PRO_0000083550`
`NP_BIND`	`339 345`	`7`	`NADP (By similarity).`
`METAL`	`307 307`		`Magnesium or manganese (By similarity).`
`BINDING`	`104 104`		`NADP (By similarity).`
`BINDING`	`113 113`		`Substrate (By similarity).`
`BINDING`	`115 115`		`Substrate (By similarity).`
`BINDING`	`119 119`		`Substrate (By similarity).`
`BINDING`	`129 129`		`Substrate (By similarity).`
`BINDING`	`153 153`		`Substrate (By similarity).`
`BINDING`	`352 352`		`NADP; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`390 390`		`NADP (By similarity).`
`BINDING`	`394 394`		`NADP (By similarity).`
`SITE`	`160 160`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`230 230`	`1`	`Critical for catalysis (By similarity).`
`MOD_RES`	`113 113`		`Phosphoserine (By similarity).`
`CONFLICT`	`26 26`		`N -> G (in Ref. 2; AA sequence).`

Sequence information

Length: 415 AA [This is the length of the unprocessed precursor]

Molecular weight: 45145 Da [This is the MW of the unprocessed precursor]

CRC64: 353EFF202824696E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTNKIIIPTT GDKITFIDGK LSVPNNPIIP YIEGDGIGVD VTPPMLKVVN AAVAKAYGGD 

        70         80         90        100        110        120 
RKIEWLEVYA GEKATKMYDS ETWLPEETLN ILQEYKVSIK GPLTTPVGGG MSSLNVAIRQ 

       130        140        150        160        170        180 
MLDLYVCQRP VQWFTGVPSP VKRPSEVDMV IFRENTEDIY AGIEYKAGSD KAKSVIKFLI 

       190        200        210        220        230        240 
EEMGASNIRF TENCGIGIKP VSKEGSQRLV RQAIQYAIDN NKDSVTLVHK GNIMKFTEGA 

       250        260        270        280        290        300 
FKDWGYELAI EEFGASLLHG GPWCSLKNPN TGKEIIIKDV IADAMLQQVL LRPAEYSVIA 

       310        320        330        340        350        360 
TLNLNGDYLS DALAAQVGGI GIAPGANLGD EVAVFEATHG TAPKYAGKNK VNPGSVILSA 

       370        380        390        400        410 
EMMLRHMGWL EADLLLKGMS GAIQAKTVTY DFERLMDDAT LVSCSAFGDC IIDHM

P41560 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