NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8169222 [NCBI, ExPASy, EBI, Israel, Japan]
Muro-Pastor M.I., Florencio F.J.;
"NADP(+)-isocitrate dehydrogenase from the cyanobacterium Anabaena sp. strain PCC 7120: purification and characterization of the enzyme and cloning, sequencing, and disruption of the icd gene.";
J. Bacteriol. 176:2718-2726(1994).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/8.5.205; PubMed=11759840 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., Yasuda M., Tabata S.;
"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120.";
DNA Res. 8:205-213(2001).

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

X77654; CAA54734.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000019; BAB73526.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A55591; A55591.
AE2034; AE2034.

RefSeq

NP_485867.1; -.

3D structure databases

HSSP

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

ModBase

P50214.

Enzyme and pathway databases

BioCyc

NSP103690:ALR1827-MON; -.

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.

Genome annotation databases

GeneID

1105419; -.

GenomeReviews

BA000019_GR; alr1827.

KEGG

ana:alr1827; -.

NMPDR

fig|103690.1.peg.2134; -.

Phylogenomic databases

HOGENOM

P50214; -.

Genome annotation databases

CMR

P50214; alr1827.

Other

ProtoNet

P50214.

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

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 473`	`473`	`Isocitrate dehydrogenase [NADP].`	`PRO_0000083547`
`NP_BIND`	`394 400`	`7`	`NADP (By similarity).`
`METAL`	`362 362`		`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`	`407 407`		`NADP; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`446 446`		`NADP (By similarity).`
`BINDING`	`450 450`		`NADP (By similarity).`
`SITE`	`160 160`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`237 237`	`1`	`Critical for catalysis (By similarity).`
`MOD_RES`	`113 113`		`Phosphoserine (By similarity).`

Sequence information

Length: 473 AA [This is the length of the unprocessed precursor]

Molecular weight: 52228 Da [This is the MW of the unprocessed precursor]

CRC64: D30941B992A38AAB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYNKITPPTT GEKITFKNGE PVVPDNPIIP FIRGDGTGID IWPATEKVLD AAVAKAYQGK 

        70         80         90        100        110        120 
RKISWFKVYA GDEACDLYGT YQYLPEDTLT AIREYGVAIK GPLTTPVGGG IRSLNVALRQ 

       130        140        150        160        170        180 
IFDLYACVRP CRYYAGTPSP HKNPEKLDVI VYRENTEDIY LGIEWKQGSE IGDRLISILN 

       190        200        210        220        230        240 
KELIPATPEH GKKQIPLDSG IGIKPISKTG SQRLVRRAIK HALTLPKDKQ QVTLVHKGNI 

       250        260        270        280        290        300 
MKYTEGAFRD WGYELATSEF RQETVTERES WILSNKEKNP NISLEDNARQ IDPGFDALTP 

       310        320        330        340        350        360 
EKKAQIVKEV ETVLNSIWES HGNGKWKEKV LVNDRIADSI FQQIQTRPDE YSILATMNLN 

       370        380        390        400        410        420 
GDYLSDAAAA IVGGLGMGPG ANIGDSCAVF EATHGTAPKH AGLDRINPGS VILSGVMMLE 

       430        440        450        460        470 
YMGWQEAADL IKKGLSDAIA NSQVTYDLAR LLEPPVEPLK CSEFADAIIK HFG

P50214 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