Reviewed, UniProtKB/Swiss-Prot Q6GG12 (IDH_STAAR)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NADP]
      Short name=IDH
    EC=1.1.1.42
Alternative name(s):
    Oxalosuccinate decarboxylase
    NADP(+)-specific ICDH
    IDP

Gene names

Name:	icd
Synonyms:	citC
Ordered Locus Names:	SAR1773

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 422	422	Isocitrate dehydrogenase [NADP]		PRO_0000083562
Regions
	Nucleotide binding	344 – 350	7	NADP By similarity
Sites
	Metal binding	310	1	Magnesium or manganese By similarity
	Binding site	94	1	NADP By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	105	1	Substrate By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	119	1	Substrate By similarity
	Binding site	143	1	Substrate By similarity
	Binding site	357	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	396	1	NADP By similarity
	Binding site	400	1	NADP By similarity
	Site	150	1	Critical for catalysis By similarity
	Site	220	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GG12-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 65A3776BC6940AA2	FASTA	422	46,479
	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 TEFGDQVFTW QQYDEIVEKE GRDAANVAQE 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

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571856 Genomic DNA. Translation: CAG40764.1.
RefSeq	YP_041160.1.
3D structure databases
SMR	Q6GG12. Positions 3-421.
ModBase	Search...
Genome annotation databases
GeneID	2861358.
GenomeReviews	Gene locus SAR1773 in contig BX571856_GR.
KEGG	sar:SAR1773.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6GG12.
Enzyme and pathway databases
BioCyc	SAUR282458:SAR1773-MON.
Family and domain databases
InterPro	IPR004439. IsoCit_DHase_NADP_prok. IPR001804. IsoCit_IM_DHase. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit. PTHR11835:SF1. NADP_IDH_prok. 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_STAAR

Accession

Primary (citable) accession number: Q6GG12

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	July 19, 2004
Last modified:	November 25, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)