ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q59940

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name IDH_STRMU
Primary accession number Q59940
Secondary accession number Q59927
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 28, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 58)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP]
Synonyms IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
Gene name
Name: icd
Synonyms: idh
OrderedLocusNames: SMU_672
From
Streptococcus mutans [TaxID: 1309] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JH1005;
Cvitkovitch D.G., Gutierrez J.A., Bleiweis A.S.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700610 / UA159 / Serotype c;
DOI=10.1073/pnas.172501299; PubMed=12397186 [NCBI, ExPASy, EBI, Israel, Japan]
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen.";
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-224.
STRAIN=JH1005;
Gutierrez J.A., Crowley P.J., Brown D.P., Hillman J.D., Youngman P., Bleiweis A.S.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
Comments
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
U62799; AAC44826.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014133; AAN58406.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48886; AAC44503.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_721100.1; -.
3D structure databases
HSSP P39126; 1HQS. [HSSP ENTRY / PDB]
ModBase Q59940.
Enzyme and pathway databases
BioCyc SMUT210007:SMU_672-MON; -.
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.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS Q59940.
Genome annotation databases
GeneID 1028090; -.
GenomeReviews AE014133_GR; SMU_672.
KEGG smu:SMU.672; -.
NMPDR fig|210007.1.peg.613; -.
Phylogenomic databases
HOGENOM Q59940; -.
Genome annotation databases
CMR Q59940; SMU_672.
Other
ProtoNet Q59940.
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   393  393     Isocitrate dehydrogenase [NADP]. PRO_0000083568
METAL   283   283        Magnesium or manganese (By similarity). 
BINDING   102   102        Substrate (By similarity). 
BINDING   104   104        Substrate (By similarity). 
BINDING   108   108        Substrate (By similarity). 
BINDING   118   118        Substrate (By similarity). 
BINDING   142   142        Substrate (By similarity). 
SITE   149   149  1     Critical for catalysis (By similarity). 
SITE   219   219  1     Critical for catalysis (By similarity). 
MOD_RES   102   102        Phosphoserine (By similarity). 
CONFLICT   67    67        N -> K (in Ref. 1; AAC44826). 
CONFLICT   383   383        R -> C (in Ref. 1; AAC44826). 
Sequence information
Length: 393 AA [This is the length of the unprocessed precursor] Molecular weight: 43141 Da [This is the MW of the unprocessed precursor] CRC64: 0F19F22A93D9DCD6 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAEKVSFEEG KLQVPDKPVI PYIEGDGVGQ DIWKNAQIVF DKAIAKVYGG HKQVIWREVL 

        70         80         90        100        110        120 
AGKKAYNETG NWLPNETLEI IKTHLLAIKG PLETPVGGGI RSLNVALRQE LDLFACVRPV 

       130        140        150        160        170        180 
RYFKGVPSPL KHPEKTAITI FRENTEDIYA GIEWNAGTAE VQKVINFLQD DMQVKKIRFP 

       190        200        210        220        230        240 
KSSSIGIKPI SIEGSQRLIR AAIEYALANN LTKVTLVHKG NIQKFTEGGF RKWGYELAKR 

       250        260        270        280        290        300 
EYAAELASGQ LVVDDIIADN FLQQILLKPE RFDVVALTNL NGDYASDALA AQVGGIGISP 

       310        320        330        340        350        360 
GANINYQTGH AIFEATHGTA PDIAGQDLAN PSSVLLSGCM LFDYIGWSKV SDLIMKAVEK 

       370        380        390 
AIANGQVTID FAKELGVEAL TTRQFSEVLL TYL
Q59940 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!