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Q59940 (IDH_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP]

Short name=IDH
EC=1.1.1.42
Alternative name(s):
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:icd
Synonyms:idh
Ordered Locus Names:SMU_672
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Isocitrate dehydrogenase [NADP]
PRO_0000083568

Sites

Metal binding2831Magnesium or manganese By similarity
Binding site1021Substrate By similarity
Binding site1041Substrate By similarity
Binding site1081Substrate By similarity
Binding site1181Substrate By similarity
Binding site1421Substrate By similarity
Site1491Critical for catalysis By similarity
Site2191Critical for catalysis By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Experimental info

Sequence conflict671N → K in AAC44826. Ref.1
Sequence conflict3831R → C in AAC44826. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59940 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 0F19F22A93D9DCD6

FASTA39343,141
        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 

« Hide

References

« Hide 'large scale' references
[1]Cvitkovitch D.G., Gutierrez J.A., Bleiweis A.S.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: JH1005.
[2]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
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.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.
[3]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
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-224.
Strain: JH1005.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62799 Genomic DNA. Translation: AAC44826.1.
AE014133 Genomic DNA. Translation: AAN58406.1.
U48886 Genomic DNA. Translation: AAC44503.1.
RefSeqNP_721100.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ59940.
SMRQ59940. Positions 2-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.672.

Proteomic databases

PRIDEQ59940.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58406; AAN58406; SMU_672.
GeneID1028090.
KEGGsmu:SMU_672.
PATRIC19663529. VBIStrMut61772_0597.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0538.
KOK00031.
OMAAITIFRE.
OrthoDBEOG6SNDTP.
PhylomeDBQ59940.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-656-MONOMER.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004439. Isocitrate_DH_NADP_dimer_prok.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00183. prok_nadp_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIDH_STRMU
AccessionPrimary (citable) accession number: Q59940
Secondary accession number(s): Q59927
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: July 9, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families