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G7KHI5 (G7KHI5_MEDTR) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH. PIRNR PIRNR000108

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity. PIRNR PIRNR000108 PIRSR PIRSR000108-3

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family. PIRNR PIRNR000108 RuleBase RU004443

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding144 – 1463NADP By similarity PIRSR PIRSR000108-4
Nucleotide binding378 – 3836NADP By similarity PIRSR PIRSR000108-4
Region163 – 1697Substrate binding By similarity PIRSR PIRSR000108-2

Sites

Metal binding3201Magnesium or manganese By similarity PIRSR PIRSR000108-3
Metal binding3431Magnesium or manganese By similarity PIRSR PIRSR000108-3
Binding site1461Substrate By similarity PIRSR PIRSR000108-2
Binding site1511NADP By similarity PIRSR PIRSR000108-4
Binding site1781Substrate By similarity PIRSR PIRSR000108-2
Binding site2011Substrate By similarity PIRSR PIRSR000108-2
Binding site3281NADP By similarity PIRSR PIRSR000108-4
Binding site3961NADP; via amide nitrogen and carbonyl oxygen By similarity PIRSR PIRSR000108-4
Site2081Critical for catalysis By similarity PIRSR PIRSR000108-1
Site2801Critical for catalysis By similarity PIRSR PIRSR000108-1

Sequences

Sequence LengthMass (Da)Tools
G7KHI5 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: 34FD52C6E39D13E1

FASTA48254,523
        10         20         30         40         50         60 
MLRASSSSSL FRLTSTLTML SSSCSLRNPN NLLFHSTPSS SLFLPHPPNS LSFHNHNHNP 

        70         80         90        100        110        120 
FIPLRCFASS TPIHVANPIV EMDGDEMTRI IWKMIKDKLI FPYLDLNIKY FDLGVLNRDA 

       130        140        150        160        170        180 
TEDRVTVESA EATLKYNVAV KCATITPDET RVKEFGLKSM WRSPNGTIRN ILNGTVFREP 

       190        200        210        220        230        240 
IICRNIPRII PGWKKPICIG RHAFGDQYRA TDTVINGPGK LKLVFVPEDG DTPVELDVHD 

       250        260        270        280        290        300 
FKGPGVALAM YNVDESIRAF AESSMSLAFT KKWPLYLSTK NTILKKYDGR FKDIFQEVYE 

       310        320        330        340        350        360 
ERWRQKFEEH SIWYEHRLID DMVAYALKSE GGYVWACKNY DGDVQSDLLA QGFGSLGLMT 

       370        380        390        400        410        420 
SVLLSSDGKT LEAEAAHGTV TRHFRFHQKG QETSTNSIAS IFAWTRGLEH RAKLDKNEKL 

       430        440        450        460        470        480 
LDFADKLEAA CVETVESGKM TKDLALLIHG PKVSREFYLN TEEFIDAVAS NLERKLREPA 


TV 

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References

[1]"The Medicago genome provides insight into the evolution of rhizobial symbioses."
Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K., Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., Krishnakumar V. expand/collapse author list , Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.
Nature 480:520-524(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A17 EMBL AES74397.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM001222 Genomic DNA. Translation: AES74397.1.
RefSeqXP_003618179.1. XM_003618131.1.
UniGeneMtr.11394.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11419675.
KEGGmtr:MTR_6g005470.

Phylogenomic databases

KOK00031.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11822. PTHR11822. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG7KHI5_MEDTR
AccessionPrimary (citable) accession number: G7KHI5
Entry history
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: March 19, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)