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Q98MY4 (Q98MY4_RHILO) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 73. 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 namesRecommended name:
Dihydrolipoyl dehydrogenase RuleBase RU003692

EC=1.8.1.4 RuleBase RU003692
Gene names
Ordered Locus Names:mlr0388
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. RuleBase RU003692

Cofactor

Binds 1 FAD per subunit By similarity. RuleBase RU003692

Miscellaneous

The active site is a redox-active disulfide bond By similarity. RuleBase RU003692

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. RuleBase RU003691

Sequences

Sequence LengthMass (Da)Tools
Q98MY4 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 65CEA1B4B306C0C9

FASTA48151,498
        10         20         30         40         50         60 
MAENYDVIII GSGPGGYVTA VRSAQLGFKT AIVEREHLGG ICLNWGCIPT KALLRSAEIM 

        70         80         90        100        110        120 
HYSDHLKDYG LKLDGKVSVD TSAVVDRSRK VSLRLNGGVA FLMKKNKVDV IWGEAKLSKP 

       130        140        150        160        170        180 
GEVVVSKTAK TPMEPQPPVP KGVKGEGTYT AKHIILATGA RPRALPGIEP DGKLIWTYFE 

       190        200        210        220        230        240 
AMVPKEMPKS LLVMGSGAIG IEFASFYRTM GADVTVVELL PAVMPVEDAE VSKFAQKQFE 

       250        260        270        280        290        300 
KQGMKIILEA KVTKVEKGAN SVTAHVEMKD GKVEKITADR MISAVGVQGN IENLGLEALG 

       310        320        330        340        350        360 
VKTDRGCIVV DGYGKTNVPG IYAIGDVAGP PMLAHKAEHE GVVCVEKIAG FPGVHAIDKL 

       370        380        390        400        410        420 
KIPGCTYCNP QVASVGLTEA KAKAEGKDIR VGRFQFAANG KAIALGEDQG FIKTIFDKKT 

       430        440        450        460        470        480 
GQLLGAHMVG AEVTELIQGF VVAMNLETTE EELMHTIFPH PTLSEMMKES VLDAYGRALN 


A 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB47979.1.
RefSeqNP_102193.1. NC_002678.2.

3D structure databases

HSSPHSSP built from PDB template 1DXL based on UniProtKB P31023.
ProteinModelPortalQ98MY4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1224856.
GenomeReviewsGene locus mlr0388 in contig BA000012_GR.
KEGGmlo:mlr0388.
NMPDRfig|266835.1.peg.298.
PATRIC22474772. VBIMesLot2464_0308.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG515043.
OMAHYMQHAK.
ProtClustDBPRK06416.

Family and domain databases

InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KOK00382.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 2 hits.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. Lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ98MY4_RHILO
AccessionPrimary (citable) accession number: Q98MY4
Entry history
Integrated into UniProtKB/TrEMBL: October 1, 2001
Last sequence update: October 1, 2001
Last modified: January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)