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Reviewed, UniProtKB/Swiss-Prot Q5RBD5 (IVD_PONAB)

Last modified June 16, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Isovaleryl-CoA dehydrogenase, mitochondrial
      Short name=IVD
    EC=1.3.99.10
Gene names
Name: IVD
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

3-methylbutanoyl-CoA + acceptor = 3-methylbut-2-enoyl-CoA + reduced acceptor.

Cofactor

FAD By similarity.

Pathway

Amino-acid degradation; L-leucine degradation; HMG-CoA from 3-isovaleryl-CoA: step 1/3.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

isovaleryl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion By similarity
Chain30 – 423394Isovaleryl-CoA dehydrogenase, mitochondrial
PRO_0000000533

Sites

Active site2831Proton acceptor By similarity

Amino acid modifications

Modified residue751N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RBD5-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 87A4DB40CF56D886

FASTA42346,275
        10         20         30         40         50         60 
MATATRLLGW RVASWRMRPP PAGFVSQRAH SLLPVDDAIN GLSEEQRQLR QTVAKFLQEH 

        70         80         90        100        110        120 
LAPKAQEIDR SNEFKNLREF WKQLGNLGVL GITAPVQYGG SGLGYLEHVL VMEEISRASG 

       130        140        150        160        170        180 
AVGLSYGAHS NLCINQLVRN GNEAQKEKYL PKLISGEYIG ALAMSEPNAG SDVVSMKLKA 

       190        200        210        220        230        240 
EKKGNHYILN GNKFWITNGP DADVLIVYAK TDLAAVPASR GITAFIVEKG MPGFSTSKKL 

       250        260        270        280        290        300 
DKLGMRGSNT CELIFEDCKV PAANILGHEN KGVYVLMSGL DLERLVLAGG PLGLMQAVLD 

       310        320        330        340        350        360 
HTIPYLHVRE AFGQKIGHFQ LMQGKMADMY TRLMACRQYV YNVAKACDEG HCTAKDCAGV 

       370        380        390        400        410        420 
ILYSAECATQ VALDGIQCFG GNGYINDFPM GRFLRDAKLY EIGAGTSEVR RLVIGRAFNA 


DFH 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

CR858716 mRNA. Translation: CAH90925.1.
RefSeqNP_001125529.1.
UniGenePab.7824

3D structure databases

SMRQ5RBD5. Positions 35-421.
ModBaseSearch...

Genome annotation databases

GeneID100172441.

Phylogenomic databases

HOVERGENQ5RBD5.

Enzyme and pathway databases

BRENDA1.3.99.10. 269192.

Family and domain databases

InterProIPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_M.
IPR013786. AcylCoA_DH/ox_N.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIVD_PONAB
AccessionPrimary (citable) accession number: Q5RBD5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 21, 2004
Last modified: June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents