Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9SWG0 (IVD_ARATH)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Isovaleryl-CoA dehydrogenase, mitochondrial
      Short name=IVD
    EC=1.3.99.10
Gene names
Name: IVD
Ordered Locus Names: At3g45300
ORF Names: F18N11.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Hide | Top

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

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

Cofactor

FAD. UniProtKB P26440

Pathway

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

Subunit structure

Homodimer By similarity. UniProtKB Q9FS87

Subcellular location

Mitochondrion. Ref.1 Ref.6

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Hide | Top

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from direct assay. Source: TAIR

   Molecular functionATP binding

Inferred from direct assay. Source: TAIR

FAD binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

isovaleryl-CoA dehydrogenase activity

Inferred from direct assay. Source: TAIR

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion By similarity UniProtKB Q9FS87
Chain26 – 409384Isovaleryl-CoA dehydrogenase, mitochondrial UniProtKB Q9FS87
PRO_0000000535

Sites

Active site2701Proton acceptor By similarity UniProtKB P26440

Experimental info

Sequence conflict491N → I Ref.1
Sequence conflict491N → I Ref.5
Sequence conflict2821M → V in AAL32645. Ref.4
Sequence conflict2821M → V in AAM91199. Ref.4

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9SWG0-1 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 6D3D86C8F632067C

FASTA40944,773
        10         20         30         40         50         60 
MQRFFSARSI LGYAVKTRRR SFSSRSSSLL FDDTQLQFKE SVSKFAQDNI APHAERIDKT 

        70         80         90        100        110        120 
NSFPKDVNLW KLMGEFNLHG ITAPEEYGGL GLGYLYHCIA MEEISRASGS VALSYGAHSN 

       130        140        150        160        170        180 
LCINQLVRNG TAAQKEKYLP KLISGEHVGA LAMSEPNAGS DVVGMKCKAE KVDGGYILNG 

       190        200        210        220        230        240 
NKMWCTNGPS AETLVVYAKT DTKAGSKGIT AFIIEKGMTG FSTAQKLDKL GMRGSDTCEL 

       250        260        270        280        290        300 
VFENCFVPEE NILDKEGKGV YVLMSGLDLE RLVLAAGPLG IMQACLDNVL PYIRQREQFG 

       310        320        330        340        350        360 
RPVGEFQFIQ GKVADMYTAL QSSRSYVYSV ARDCDNGKVD PKDCAGTILC AAERATQVAL 

       370        380        390        400 
QAIQCLGGNG YINEYATGRL LRDAKLYEIG AGTSEIRRIV IGRELFKEE

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"In plants a putative isovaleryl-CoA-dehydrogenase is located in mitochondria."
Daeschner K., Thalheim C., Guha C., Brennicke A., Binder S.
Plant Mol. Biol. 39:1275-1282(1999) [PubMed: 10380813] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]"Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria."
Faivre-Nitschke S.E., Couee I., Vermel M., Grienenberger J.-M., Gualberto J.M.
Eur. J. Biochem. 268:1332-1339(2001) [PubMed: 11231285] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
Plant Cell 16:241-256(2004) [PubMed: 14671022] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Hide | Top

Cross-references

Sequence databases

AF160729 mRNA. Translation: AAD45605.1.
Y12695 mRNA. Translation: CAA73227.1.
AL132953 Genomic DNA. Translation: CAB72479.1.
AY062567 mRNA. Translation: AAL32645.1.
AY128799 mRNA. Translation: AAM91199.1.
AY087286 mRNA. Translation: AAM64839.1.
IPIIPI00541942.
PIRT47470.
RefSeqNP_190116.1.
UniGeneAt.428

3D structure databases

HSSPHSSP built from PDB template 1IVH based on UniProtKB P26440.
ModBaseSearch...

Proteomic databases

PRIDEQ9SWG0.

Genome annotation databases

GeneID823668.
GenomeReviewsGene locus AT3G45300 in contig BA000014_GR.
KEGGath:AT3G45300.
NMPDRfig|3702.1.peg.15742.

Organism-specific databases

GeneFarm4384.
TAIRAt3g45300.

Phylogenomic databases

OMAQ9SWG0. ELFNETR.

Enzyme and pathway databases

BRENDA1.3.99.10. 302.

Gene expression databases

ArrayExpressQ9SWG0.
GermOnlineAT3G45300. Arabidopsis thaliana.

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...

Hide | Top

Entry information

Entry nameIVD_ARATH
AccessionPrimary (citable) accession number: Q9SWG0
Secondary accession number(s): Q8W4G7, Q9XFT2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 30, 2006
Last modified: June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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