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Q9SWG0 (IVD_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

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

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; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3.

Subunit structure

Homodimer By similarity. Ref.2 UniProtKB Q9FS87

Subcellular location

Mitochondrion Ref.1 Ref.7.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processleucine catabolic process

Inferred from direct assay. Source: TAIR

   Cellular componentmitochondrial matrix

Inferred from direct assay. Source: TAIR

   Molecular functionATP binding

Inferred from direct assay. Source: TAIR

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

isovaleryl-CoA dehydrogenase activity

Inferred from direct assay. Source: TAIR

Complete GO annotation...

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

Regions

Nucleotide binding151 – 16010FAD By similarity
Nucleotide binding184 – 1863FAD By similarity
Nucleotide binding364 – 3685FAD By similarity
Nucleotide binding393 – 3953FAD By similarity
Region206 – 2072Substrate binding By similarity
Region268 – 2714Substrate binding By similarity
Region391 – 3922Substrate binding By similarity

Sites

Active site2701Proton acceptor By similarity UniProtKB P26440
Binding site1601Substrate; via carbonyl oxygen By similarity
Binding site2611Substrate By similarity
Binding site2961FAD By similarity
Binding site3071FAD By similarity

Experimental info

Sequence conflict491N → I in AAD45605. Ref.2
Sequence conflict491N → I in AAM64839. Ref.6
Sequence conflict2821M → V in AAL32645. Ref.5
Sequence conflict2821M → V in AAM91199. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9SWG0 [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

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]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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.
[6]"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].
[7]"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].
Strain: cv. Landsberg erecta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y12695 mRNA. Translation: CAA73227.1.
AF160729 mRNA. Translation: AAD45605.1.
AL132953 Genomic DNA. Translation: CAB72479.1.
CP002686 Genomic DNA. Translation: AEE78020.1.
AY062567 mRNA. Translation: AAL32645.1.
AY128799 mRNA. Translation: AAM91199.1.
AY087286 mRNA. Translation: AAM64839.1.
IPIIPI00541942.
PIRT47470.
RefSeqNP_190116.1. NM_114399.4.
UniGeneAt.428.

3D structure databases

ProteinModelPortalQ9SWG0.
SMRQ9SWG0. Positions 31-403.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9SWG0.

Proteomic databases

PRIDEQ9SWG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G45300.1; AT3G45300.1; AT3G45300.
GeneID823668.
GenomeReviewsGene locus AT3G45300 in contig BA000014_GR.
KEGGath:AT3G45300.
NMPDRfig|3702.1.peg.15742.

Organism-specific databases

GeneFarm4384.
TAIRAt3g45300.

Phylogenomic databases

GeneTreeEPGT00070000028664.
HOGENOMHBG699365.
InParanoidQ9SWG0.
OMAKCGMRAS.
PhylomeDBQ9SWG0.
ProtClustDBPLN02519.

Gene expression databases

ArrayExpressQ9SWG0.
GenevestigatorQ9SWG0.
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_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
[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.
KOK00253.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: December 14, 2011
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents