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Q9SUC0 (3HIDH_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial
Short name=HIBADH
EC=1.1.1.31
Gene names
Ordered Locus Names:At4g20930
ORF Names:T13K14.90
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 length347 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-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the 3-hydroxyisobutyrate dehydrogenase family.

Sequence caution

The sequence CAB45888.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79093.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion By similarity
Chain35 – 347313Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial
PRO_0000007162

Regions

Nucleotide binding38 – 6730NAD By similarity
Nucleotide binding101 – 1022NAD By similarity

Sites

Active site2191 By similarity
Binding site1341NAD; via amide nitrogen By similarity
Binding site2941NAD By similarity

Experimental info

Sequence conflict211S → F in AAM63893. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9SUC0 [UniParc].

Last modified April 30, 2003. Version 3.
Checksum: 6ED2E87CC3DE191C

FASTA34737,365
        10         20         30         40         50         60 
MAIRRAQTLL CLSKFKTNFV SGSLHRFSSS SQNSNQFQNV GFIGLGNMGF RMVNNLIRAG 

        70         80         90        100        110        120 
YKVTVHDINR DVMKMFTEMG VSSRETPYEV AQDSEVVITM LPSSSHVMDV YTGTNGLLLG 

       130        140        150        160        170        180 
ENDIRPALFI DSSTIDPQTT RKISLAVSNC NLKEKRDNWE KPVMLDAPVS GGVLAAEAGT 

       190        200        210        220        230        240 
LTFMVGGPED AYLAARPILQ SMGRTSIYCG GSGNGSAAKI CNNLAMAVSM LGTSEALALG 

       250        260        270        280        290        300 
QSLGISASTL TEVLNTSSGR CWSSDAYNPV PGVMKGVPSS RDYNGGFASK LMAKDLNLAA 

       310        320        330        340 
ASAEEVGHKS PLISKAQEIY KKMCEEGHET KDFSCVFRHF YNGKDEV

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL080282 Genomic DNA. Translation: CAB45888.1. Sequence problems.
AL161554 Genomic DNA. Translation: CAB79093.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84377.1.
AY086845 mRNA. Translation: AAM63893.1.
IPIIPI00533209.
RefSeqNP_567617.1. NM_118211.4.
UniGeneAt.32684.

3D structure databases

ProteinModelPortalQ9SUC0.
SMRQ9SUC0. Positions 37-343.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9SUC0.

Proteomic databases

PRIDEQ9SUC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G20930.1; AT4G20930.1; AT4G20930.
GeneID827841.
GenomeReviewsGene locus AT4G20930 in contig CT486007_GR.
KEGGath:AT4G20930.
NMPDRfig|3702.1.peg.19926.

Organism-specific databases

TAIRAt4g20930.

Phylogenomic databases

GeneTreeEPGT00070000030136.
HOGENOMHBG729179.
InParanoidQ9SUC0.
OMAPMARNLI.
PhylomeDBQ9SUC0.
ProtClustDBCLSN2689528.

Gene expression databases

ArrayExpressQ9SUC0.
GenevestigatorQ9SUC0.
GermOnlineAT4G20930. Arabidopsis thaliana.

Family and domain databases

InterProIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR015815. 3hydroxyacid_DH/Rdtase.
IPR008927. 6-PGluconate_DH_C-like.
IPR006115. 6PGDH_NADP-bd.
IPR013328. DH_multihelical.
IPR011548. IsoBut3OH_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KOK00020.
PANTHERPTHR22981. 3hydroxy_acid_DH. 1 hit.
PfamPF03446. NAD_binding_2. 1 hit.
[Graphical view]
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR01692. HIBADH. 1 hit.
PROSITEPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name3HIDH_ARATH
AccessionPrimary (citable) accession number: Q9SUC0
Secondary accession number(s): Q8LC25
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: April 30, 2003
Last modified: November 16, 2011
This is version 88 of the entry and version 3 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

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