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

Names and origin

Protein names

Recommended name:
    Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial
      Short name=HIBADH
    EC=1.1.1.31

Gene names

Ordered Locus Names:	At4g20930
ORF Names:	T13K14.90

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro valine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxyisobutyrate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD or NADH binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 34	34	Mitochondrion By similarity
	Chain	35 – 347	313	Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial		PRO_0000007162
Regions
	Nucleotide binding	38 – 67	30	NAD By similarity
	Nucleotide binding	101 – 102	2	NAD By similarity
Sites
	Active site	219	1	By similarity
	Binding site	134	1	NAD; via amide nitrogen By similarity
	Binding site	294	1	NAD By similarity
Experimental info
	Sequence conflict	21	1	S → F in AAM63893. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9SUC0-1 [UniParc]. Last modified April 30, 2003. Version 3. Checksum: 6ED2E87CC3DE191C	FASTA	347	37,365
	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

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. , 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]

"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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL080282 Genomic DNA. Translation: CAB45888.1. Sequence problems. AL161554 Genomic DNA. Translation: CAB79093.1. Sequence problems. AY086845 mRNA. Translation: AAM63893.1.
IPI	IPI00533209.
RefSeq	NP_567617.1.
UniGene	At.32684
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9SUC0.
Genome annotation databases
GeneID	827841.
GenomeReviews	Gene locus AT4G20930 in contig CT486007_GR.
KEGG	ath:AT4G20930.
NMPDR	fig|3702.1.peg.19926.
Organism-specific databases
TAIR	At4g20930.
Phylogenomic databases
OMA	Q9SUC0. PMARNLI.
Enzyme and pathway databases
BRENDA	1.1.1.31. 302.
Gene expression databases
ArrayExpress	Q9SUC0.
GermOnline	AT4G20930. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002204. 3-OH-isobutyrate_DH-rel_CS. IPR015815. 3hydroxyacid_DH/Rdtase. IPR006115. 6PGDH_NAD-bd. IPR013328. DH_multihelical. IPR011548. IsoBut3OH_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR22981. 3hydroxy_acid_DH. 1 hit.
Pfam	PF03446. NAD_binding_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01692. HIBADH. 1 hit.
PROSITE	PS00895. 3_HYDROXYISOBUT_DH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

3HIDH_ARATH

Accession

Primary (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:	June 16, 2009
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)