P31937 (3HIDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

HIBADH

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH. Ref.8
Pathway	Amino-acid degradation; L-valine degradation. Ref.8
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion.
Tissue specificity	Detected in skin fibroblasts. Ref.8
Sequence similarities	Belongs to the 3-hydroxyisobutyrate dehydrogenase family.

Ontologies

Keywords
Biological process	Branched-chain amino acid catabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro valine catabolic process Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	3-hydroxyisobutyrate dehydrogenase activity Inferred from direct assay Ref.8. Source: UniProtKB NAD 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 – 36

36

Mitochondrion Ref.7

Chain

37 – 336

300

3-hydroxyisobutyrate dehydrogenase, mitochondrial

PRO_0000007158

Regions

Nucleotide binding

40 – 68

29

NAD

Nucleotide binding

103 – 104

2

NAD

Sites

Active site

209

1

By similarity

Binding site

108

1

NAD

Binding site

134

1

NAD

Binding site

284

1

NAD

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

336

Helix Strand Turn

Details...

Beta strand

42 – 45

4

Helix

51 – 60

10

Beta strand

65 – 68

4

Helix

73 – 79

7

Turn

80 – 82

3

Helix

89 – 95

7

Beta strand

97 – 101

5

Helix

106 – 114

9

Helix

119 – 121

3

Beta strand

128 – 131

4

Helix

137 – 149

13

Beta strand

153 – 156

4

Beta strand

159 – 161

3

Helix

162 – 168

7

Beta strand

171 – 177

7

Helix

179 – 181

3

Helix

182 – 189

8

Turn

190 – 192

3

Beta strand

193 – 201

9

Helix

204 – 232

29

Helix

237 – 245

9

Helix

252 – 256

5

Turn

261 – 263

3

Beta strand

265 – 267

3

Helix

268 – 271

4

Beta strand

275 – 278

4

Helix

279 – 295

17

Helix

301 – 314

14

Turn

315 – 317

3

Helix

323 – 325

3

Helix

326 – 330

5

Sequences

	Sequence		Length	Mass (Da)
	P31937 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: DA3128774A91AF48	FASTA	336	35,329
	10 20 30 40 50 60 MAASLRLLGA ASGLRYWSRR LRPAAGSFAA VCSRSVASKT PVGFIGLGNM GNPMAKNLMK 70 80 90 100 110 120 HGYPLIIYDV FPDACKEFQD AGEQVVSSPA DVAEKADRII TMLPTSINAI EAYSGANGIL 130 140 150 160 170 180 KKVKKGSLLI DSSTIDPAVS KELAKEVEKM GAVFMDAPVS GGVGAARSGN LTFMVGGVED 190 200 210 220 230 240 EFAAAQELLG CMGSNVVYCG AVGTGQAAKI CNNMLLAISM IGTAEAMNLG IRLGLDPKLL 250 260 270 280 290 300 AKILNMSSGR CWSSDTYNPV PGVMDGVPSA NNYQGGFGTT LMAKDLGLAQ DSATSTKSPI 310 320 330 LLGSLAHQIY RMMCAKGYSK KDFSSVFQFL REEETF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new partner gene of the TEL/ETV6, TSL, cloned in acute myeloid leukemia with t(7;12)(p15;p13)." Yuji K., Mitani K., Ueno H., Sato Y., Ikawa S., Hangaishi A., Ogawa S., Suzuki T., Nakamoto T., Qiao Y., Hirai H. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and identification of human gene 1 transactivated by hepatitis C virus NS5A protein." Liu Y., Cheng J., Lu Y., Wang G., Zhang L., Chen J., Li L. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[7]	"Human liver protein map: update 1993." Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F. Electrophoresis 14:1216-1222(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 37-47. Tissue: Liver.
[8]	"Clinical, biochemical, and molecular findings in three patients with 3-hydroxyisobutyric aciduria." Loupatty F.J., van der Steen A., Ijlst L., Ruiter J.P., Ofman R., Baumgartner M.R., Ballhausen D., Yamaguchi S., Duran M., Wanders R.J. Mol. Genet. Metab. 87:243-248(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Crystal structure of human hydroxyisobutyrate dehydrogenase." Structural genomics consortium (SGC) Submitted (APR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 41-335 OF APOPROTEIN AND IN COMPLEX WITH NADH.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF529362 mRNA. Translation: AAQ09596.1.
AB050000 mRNA. Translation: BAF42045.1.
AK316605 mRNA. Translation: BAG38192.1.
AC007130 Genomic DNA. No translation available.
AC005091 Genomic DNA. No translation available.
CH236948 Genomic DNA. Translation: EAL24214.1.
CH471073 Genomic DNA. Translation: EAW93897.1.
BC032324 mRNA. Translation: AAH32324.1.

IPI

IPI00013860.

RefSeq

NP_689953.1. NM_152740.3.

UniGene

Hs.406758.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GF2	X-ray	2.38	A/B/C/D	41-335	[»]
2I9P	X-ray	2.55	A/B/C/D	41-336	[»]

ProteinModelPortal

P31937.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000265395.

PTM databases

PhosphoSite

P31937.

Polymorphism databases

DMDM

12643395.

2D gel databases

SWISS-2DPAGE

P31937.

Proteomic databases

PaxDb

P31937.

PRIDE

P31937.

Protocols and materials databases

DNASU

11112.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265395; ENSP00000265395; ENSG00000106049.

GeneID

11112.

KEGG

hsa:11112.

UCSC

uc003szf.3. human.

Organism-specific databases

CTD

11112.

GeneCards

GC07M027565.

HGNC

HGNC:4907. HIBADH.

HPA

HPA019522.
HPA021002.

MIM

608475. gene.

neXtProt

NX_P31937.

PharmGKB

PA29280.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2084.

HOGENOM

HOG000219610.

HOVERGEN

HBG050424.

InParanoid

P31937.

KO

K00020.

OMA

QIAFIGL.

OrthoDB

EOG476K0N.

PhylomeDB

P31937.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00362.

Gene expression databases

ArrayExpress

P31937.

Bgee

P31937.

CleanEx

HS_HIBADH.

Genevestigator

P31937.

GermOnline

ENSG00000106049. Homo sapiens.

Family and domain databases

Gene3D

1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.

InterPro

IPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR006115. 6PGDH_NADP-bd.
IPR013328. DH_multihelical.
IPR015815. HIBADH-type.
IPR011548. IsoBut3OH_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

PANTHER

PTHR22981. PTHR22981. 1 hit.

Pfam

PF03446. NAD_binding_2. 1 hit.
[Graphical view]

PIRSF

PIRSF000103. HIBADH. 1 hit.

SUPFAM

SSF48179. 6DGDH_C_like. 1 hit.

TIGRFAMs

TIGR01692. HIBADH. 1 hit.

PROSITE

PS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HIBADH. human.

DrugBank

DB00157. NADH.

EvolutionaryTrace

P31937.

GenomeRNAi

11112.

NextBio

42238.

SOURCE

Search...

Entry information

Entry name

3HIDH_HUMAN

Accession

Primary (citable) accession number: P31937
Secondary accession number(s): Q546Z2, Q9UDN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 24, 2001
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.