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UniProtKB/Swiss-Prot entry P31937


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 3HIDH_HUMAN
Primary accession number P31937
Secondary accession number Q9UDN3
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on January 24, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 86)
Name and origin of the protein
Protein name 3-hydroxyisobutyrate dehydrogenase, mitochondrial [Precursor]
Synonyms HIBADH
EC 1.1.1.31
Gene name
Name: HIBADH
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 37-47.
TISSUE=Liver;
DOI=10.1002/elps.11501401181; PubMed=8313870 [NCBI, ExPASy, EBI, Israel, Japan]
Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
"Human liver protein map: update 1993.";
Electrophoresis 14:1216-1222(1993).
[4]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 41-335 OF APOPROTEIN AND IN COMPLEX WITH NADH.
Structural genomics consortium (SGC);
"Crystal structure of human hydroxyisobutyrate dehydrogenase.";
Submitted (APR-2006) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AC007130; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC005091; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC032324; AAH32324.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_689953.1; -.
UniGene Hs.406758
3D structure databases
PDB
2GF2; X-ray; 2.38 A; A/B/C/D=41-335.[ExPASy / RCSB / EBI]
2I9P; X-ray; 2.55 A; A/B/C/D=41-336.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2GF2; -.
2I9P; -.
ModBase P31937.
PTM databases
PhosphoSite P31937; -.
Enzyme and pathway databases
Reactome REACT_13; Metabolism of amino acids.
2D gel databases
SWISS-2DPAGE P31937; -.
Siena-2DPAGE P31937; -.
Organism-specific databases
H-InvDB HIX0006550; -.
HGNC HGNC:4907; HIBADH.
GenAtlas HIBADH.
MIM 608475; gene. [NCBI / EBI]
PharmGKB PA29280; -.
GeneCards P31937.
Gene expression databases
ArrayExpress P31937; -.
CleanEx HS_HIBADH; -.
GermOnline ENSG00000106049; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (non-traceable author statement from UniProtKB).
GO:0008442; Molecular function: 3-hydroxyisobutyrate dehydrogenase activity (non-traceable author statement from UniProtKB).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0004616; Molecular function: phosphogluconate dehydrogenase (decarboxylating) activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006098; Biological process: pentose-phosphate shunt (inferred from electronic annotation from InterPro).
GO:0006573; Biological process: valine metabolic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002204; 3-OH-isobutyrate_DHase-rel_CS.
IPR015815; 3hydroxyacid_DHase/Rdtase.
IPR006183; 6-phosphogluconate_DHase.
IPR006115; 6PGDH_NAD-bd.
IPR013328; DHase_multihelical.
IPR011548; IsoBut3OH_DH.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR22981; 3hydroxy_acid_DH; 1.
Pfam PF03446; NAD_binding_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00076; 6PGDHDRGNASE.
TIGRFAMs TIGR01692; HIBADH; 1.
PROSITE PS00895; 3_HYDROXYISOBUT_DH; 1.
ProtoNet P31937.
Genome annotation databases
Ensembl ENSG00000106049; Homo sapiens. [Contig view]
GeneID 11112; -.
KEGG hsa:11112; -.
Phylogenomic databases
HOGENOM P31937; -.
HOVERGEN P31937; -.
Other
DrugBank DB00157; NADH.
NextBio 42238; -.
SOURCE HIBADH; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    36  36     Mitochondrion. 
CHAIN   37   336  300     3-hydroxyisobutyrate dehydrogenase, mitochondrial. PRO_0000007158
NP_BIND   40    68  29     NAD. 
NP_BIND   103   104  2     NAD. 
ACT_SITE   209   209        By similarity. 
BINDING   108   108        NAD. 
BINDING   134   134        NAD. 
BINDING   284   284        NAD. 
STRAND   42    45  4      
HELIX   51    60  10      
STRAND   65    68  4      
HELIX   73    79  7      
TURN   80    82  3      
HELIX   89    95  7      
STRAND   97   101  5      
HELIX   106   114  9      
HELIX   119   121  3      
STRAND   128   131  4      
HELIX   137   149  13      
STRAND   153   156  4      
STRAND   159   161  3      
HELIX   162   168  7      
STRAND   171   177  7      
HELIX   179   181  3      
HELIX   182   189  8      
TURN   190   192  3      
STRAND   193   201  9      
HELIX   204   232  29      
HELIX   237   245  9      
HELIX   252   256  5      
TURN   261   263  3      
STRAND   265   267  3      
HELIX   268   271  4      
STRAND   275   278  4      
HELIX   279   295  17      
HELIX   301   314  14      
TURN   315   317  3      
HELIX   323   325  3      
HELIX   326   330  5      
Sequence information
Length: 336 AA [This is the length of the unprocessed precursor] Molecular weight: 35329 Da [This is the MW of the unprocessed precursor] CRC64: DA3128774A91AF48 [This is a checksum on the sequence]
        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 

P31937 in FASTA format

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