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Identification
HMDB Protein ID HMDBP00982
Secondary Accession Numbers
  • 6270
  • HMDBP07422
Name Methylglutaconyl-CoA hydratase, mitochondrial
Synonyms
  1. AU-binding protein/enoyl-CoA hydratase
  2. AU-specific RNA-binding enoyl-CoA hydratase
Gene Name AUH
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA. Has very low enoyl-CoA hydratase activity. Was originally identified as RNA-binding protein that binds in vitro to clustered 5'-AUUUA-3' motifs.
Pathways
  • 2-Methyl-3-Hydroxybutryl CoA Dehydrogenase Deficiency
  • 3-Hydroxy-3-Methylglutaryl-CoA Lyase Deficiency
  • 3-hydroxyisobutyric acid dehydrogenase deficiency
  • 3-hydroxyisobutyric aciduria
  • 3-Methylcrotonyl Coa Carboxylase Deficiency Type I
  • 3-Methylglutaconic Aciduria Type I
  • 3-Methylglutaconic Aciduria Type III
  • 3-Methylglutaconic Aciduria Type IV
  • Beta-Ketothiolase Deficiency
  • Isobutyryl-coa dehydrogenase deficiency
  • Isovaleric acidemia
  • Isovaleric Aciduria
  • L-leucine degradation
  • Maple Syrup Urine Disease
  • Methylmalonate Semialdehyde Dehydrogenase Deficiency
  • Methylmalonic Aciduria
  • Propionic Acidemia
  • Valine, Leucine and Isoleucine Degradation
  • Valine, leucine and isoleucine degradation
Reactions
3-Hydroxy-3-methylglutaryl-CoA → 3-Methylglutaconyl-CoA + Water details
3-Hydroxy-3-methylglutaryl-CoA → 3-Methylglutaconyl-CoA + Water details
GO Classification
Biological Process
branched-chain amino acid catabolic process
leucine catabolic process
mRNA catabolic process
Cellular Component
mitochondrial matrix
Function
catalytic activity
Molecular Function
enoyl-CoA hydratase activity
methylglutaconyl-CoA hydratase activity
mRNA 3'-UTR binding
Process
metabolic process
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 9
Locus 9q22.31
SNPs AUH
Gene Sequence
>1020 bp
ATGGCGGCCGCGGTGGCGGCGGCACCTGGGGCCTTGGGATCCCTGCATGCTGGCGGCGCC
CGCCTGGTGGCCGCTTGCAGTGCGTGGCTCTGCCCGGGGTTGAGGCTGCCCGGCTCGTTG
GCAGGCCGGCGAGCGGGCCCGGCGATCTGGGCCCAGGGCTGGGTACCTGCGGCCGGGGGT
CCCGCCCCGAAAAGGGGCTACAGCTCTGAGATGAAGACGGAGGACGAGCTGCGGGTGCGG
CACCTGGAGGAGGAGAACCGAGGAATTGTGGTGCTTGGAATAAACAGAGCTTATGGCAAA
AATTCACTCAGTAAAAATCTTATAAAAATGCTATCAAAAGCTGTGGATGCTTTGAAATCT
GATAAGAAAGTACGGACCATAATAATCAGGAGTGAAGTCCCAGGGATATTCTGTGCTGGT
GCTGACCTTAAGGAAAGAGCCAAAATGAGTTCCAGTGAAGTTGGTCCTTTTGTCTCCAAA
ATAAGAGCAGTGATTAACGATATTGCTAATCTTCCAGTGCCAACAATTGCAGCAATAGAT
GGACTCGCTTTAGGTGGTGGTCTTGAACTGGCTTTAGCCTGTGATATACGAGTAGCAGCT
TCCTCTGCAAAAATGGGCCTGGTTGAAACAAAATTGGCGATTATTCCTGGTGGAGGGGGG
ACACAGCGATTGCCACGCGCCATTGGAATGTCCCTGGCCAAGGAGCTCATATTCTCTGCG
CGAGTCCTCGATGGCAAAGAAGCCAAAGCAGTGGGCTTAATCAGCCACGTTCTGGAACAG
AACCAGGAGGGAGACGCGGCCTACAGGAAGGCCTTGGACCTGGCGAGAGAGTTTTTACCT
CAGGGACCTGTTGCAATGAGAGTGGCAAAATTAGCAATTAATCAAGGGATGGAGGTCGAT
TTAGTAACAGGGTTAGCCATAGAAGAAGCTTGTTATGCTCAGACCATTCCAACAAAAGAC
AGACTTGAAGGTCTTCTTGCTTTTAAAGAGAAAAGGCCCCCTCGCTATAAAGGAGAATAA
Protein Properties
Number of Residues 339
Molecular Weight 35608.18
Theoretical pI 9.476
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Methylglutaconyl-CoA hydratase, mitochondrial
MAAAVAAAPGALGSLHAGGARLVAACSAWLCPGLRLPGSLAGRRAGPAIWAQGWVPAAGG
PAPKRGYSSEMKTEDELRVRHLEEENRGIVVLGINRAYGKNSLSKNLIKMLSKAVDALKS
DKKVRTIIIRSEVPGIFCAGADLKERAKMSSSEVGPFVSKIRAVINDIANLPVPTIAAID
GLALGGGLELALACDIRVAASSAKMGLVETKLAIIPGGGGTQRLPRAIGMSLAKELIFSA
RVLDGKEAKAVGLISHVLEQNQEGDAAYRKALDLAREFLPQGPVAMRVAKLAINQGMEVD
LVTGLAIEEACYAQTIPTKDRLEGLLAFKEKRPPRYKGE
GenBank ID Protein 780241
UniProtKB/Swiss-Prot ID Q13825
UniProtKB/Swiss-Prot Entry Name AUHM_HUMAN
PDB IDs
GenBank Gene ID X79888
GeneCard ID AUH
GenAtlas ID AUH
HGNC ID HGNC:890
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  3. Nakagawa J, Waldner H, Meyer-Monard S, Hofsteenge J, Jeno P, Moroni C: AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity. Proc Natl Acad Sci U S A. 1995 Mar 14;92(6):2051-5. [PubMed:7892223 ]
  4. IJlst L, Loupatty FJ, Ruiter JP, Duran M, Lehnert W, Wanders RJ: 3-Methylglutaconic aciduria type I is caused by mutations in AUH. Am J Hum Genet. 2002 Dec;71(6):1463-6. Epub 2002 Nov 14. [PubMed:12434311 ]
  5. Kurimoto K, Fukai S, Nureki O, Muto Y, Yokoyama S: Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase. Structure. 2001 Dec;9(12):1253-63. [PubMed:11738050 ]
  6. Ly TB, Peters V, Gibson KM, Liesert M, Buckel W, Wilcken B, Carpenter K, Ensenauer R, Hoffmann GF, Mack M, Zschocke J: Mutations in the AUH gene cause 3-methylglutaconic aciduria type I. Hum Mutat. 2003 Apr;21(4):401-7. [PubMed:12655555 ]