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Bovine Rumen Metabolome Database



Showing metabocard for Acetoacetic acid (RMDB00060)

Legend: metabolite field enzyme field

Version 1.0
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-06 15:30:00
Accession Number RMDB00060
Common Name Acetoacetic acid
Description It is a weak organic acid one of the ketone bodies produced in the liver and occurring in excess in the blood and urine in ketosis.. Persistent mild hyperketonemia is a common finding in newborns. These compounds serve as an indispensable source of energy for extrahepatic tissues, especially the brain and lung of developing rats. Another important function of ketone bodies is to provide acetoacetyl-CoA and acetyl-CoA for synthesis of cholesterol, fatty acids, and complex lipids. During the early postnatal period, acetoacetate (AcAc) and beta-hydroxybutyrate are preferred over glucose as substrates for synthesis of phospholipids and sphingolipids in accord with requirements for brain growth and myelination. Thus, during the first 2 wk of postnatal development, when the accumulation of cholesterol and phospholipids accelerates, the proportion of ketone bodies incorporated into these lipids increases. On the other hand, an increased proportion of ketone bodies are utilized for cerebroside synthesis during the period of active myelination. In the lung, AcAc serves better than glucose as a precursor for the synthesis of lung phospholipids. The synthesized lipids, particularly dipalmityl phosphatidylcholine, are incorporated into surfactant, and thus have a potential role in supplying adequate surfactant lipids to maintain lung function during the early days of life. (PMID 3884391) The acid is also present in the metabolism of those undergoing starvation or prolonged physical exertion as part of gluconeogenesis. When ketone bodies are measured by way of urine concentration, acetoacetic acid, along with beta-hydroxybutyric acid or acetone, is what is detected.
Synonyms
  1. 3-Ketobutyrate
  2. 3-Oxo-butanoate
  3. 3-Oxo-butanoic acid
  4. 3-Oxobutyrate
  5. 3-Oxobutyric acid
  6. Acetoacetate
  7. diacetate
  8. diacetic acid
  9. 3-Ketobutyric acid
Chemical IUPAC Name 3-oxobutanoic acid
Chemical Formula C4H6O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Keto-Acids
Sub Class
  • Short chain keto-acids
Family
  • Mammalian_Metabolite
Species
  • ketone; carboxylic acid
Biofunction
  • Component of Butanoate metabolism; Component of Tyrosine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 102.089
Monoisotopic Molecular Weight 102.031693
Isomeric SMILES CC(=O)CC(O)=O
Canonical SMILES CC(=O)CC(O)=O
KEGG Compound ID C00164 Link Image
BioCyc ID 3-KETOBUTYRATE Link Image
BiGG ID 1485291 Link Image
Wikipedia Link Acetoacetic acid Link Image
METLIN ID 276 Link Image
PubChem Compound 96 Link Image
PubChem Substance 3464 Link Image
ChEBI ID 15344 Link Image
CAS Registry Number 541-50-4
InChI Identifier InChI=1/C4H6O3/c1-3(5)2-4(6)7/h2H2,1H3,(H,6,7)
Synthesis Reference Lopez-Soriano, F. J.; Argiles, J. M. A simple method for the preparation of acetoacetate. Analytical Letters (1985), 18(B5), 589-92.
Melting Point (Experimental) 36.5 oC
Experimental Water Solubility 1000 mg/mL at 20 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 240.00002 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.47 [Predicted by ALOGPS]; 0 [Predicted by PubChem via XLOGP]; -0.98 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1QCO Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
  • peroxisome
Biofluid Location
  • Cow_Milk
  • Rumen
Tissue Location
Concentrations (Normal)
Biofluid Rumen
Value 67.72 +/- 9.42 uM
Age 4-5 years old
Sex Female (lactating)
Condition Normal (0% barley grain in dry matter (DM) basis)
Breed Holstein-Friesian
Experimental Condition Rumen fluid for the analysis was collected 15-20 minutes before the morning feeding on days 12 and 21 of each experimental period. Cows were fed once daily at 0800.
Comments Not Available
References
  • The rumen metabolome (in preparation)
Biofluid Rumen
Value 48.3 +/- 1.7 uM
Age N/A
Sex Female
Condition Normal
Breed Not Available
Experimental Condition Not Available
Comments Not Available
References
  • Metabolomics reveals unhealthy alterations in rumen metabolism with increased proportion of cereal grain in the diet of dairy cows. Burim N. Ametaj, Qendrim Zebeli, Fozia Saleem, Nikolaos Psychogios, Michael J. Lewis, Suzanna M. Dunn, Jianguo Xia and David S. Wishart Metabolomics 2010;6(4):583-594
Concentrations (Abnormal)
Biofluid Rumen
Value 64 +/- 9 uM
Age 4-5 years old
Sex Female (lactating)
Condition 15% barley grain in dry matter (DM) basis
Breed Holstein-Friesian
Experimental Condition Rumen fluid for the analysis was collected 15-20 minutes before the morning feeding on days 12 and 21 of each experimental period. Cows were fed once daily at 0800.
Comments Not Available
References
  • The rumen metabolome (in preparation)
Biofluid Rumen
Value 78 +/- 15 uM
Age 4-5 years old
Sex Female (lactating)
Condition 30% barley grain in dry matter (DM) basis
Breed Holstein-Friesian
Experimental Condition Rumen fluid for the analysis was collected 15-20 minutes before the morning feeding on days 12 and 21 of each experimental period. Cows were fed once daily at 0800.
Comments Not Available
References
  • The rumen metabolome (in preparation)
Biofluid Rumen
Value 80 +/- 27 uM
Age 4-5 years old
Sex Female (lactating)
Condition 45% barley grain in dry matter (DM) basis
Breed Holstein-Friesian
Experimental Condition Rumen fluid for the analysis was collected 15-20 minutes before the morning feeding on days 12 and 21 of each experimental period. Cows were fed once daily at 0800.
Comments Not Available
References
  • The rumen metabolome (in preparation)
Pathway Names Not Available
HMDB Pathways Not Available
KEGG Pathways Not Available
SimCell Pathways Not Available
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Fumarylacetoacetase
  2. Hydroxyacid-oxoacid transhydrogenase, mitochondrial
  3. 3-hydroxybutyrate dehydrogenase type 2
  4. D-beta-hydroxybutyrate dehydrogenase, mitochondrial
  5. Hydroxymethylglutaryl-CoA lyase, mitochondrial
Enzyme 1 [top]
Enzyme 1 ID 427
Enzyme 1 Name Fumarylacetoacetase
Enzyme 1 Synonyms
  1. FAA
  2. Fumarylacetoacetate hydrolase
  3. Beta-diketonase
Enzyme 1 Gene Name FAH
Enzyme 1 Protein Sequence >Fumarylacetoacetase
MSFVPVAEDSDFPIHNLPYGVFSTRGNPRPRIGVAIGDQILDLSVIKHLFTGPILSGHQD
VFNKPTLNSFMGLGQAAWKEARAFLQNLLSASQARLRDDVELRQRAFTSQASATMYLPAT
IGDYTDFYSSRHHATNVGVMFRGKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPLGQM
RPDDSKPPVYGACKLLDFELEMAFFVGPGNKLGEPIPISKAHEHIFGMVLMNDWSARDIQ
KWEYVPLGPFLGKSFGTTISPWVVPMDALMPFAVSNPEQDPKPLPYLCHDQPYTFDINLS
VALKGEGMSQAATICRSNFKYMYWTMLQQLTHHSVNGCNLQPGDLLASGTISGPEPESFG
CMLELSWKGTRAVELGNGQTRKFLLDGDEVIMTGHCQGDGYRIGFGQCAGKVLPALSFA
Enzyme 1 Number of Residues 419
Enzyme 1 Molecular Weight 46155.6
Enzyme 1 Theoretical pI 6.99
Enzyme 1 GO Classification
Function
Process
Component
Enzyme 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 1 Specific Function 4-fumarylacetoacetate + H(2)O = acetoacetate + fumarate
Enzyme 1 Pathways
  • Amino-acid degradation
  • L-phenylalanine degradation
  • acetoacetate and fumarate from L-phenylalanine:step 6/6
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 148745316 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID A5PKH3 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name FAAA_BOVIN Link Image
Enzyme 1 PDB ID 1QQJ Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1260 bp
ATGTCCTTCGTCCCGGTGGCCGAGGATTCTGACTTCCCCATCCACAACCTGCCCTACGGC
GTCTTCTCCACCCGAGGCAACCCAAGACCGAGGATTGGCGTGGCCATTGGGGACCAGATC
CTGGACCTCAGTGTCATCAAGCACCTCTTCACTGGGCCGATCCTCTCCGGACACCAGGAT
GTCTTCAATAAGCCAACTCTCAACAGCTTCATGGGCCTGGGTCAGGCTGCCTGGAAGGAG
GCTAGAGCATTCTTGCAGAACCTGCTGTCTGCCAGCCAAGCCAGGCTCAGAGATGACGTG
GAGCTTCGGCAGCGTGCCTTCACATCCCAGGCTTCCGCTACGATGTATCTTCCGGCCACC
ATAGGTGACTACACGGACTTCTATTCCTCTCGGCATCATGCCACCAATGTCGGGGTTATG
TTCAGGGGCAAGGAGAATGCACTGATGCCAAACTGGCTGCACCTGCCCGTGGGCTACCAC
GGGCGCGCTTCCTCCGTGGTGGTGTCTGGCACCCCGATCCGCAGGCCCCTGGGGCAGATG
CGACCCGACGACTCTAAGCCTCCCGTTTATGGTGCCTGCAAACTCCTGGACTTCGAGTTG
GAGATGGCTTTCTTTGTAGGCCCTGGGAACAAACTCGGAGAGCCAATCCCCATTTCCAAG
GCCCACGAGCACATTTTTGGAATGGTCCTTATGAACGACTGGAGTGCTCGAGACATCCAG
AAATGGGAGTACGTCCCACTTGGGCCGTTCCTTGGGAAGAGTTTTGGAACCACCATCTCT
CCGTGGGTGGTGCCCATGGATGCCCTCATGCCCTTTGCTGTGTCCAACCCGGAGCAGGAC
CCCAAGCCCCTGCCGTATCTCTGCCATGACCAGCCCTACACATTCGACATCAACCTCTCT
GTTGCCCTGAAAGGAGAAGGAATGAGCCAGGCAGCTACCATATGCAGGTCTAATTTTAAG
TACATGTACTGGACAATGCTGCAGCAGCTCACCCACCACTCTGTCAATGGCTGCAACCTG
CAGCCGGGCGACCTCTTGGCTTCTGGAACCATCAGCGGGCCGGAGCCAGAGAGCTTCGGC
TGCATGCTGGAGCTGTCGTGGAAGGGCACAAGGGCCGTAGAGCTGGGGAATGGCCAGACC
AGGAAGTTCCTGCTGGATGGGGATGAAGTCATCATGACAGGGCACTGCCAGGGGGATGGG
TACCGCATTGGCTTCGGCCAGTGTGCGGGAAAAGTGCTGCCTGCCCTGTCGTTCGCCTGA
Enzyme 1 GenBank Gene ID BC142487 Link Image
Enzyme 1 GeneCard ID FAH Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Chromosome:1
Enzyme 1 Locus 15q23-q25
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References Not Available
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 595
Enzyme 2 Name Hydroxyacid-oxoacid transhydrogenase, mitochondrial
Enzyme 2 Synonyms
  1. HOT
  2. Alcohol dehydrogenase iron-containing protein 1
Enzyme 2 Gene Name ADHFE1
Enzyme 2 Protein Sequence >Hydroxyacid-oxoacid transhydrogenase, mitochondrial
MAAARSRVVHLLRLLQRAACQCPSHSHTYSQAPGLSPSGKTTDYAFEMAVSTIRYGAGVT
KEVGMDLQSMGAKNVCLMTDKNLSQLPPVQTVMDSLVKNGINFKVYDHVRVEPTDTSFME
AIEFAKKGAFDAFLAVGGGSTIDTCKAANLYSSSPDSDFLDYVNAPIGKGKPVTVPLKPL
IAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLIDPLHTLHMPERVVANSGF
DVLCHALESYTALPYHMRSPCPSSPITRPAYQGSNPISDIWAVHALRIVAKYLKRAIRNP
DDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKDYNVDHPLVPHGLSV
VLTSPAVFTFTSQMFPERHLEVAEILGADTRTARRPDAGPVLADTLRKFLFDLDVDDGLA
AIGYSKADIPELVKGTLPQERVTKLAPRPQSEEDLSALFEASMKLY
Enzyme 2 Number of Residues 466
Enzyme 2 Molecular Weight 50342.2
Enzyme 2 Theoretical pI 7.65
Enzyme 2 GO Classification
Function
Process
Component
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2- hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2-KG as hydrogen acceptor, resulting in the formation of D-2-HG
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 151553907 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID A6QP15 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HOT_BOVIN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1401 bp
ATGGCCGCCGCTCGCTCTCGGGTAGTGCACTTGCTGAGGCTTCTGCAACGCGCAGCATGC
CAGTGCCCGAGTCATTCTCATACTTATTCCCAAGCTCCTGGACTTTCACCTTCTGGGAAA
ACAACAGATTATGCCTTCGAGATGGCTGTTTCAACTATTAGATATGGAGCAGGAGTTACA
AAGGAAGTGGGCATGGACCTACAAAGCATGGGTGCTAAAAATGTTTGTTTGATGACAGAC
AAGAACCTCTCCCAACTCCCTCCTGTACAGACAGTGATGGATTCCCTAGTGAAGAATGGC
ATAAACTTTAAGGTTTATGATCATGTGAGAGTGGAACCAACTGATACAAGCTTCATGGAA
GCCATTGAATTTGCCAAAAAGGGAGCTTTCGATGCCTTCCTGGCCGTGGGTGGCGGTTCC
ACCATAGACACCTGTAAAGCCGCTAATCTGTATTCATCCAGCCCTGACTCTGACTTCCTA
GACTACGTCAATGCCCCCATTGGGAAGGGAAAGCCTGTGACTGTGCCTCTGAAACCTCTG
ATCGCAGTTCCAACTACCTCAGGCACTGGGAGCGAAACTACCGGAGTTGCCATTTTTGAC
TACGAACACTTGAAAGTAAAAACTGGCATTGCTTCGCGAGCCATCAAACCCACACTCGGC
CTGATTGATCCTCTACACACCCTGCACATGCCTGAGCGGGTGGTCGCCAACAGTGGCTTC
GATGTGCTCTGCCACGCCCTGGAGTCCTACACTGCCCTCCCATATCACATGCGGAGCCCC
TGCCCTTCAAGCCCTATCACTCGGCCAGCCTACCAGGGCAGCAACCCCATCAGTGACATC
TGGGCAGTCCACGCACTGCGGATCGTTGCCAAGTATCTGAAGAGGGCTATCAGAAATCCT
GATGATCTTGAAGCAAGGTCTAATATGCACTTGGCAAGTGCTTTTGCTGGCATTGGCTTT
GGAAATGCTGGTGTTCATCTATGCCATGGAATGTCTTACCCAATTTCTGGCTTAGTGAAG
ACTTATAAAGCAAAGGATTACAATGTGGATCATCCCCTGGTGCCTCATGGCCTTTCTGTG
GTGCTCACCTCCCCAGCAGTGTTCACATTTACATCACAGATGTTTCCTGAGCGGCACTTG
GAAGTGGCAGAAATATTGGGAGCTGACACCCGCACTGCCAGGAGGCCAGATGCTGGGCCT
GTCTTGGCAGACACGCTGCGGAAATTCTTATTCGATCTGGATGTGGATGACGGCCTGGCT
GCCATTGGCTACTCCAAGGCCGACATCCCCGAGCTGGTGAAAGGAACGCTGCCCCAGGAA
AGAGTCACCAAGCTTGCACCACGCCCTCAGTCAGAAGAGGATCTATCTGCTCTGTTTGAA
GCATCAATGAAACTGTATTAA
Enzyme 2 GenBank Gene ID BC149097 Link Image
Enzyme 2 GeneCard ID ADHFE1 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Chromosome:8
Enzyme 2 Locus 8q13.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 1009
Enzyme 3 Name 3-hydroxybutyrate dehydrogenase type 2
Enzyme 3 Synonyms
  1. R-beta-hydroxybutyrate dehydrogenase
  2. Dehydrogenase/reductase SDR family member 6
Enzyme 3 Gene Name BDH2
Enzyme 3 Protein Sequence >3-hydroxybutyrate dehydrogenase type 2
MGRLDGKVIVLTAAAQGIGRAAALAFAKEGAKVIATDINDSKLQELDKYPGIHTRVLDVT
KKKQIDQFANDIERLDVLFNVAGFVHHGTILDCEETDWDFSMNLNVRSMYLMIKAFLPKM
MAQKSGNIINMSSVASSIKGVVNRCVYSTTKAAVIGLTKSVAADFIQQGIRCNCVCPGTV
DTPSLQERIQARPNPEEALSDFLKRQKTGRFATAEEVALLCVYLASDESAYITGNPVIID
GGWSL
Enzyme 3 Number of Residues 245
Enzyme 3 Molecular Weight 26661.5
Enzyme 3 Theoretical pI 7.30
Enzyme 3 GO Classification
Function
Process
Component
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + NADH
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 74355014 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q3T046 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name BDH2_BOVIN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >738 bp
ATGGGTCGACTTGATGGGAAGGTCATTGTCCTGACGGCTGCTGCTCAGGGGATCGGCCGG
GCAGCCGCATTGGCTTTTGCAAAAGAAGGTGCCAAAGTCATAGCCACCGATATCAATGAC
TCCAAACTTCAGGAACTGGATAAGTACCCAGGTATTCACACTCGGGTCCTTGATGTCACA
AAGAAGAAGCAAATTGACCAGTTTGCCAATGACATTGAGAGACTTGATGTTCTCTTTAAC
GTTGCTGGTTTCGTCCATCACGGAACCATCCTGGACTGTGAAGAGACAGACTGGGACTTC
TCGATGAACCTCAACGTCCGCAGCATGTACCTGATGATCAAGGCTTTTCTTCCTAAGATG
ATGGCTCAGAAATCTGGCAACATTATCAACATGTCCTCTGTGGCTTCCAGCATCAAAGGC
GTTGTGAACAGGTGCGTGTACAGCACAACCAAGGCGGCCGTGATCGGCCTCACAAAGTCC
GTGGCTGCAGACTTCATCCAGCAGGGTATCCGGTGCAACTGTGTGTGTCCAGGAACAGTT
GATACCCCATCTCTGCAAGAAAGAATACAAGCCAGACCAAATCCTGAAGAGGCACTGAGC
GATTTCCTAAAGAGACAGAAAACAGGAAGATTTGCAACTGCAGAAGAAGTAGCCCTGCTC
TGCGTGTACTTGGCCTCTGATGAATCTGCCTACATCACGGGGAATCCTGTCATCATTGAT
GGAGGCTGGAGTTTGTGA
Enzyme 3 GenBank Gene ID BC102567 Link Image
Enzyme 3 GeneCard ID BDH2 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Chromosome:4
Enzyme 3 Locus 4q24
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 1010
Enzyme 4 Name D-beta-hydroxybutyrate dehydrogenase, mitochondrial
Enzyme 4 Synonyms
  1. BDH
  2. 3-hydroxybutyrate dehydrogenase
Enzyme 4 Gene Name BDH1
Enzyme 4 Protein Sequence >D-beta-hydroxybutyrate dehydrogenase, mitochondrial
MLTARLSRPLSQLPRKTLNFSDRENGTRGSLLLYSAPFVPVGRRTYAASVDPVGSKAVLI
TGCDSGFGFSLAKHLHSEGFLVFAGCLMKDKGSDGVKELDSMKSDRLRTVQLNVCKSEEV
DKAAEVIRSSLEDPEKGLWGLVNNAGISTFGDVEFTSMETYKEVAEVNLWGTVRVTKAFL
PLIRRAKGRVVNISSMMGRMANVARSPYCITKFGVEAFSDCLRYEMHPLGVKVSVVEPGN
FIAATSLYGGTERIQAIANKMWEELPEVVRQDYGRKYFDEKVARMESYCTSGSTDTSPVI
KAVTHALTATTPYTRYHPMDYYWWLRMQIMTHFPGAISDRIYIH
Enzyme 4 Number of Residues 344
Enzyme 4 Molecular Weight 38390.8
Enzyme 4 Theoretical pI 8.90
Enzyme 4 GO Classification
Function
Process
Component
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + NADH
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 73587365 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q02337 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name BDH_BOVIN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1035 bp
ATGCTAACAGCCCGCCTCTCCAGACCCCTGTCACAGCTTCCAAGGAAAACCCTGAATTTC
TCTGATAGAGAAAATGGGACAAGAGGCTCGCTGCTGCTTTACTCTGCGCCCTTTGTTCCT
GTTGGCCGTCGGACTTACGCTGCTTCAGTGGACCCGGTTGGCAGCAAAGCTGTCCTGATC
ACGGGCTGTGACTCGGGATTTGGGTTCTCCTTGGCCAAGCATCTGCATTCAGAAGGCTTC
CTTGTGTTTGCTGGCTGTTTGATGAAGGACAAAGGGAGTGATGGGGTCAAAGAGCTGGAC
AGCATGAAGAGTGATCGCTTAAGAACTGTCCAGCTCAACGTCTGCAAAAGCGAAGAGGTG
GATAAAGCGGCGGAGGTCATCCGCTCAAGCCTGGAGGACCCTGAGAAAGGCTTGTGGGGC
CTGGTTAACAATGCGGGCATCTCGACGTTTGGAGACGTGGAGTTCACCAGCATGGAGACC
TACAAGGAGGTGGCGGAAGTGAACCTCTGGGGCACTGTTCGGGTGACGAAAGCCTTCCTC
CCCCTCATCCGGAGGGCAAAAGGCCGCGTTGTTAACATCAGCAGCATGATGGGCCGCATG
GCCAACGTGGCCCGCTCCCCGTACTGCATCACCAAGTTCGGGGTGGAGGCTTTCTCTGAC
TGCCTGCGCTACGAGATGCACCCGCTGGGAGTAAAGGTCAGCGTGGTGGAACCCGGCAAC
TTCATCGCCGCCACCAGCCTCTACGGCGGTACTGAGCGCATCCAGGCCATCGCCAACAAG
ATGTGGGAGGAGCTGCCTGAGGTGGTGCGCCAGGACTACGGCAGGAAGTACTTCGATGAG
AAGGTCGCCAGGATGGAGAGCTACTGCACCAGCGGCTCCACGGACACCTCTCCTGTCATC
AAGGCTGTGACACACGCCCTGACTGCCACCACTCCCTACACTCGCTACCATCCCATGGAC
TACTACTGGTGGCTGCGGATGCAGATCATGACCCACTTCCCCGGAGCCATCTCCGACAGG
ATCTATATTCACTGA
Enzyme 4 GenBank Gene ID BC103051 Link Image
Enzyme 4 GeneCard ID BDH1 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Chromosome:3
Enzyme 4 Locus 3q29
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. [PubMed Link Image]
  2. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 1139
Enzyme 5 Name Hydroxymethylglutaryl-CoA lyase, mitochondrial
Enzyme 5 Synonyms
  1. HMG-CoA lyase
  2. HL
  3. 3-hydroxy-3-methylglutarate-CoA lyase
Enzyme 5 Gene Name HMGCL
Enzyme 5 Protein Sequence >Hydroxymethylglutaryl-CoA lyase, mitochondrial
MATVKKVLPRRLVGLATLRAVSTSSVGTFPKQVKIVEVGPRDGLQNEKNIVPTPVKIKLI
DMLSEAGLPVVEATSFVSPKWVPQMADHAEVLKGIQKFPGVNYPVLTPNFKGFQAAVAAG
AKEVAIFGAASELFTKKNINCSIDESLQRFDEILKAARAAGISVRGYVSCVLGCPYEGKI
SPAKVAEVTKKLYSMGCYEISLGDTIGVGTPGAMKDMLSAVLQEVPVTALAVHCHDTYGQ
ALANTLTALQMGVSVMDSSVAGLGGCPYAQGASGNLATEDLVYMLAGLGIHTGVNLQKLL
EAGAFICQALNRRTNSKVAQATCKL
Enzyme 5 Number of Residues 325
Enzyme 5 Molecular Weight 34167.6
Enzyme 5 Theoretical pI 8.88
Enzyme 5 GO Classification
Function
Process
Component
Enzyme 5 General Function Amino acid transport and metabolism
Enzyme 5 Specific Function (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl- CoA + acetoacetate
Enzyme 5 Pathways
  • Metabolic intermediate metabolism
  • (S)-3-hydroxy-3- methylglutaryl-CoA degradation
  • acetoacetate from (S)-3-hydroxy-3- methylglutaryl-CoA:step 1/1
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 109939905 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q29448 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name HMGCL_BOVIN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >978 bp
ATGGCGACAGTGAAGAAGGTGCTCCCGCGGAGGCTGGTGGGCTTGGCGACCCTCCGGGCT
GTCAGCACCTCATCTGTGGGTACGTTCCCAAAGCAAGTGAAAATTGTGGAAGTTGGTCCT
CGAGACGGACTACAAAATGAAAAGAATATTGTACCTACTCCAGTGAAAATCAAGCTAATA
GACATGCTTTCCGAAGCAGGACTCCCTGTGGTAGAAGCCACCAGCTTCGTGTCTCCCAAA
TGGGTTCCACAGATGGCTGACCATGCTGAAGTCTTGAAAGGCATCCAGAAATTTCCTGGC
GTCAACTACCCAGTCCTGACCCCAAACTTCAAAGGCTTCCAGGCAGCGGTTGCTGCCGGA
GCCAAGGAAGTGGCCATCTTTGGAGCCGCCTCTGAACTCTTCACCAAGAAGAACATCAAC
TGCTCCATAGATGAGAGTTTGCAGCGGTTTGATGAAATCTTGAAGGCAGCTCGGGCAGCC
GGTATCTCTGTGCGGGGGTACGTCTCCTGTGTGCTTGGATGTCCCTACGAAGGGAAGATC
TCCCCGGCTAAAGTCGCTGAGGTCACCAAGAAGCTGTACTCCATGGGCTGCTACGAGATC
TCCCTGGGGGACACCATCGGCGTGGGCACCCCTGGGGCCATGAAGGACATGCTGTCTGCT
GTCCTGCAGGAGGTGCCAGTGACAGCCCTGGCCGTCCACTGCCATGACACCTACGGCCAG
GCCCTGGCCAACACCTTGACGGCCCTGCAGATGGGAGTGAGTGTCATGGACTCTTCCGTG
GCAGGACTGGGAGGCTGTCCCTATGCACAGGGGGCGTCGGGAAACTTGGCCACCGAGGAC
CTGGTCTACATGCTGGCCGGCCTGGGCATTCACACGGGTGTGAACCTCCAGAAGCTTCTG
GAAGCTGGGGCCTTCATCTGTCAAGCCCTGAACAGAAGAACCAACTCCAAAGTGGCTCAG
GCTACCTGTAAACTGTGA
Enzyme 5 GenBank Gene ID BC118276 Link Image
Enzyme 5 GeneCard ID HMGCL Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Chromosome:1
Enzyme 5 Locus 1p36.1-p35
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available