We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for 2-Acetolactate (HMDB06833)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-08-12 17:59:57
Update Date 2009-05-05 21:01:15
Accession Number HMDB06833
Secondary Accession Numbers Not Available
Common Name 2-Acetolactate
Description 2-Acetolactate is involved in the butanoate metabolism and pantothenate and CoA biosynthesis pathways. In the butanoate metabolism pathway, 2-Acetolactate is created from 2-(alpha-Hydroxyethyl)thiamine diphosphate by acetolactate synthase [EC:2.2.1.6]. 2-Acetolactate is then converted to (R)-Acetoin by acetolactate decarboxylase [EC:4.1.1.5]. In the pantothenate and CoA pathway, 2-Acetolactate is irreversibly created from pyruvate by acetolactate synthase [EC:2.2.1.6]. 2-Acetolactate is then irreversibly converted to 2,3-Dihydroxy-3-methylbutanoate by ketol-acid reductoisomerase [EC:1.1.1.86].
Synonyms Not Available
Chemical IUPAC Name Not Available
Chemical Formula C5H8O4
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
  • tertiary alcohol
  • carboxylic acid
  • alpha-hydroxyacid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 132.115
Monoisotopic Molecular Weight 132.042252
Isomeric SMILES CC(=O)C(C)(O)C(O)=O
Canonical SMILES CC(=O)C(C)(O)C(O)=O
KEGG Compound ID C00900 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB06833 Link Image
Metagene Link HMDB06833 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C5H8O4/c1-3(6)5(2,9)4(7)8/h9H,1-2H3,(H,7,8)
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 286.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.65 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
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 Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways Not Available
General References Not Available
Metabolic Enzymes
  1. Acetolactate synthase-like protein
Enzyme 1 [top]
Enzyme 1 ID 13009
Enzyme 1 Name Acetolactate synthase-like protein
Enzyme 1 Synonyms
  1. IlvB-like protein
Enzyme 1 Gene Name ILVBL
Enzyme 1 Protein Sequence >Acetolactate synthase-like protein 
METPAAAAPAGSLFPSFLLLACGTLVAALLGAAHRLGLFYQLLHKVDKASVRHGGENVAA
VLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAV
TAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVR
RVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMVPAKPPKGLVGRVVSWY
LENYLANLFAGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPTS
ADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLAGTVCDFRLSY
GRVLSHSSKIIIVNRNREEMLLNSDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVE
ELREADRQKEQTFREKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQ
PRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIP
VMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLSRENEDQVVKV
LHDAQQQCRDGHPVVVNILIGRTDFRDGSIAV
Enzyme 1 Number of Residues 632
Enzyme 1 Molecular Weight 67867.2
Enzyme 1 Theoretical pI 8.22
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • thiamin pyrophosphate binding
  • transferase activity
  • vitamin binding
Process
—
Component
—
Enzyme 1 General Function Involved in magnesium ion binding
Enzyme 1 Specific Function Not Available
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 13-33
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2725625 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID A1L0T0 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ILVBL_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1899 bp 
ATGGAGACCCCCGCGGCCGCCGCCCCCGCTGGGAGCTTATTCCCCTCCTTCCTGCTCCTG
GCCTGCGGGACGCTGGTGGCCGCCTTGCTGGGCGCCGCTCACCGCCTGGGGCTCTTCTAT
CAGCTGCTGCACAAGGTGGACAAGGCAAGCGTCCGGCATGGCGGAGAGAACGTGGCCGCT
GTGCTGAGGGCCCATGGTGTGCGGTTCATCTTCACGCTGGTCGGTGGGCACATTTCCCCG
CTGCTGGTGGCCTGTGAGAAACTGGGCATCCGTGTGGTGGACACACGCCATGAGGTCACG
GCCGTCTTTGCTGCTGATGCTATGGCCCGCCTGTCCGGGACGGTGGGCGTGGCGGCAGTG
ACAGCAGGCCCTGGCCTCACCAACACGGTGACTGCGGTGAAGAATGCTCAGATGGCTCAG
TCCCCAATCCTGCTTCTGGGTGGGGCTGCCAGCACTCTGCTGCAGAACCGGGGTGCGCTC
CAGGCTGTTGATCAGCTGTCCCTTTTCCGGCCACTCTGTAAGTTTTGTGTGTCTGTGCGG
AGGGTGCGGGACATTGTGCCCACCCTGAGGGCCGCGATGGCTGCCGCCCAGTCGGGCACC
CCAGGTCCGGTGTTTGTGGAGCTGCCCGTTGACGTGCTGTACCCCTACTTCATGGTCCAG
AAGGAGATGGTGCCAGCCAAGCCACCCAAGGGCCTCGTGGGCCGAGTGGTCTCCTGGTAT
TTAGAGAATTACCTGGCCAACCTCTTTGCAGGAGCCTGGGAGCCTCAGCCCGAGGGACCG
CTGCCCCTGGACATCCCCCAGGCTTCCCCGCAGCAGGTTCAGCGCTGTGTGGAGATCCTG
AGCCGGGCCAAGAGGCCTCTGATGGTGCTGGGGAGTCAGGCCCTGCTCACCCCAACGTCT
GCCGACAAGCTTCGGGCTGCCGTGGAGACCTTGGGTGTTCCCTGCTTCCTTGGAGGGATG
GCACGGGGGCTGTTAGGCCGCAACCACCCCCTCCACATCCGGGAGAACCGCAGTGCGGCC
CTGAAGAAGGCGGATGTCATTGTCCTAGCAGGAACTGTGTGTGACTTCCGCCTATCCTAT
GGCCGTGTCCTCAGCCACAGCAGCAAGATCATCATCGTCAATCGTAATCGGGAAGAGATG
TTGCTCAACTCAGACATCTTCTGGAAGCCCCAGGAGGCTGTGCAGGGAGATGTGGGTTCC
TTCGTGCTGAAGTTAGTGGAGGGCCTTCAGGGCCAGACCTGGGCCCCAGACTGGGTGGAG
GAGCTGCGGGAAGCCGACCGGCAGAAGGAGCAGACCTTTCGGGAGAAGGCAGCGATGCCT
GTGGCCCAGCACCTGAACCCAGTGCAGGTGCTGCAGCTGGTGGAGGAAACGCTACCTGAC
AACTCAATTCTGGTGGTGGATGGCGGGGACTTCGTGGGCACTGCTGCCCATCTGGTACAG
CCCCGCGGCCCCCTGCGCTGGCTCGATCCTGGGGCCTTTGGGACTCTGGGAGTTGGTGCA
GGATTTGCACTTGGGGCCAAGCTGTGCCGGCCAGATGCTGAGGTCTGGTGCCTGTTTGGG
GACGGAGCTTTTGGCTACAGCCTCATCGAATTTGATACATTCGTCAGACACAAGATCCCA
GTGATGGCCTTGGTAGGGAATGATGCTGGCTGGACACAGATTTCTCGGGAGCAGGTGCCC
TCTCTGGGCAGCAACGTGGCCTGTGGCCTGGCCTACACTGATTATCACAAGGCAGCCATG
GGTCTGGGGGCCCGGGGCTTGCTGCTCTCACGGGAGAACGAGGATCAGGTGGTCAAGGTG
CTGCACGATGCCCAGCAGCAGTGCCGAGACGGCCACCCGGTTGTGGTCAACATCCTCATT
GGGAGGACGGACTTCCGCGATGGCTCCATTGCTGTATAG
Enzyme 1 GenBank Gene ID AC003956 Link Image
Enzyme 1 GeneCard ID ILVBL Link Image
Enzyme 1 GenAtlas ID ILVBL Link Image
Enzyme 1 HGNC ID HGNC:6041 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 19p13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Joutel A, Ducros A, Alamowitch S, Cruaud C, Domenga V, Marechal E, Vahedi K, Chabriat H, Bousser MG, Tournier-Lasserve E: A human homolog of bacterial acetolactate synthase genes maps within the CADASIL critical region. Genomics. 1996 Dec 1;38(2):192-8. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. 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 Link Image]
Enzyme 1 Metabolite References Not Available