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Human Metabolome Database Version 2.5

 

Showing metabocard for L-2-Amino-3-oxobutanoic acid (HMDB06454)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-05-23 10:48:15
Update Date 2009-05-05 21:00:50
Accession Number HMDB06454
Secondary Accession Numbers Not Available
Common Name L-2-Amino-3-oxobutanoic acid
Description L-2-Amino-3-oxobutanoic acid or L-2-amino acetic acid is involved in glycine/serine metabolism and is a breakdown product from glycine. It spontaneously decomposes to aminoacetone. Delta-aminolevuliinate synthase is the enzyme that catalyzes the interconversion between glycine and L-2-amino-3-oxobutanoic acid. Glycine C-acetyltransferase is also capable of catalyzing this reaction.
Synonyms
  1. (2S)-2-amino-3-oxobutanoate
  2. (S)-2-Amino-3-oxobutanoic acid
  3. L-2-Amino-3-oxobutanoic acid
  4. L-2-Amino-acetoacetate
  5. L-2-Amino-3-oxobutanoate
  6. L-2-amino acetic acid
  7. 2-amino-3-oxobutanoate
  8. 2-amino-3-oxobutanoic acid
  9. (2S)-2-amino-3-oxobutanoic acid
  10. (S)-2-Amino-3-oxobutanoate
Chemical IUPAC Name (2S)-2-amino-3-oxo-butanoate
Chemical Formula C4H7NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • ketone
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 117.103
Monoisotopic Molecular Weight 117.042595
Isomeric SMILES CC(=O)[C@H](N)C(O)=O
Canonical SMILES CC(=O)C(N)C(O)=O
KEGG Compound ID C03508 Link Image
BioCyc ID AMINO-OXOBUT Link Image
BiGG ID 41986 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB06454 Link Image
Metagene Link HMDB06454 Link Image
METLIN ID Not Available
PubChem Compound 5460100 Link Image
PubChem Substance 6318 Link Image
ChEBI ID 16944 Link Image
CAS Registry Number Not Available
InChI Identifier InChI=1/C4H7NO3/c1-2(6)3(5)4(7)8/h3H,5H2,1H3,(H,7,8)/t3-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 206.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.63 [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
  • mitochondria
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
Name SMPDB Link KEGG Link
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
General References Not Available
Metabolic Enzymes
  1. 5-aminolevulinate synthase, nonspecific, mitochondrial
  2. 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
  3. Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c
Enzyme 1 [top]
Enzyme 1 ID 5251
Enzyme 1 Name 5-aminolevulinate synthase, nonspecific, mitochondrial
Enzyme 1 Synonyms
  1. ALAS-H
  2. 5-aminolevulinic acid synthase 1
  3. Delta-ALA synthase 1
  4. Delta-aminolevulinate synthase 1
Enzyme 1 Gene Name ALAS1
Enzyme 1 Protein Sequence >5-aminolevulinate synthase, nonspecific, mitochondrial 
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE
TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS
SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE
RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI
TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL
HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND
VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG
ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM
LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN
TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE
LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
Enzyme 1 Number of Residues 640
Enzyme 1 Molecular Weight 70580.3
Enzyme 1 Theoretical pI 8.57
Enzyme 1 GO Classification
Function
  • 5-aminolevulinate synthase activity
  • N-acyltransferase activity
  • N-succinyltransferase activity
  • acyltransferase activity
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • porphyrin metabolic process
  • tetrapyrrole biosynthetic process
  • tetrapyrrole metabolic process
Component
  • cell part
  • cytoplasmic part
  • intracellular part
  • mitochondrial matrix
  • mitochondrial part
Enzyme 1 General Function Involved in 5-aminolevulinate synthase activity
Enzyme 1 Specific Function Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2)
Enzyme 1 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 1 Reactions
  • succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 [RN:R00830]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 28583 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P13196 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HEM1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1923 bp 
ATGGAGAGTGTTGTTCGCCGCTGCCCATTCTTATCCCGAGTCCCCCAGGCCTTTCTGCAG
AAAGCAGGCAAATCTCTGTTGTTCTATGCCCAAAACTGCCCCAAGATGATGGAAGTTGGG
GCCAAGCCAGCCCCTCGGGCATTGTCCACTGCAGCAGTACACTACCAACAGATCAAAGAA
ACCCCTCCGGCCAGTGAGAAAGACAAAACTGCTAAGGCCAAGGTCCAACAGACTCCTGAT
GGATCCCAGCAGAGTCCAGATGGCACACAGCTTCCGTCTGGACACCCCTTGCCTGCCACA
AGCCAGGGCACTGCAAGCAAATGCCCTTTCCTGGCAGCACAGATGAATCAGAGAGGCAGC
AGTGTCTTCTGCAAAGCCAGTCTTGAGCTTCAGGAGGATGTGCAGGAAATGAATGCCGTG
AGGAAAGAGGTTGCTGAAACCTCAGCAGGCCCCAGTGTGGTTAGTGTGAAAACCGATGGA
GGGGATCCCAGTGGACTGCTGAAGAACTTCCAGGACATTATGCAAAAGCAAAGACCAGAA
AGAGTGTCTCATCTTCTTCAAGATAACTTGCCAAAATCTGTTTCCACTTTTCAGTATGAT
CGTTTCTTTGAGAAAAAAATTGATGAGAAAAAGAATGACCACACCTATCGAGTTTTTAAA
ACTGTGAACCGGCGAGCACACATCTTCCCCATGGCAGATGACTATTCAGACTCCCTCATC
ACCAAAAAGCAAGTGTCAGTCTGGTGCAGTAATGACTACCTAGGAATGAGTCGCCACCCA
CGGGTGTGTGGGGCAGTTATGGACACTTTGAAACAACATGGTGCTGGGGCAGGTGGTACT
AGAAATATTTCTGGAACTAGTAAATTCCATGTGGACTTAGAGCGGGAGCTGGCAGACCTC
CATGGGAAAGATGCCGCACTCTTGTTTTCCTCGTGCTTTGTGGCCAATGACTCAACCCTC
TTCACCCTGGCTAAGATGATGCCAGGCTGTGAGATTTACTCTGATTCTGGGAACCATGCC
TCCATGATCCAAGGGATTCGAAACAGCCGAGTGCCAAAGTACATCTTCCGCCACAATGAT
GTCAGCCACCTCAGAGAACTGCTGCAAAGATCTGACCCCTCAGTCCCCAAGATTGTGGCA
TTTGAAACTGTCCATTCAATGGATGGGGCGGTGTGCCCACTGGAAGAGCTGTGTGATGTG
GCCCATGAGTTTGGAGCAATCACCTTCGTGGATGAGGTCCACGCAGTGGGGCTTTATGGG
GCTCGAGGCGGAGGGATTGGGGATCGGGATGGAGTCATGCCAAAAATGGACATCATTTCT
GGAACACTTGGCAAAGCCTTTGGTTGTGTTGGAGGGTACATCGCCAGCACGAGTTCTCTG
ATTGACACCGTACGGTCCTATGCTGCTGGCTTCATCTTCACCACCTCTCTGCCACCCATG
CTGCTGGCTGGAGCCCTGGAGTCTGTGCGGATCCTGAAGAGCGCTGAGGGACGGGTGCTT
CGCCGCCAGCACCAGCGCAACGTCAAACTCATGAGACAGATGCTAATGGATGCCGGCCTC
CCTGTTGTCCACTGCCCCAGCCACATCATCCCTGTGCGGGTTGCAGATGCTGCTAAAAAC
ACAGAAGTCTGTGATGAACTAATGAGCAGACATAACATCTACGTGCAAGCAATCAATTAC
CCTACGGTGCCCCGGGGAGAAGAGCTCCTACGGATTGCCCCCACCCCTCACCACACACCC
CAGATGATGAACTACTTCCTTGAGAATCTGCTAGTCACATGGAAGCAAGTGGGGCTGGAA
CTGAAGCCTCATTCCTCAGCTGAGTGCAACTTCTGCAGGAGGCCACTGCATTTTGAAGTG
ATGAGTGAAAGAGAGAAGTCCTATTTCTCAGGCTTGAGCAAGTTGGTATCTGCTCAGGCC
TGA
Enzyme 1 GenBank Gene ID X56351 Link Image
Enzyme 1 GeneCard ID ALAS1 Link Image
Enzyme 1 GenAtlas ID ALAS1 Link Image
Enzyme 1 HGNC ID HGNC:396 Link Image
Enzyme 1 Chromosome Location 3
Enzyme 1 Locus 3p21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Bishop DF: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. Nucleic Acids Res. 1990 Dec 11;18(23):7187-8. [PubMed Link Image]
  2. Bawden MJ, Borthwick IA, Healy HM, Morris CP, May BK, Elliott WH: Sequence of human 5-aminolevulinate synthase cDNA. Nucleic Acids Res. 1987 Oct 26;15(20):8563. [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
Enzyme 2 [top]
Enzyme 2 ID 5278
Enzyme 2 Name 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
Enzyme 2 Synonyms
  1. AKB ligase
  2. Aminoacetone synthase
  3. Glycine acetyltransferase
Enzyme 2 Gene Name GCAT
Enzyme 2 Protein Sequence >2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial 
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRV
DGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIA
RFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLD
MADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLG
PTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPP
AVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLAS
RMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
Enzyme 2 Number of Residues 419
Enzyme 2 Molecular Weight 45284.6
Enzyme 2 Theoretical pI 8.11
Enzyme 2 GO Classification
Function
  • C-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • binding
  • catalytic activity
  • cofactor binding
  • glycine C-acetyltransferase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • metabolic process
Component
—
Enzyme 2 General Function Involved in glycine C-acetyltransferase activity
Enzyme 2 Specific Function Acetyl-CoA + glycine = CoA + 2-amino-3- oxobutanoate
Enzyme 2 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 2 Reactions
  • acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate [RN:R00371]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID O75600 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name KBL_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1260 bp 
ATGTGGCCTGGGAACGCCTGGCGCGCCGCACTCTTCTGGGTGCCCCGCGGCCGCCGCGCA
CAGTCAGCGCTGGCCCAGCTGCGTGGCATTCTGGAGGGGGAGCTGGAAGGCATCCGCGGA
GCTGGCACTTGGAAGAGTGAGCGGGTCATCACGTCCCGTCAGGGGCCGCACATCCGCGTG
GACGGCGTCTCCGGAGGAATCCTCAACTTCTGTGCCAACAACTACCTGGGCCTGAGCAGC
CACCCTGAGGTGATTCAGGCAGGTCTGCAGGCTCTGGAGGAGTTTGGAGCTGGCCTTAGC
TCGGTCCGCTTCATCTGTGGAACCCAGAGCATCCACAAGAATCTAGAAGCAAAAATAGCC
CGCTTCCACCAGCGGGAGGATGCCATCCTCTATCCCAGCTGTTATGACGCCAACGCCGGC
CTCTTTGAGGCCCTGCTGACCCCAGAGGACGCAGTCCTGTCGGACGAGCTGAACCATGCC
TCCATCATCGACGGCATCCGGCTGTGCAAGGCCCACAAGTACCGCTATCGCCACCTGGAC
ATGGCCGACCTAGAAGCCAAGCTGCAGGAGGCCCAGAAGCATCGGCTGCGCCTGGTGGCC
ACCGATGGGGCCTTTTCCATGGATGGCGACATCGCACCCCTGCAGGAGATCTGCTGCCTC
GCCTCTAGATATGGTGCCCTGGTCTTCATGGATGAATGCCATGCCACTGGTTTCCTGGGG
CCCACAGGACGGGGCACAGATGAGCTGCTGGGTGTGATGGACCAGGTCACCATCATCAAC
TCCACCCTGGGGAAGGCCCTGGGTGGAGCATCAGGGGGCTACACGACAGGGCCTGGGCCC
CTGGTGTCACTGCTGCGGCAGCGCGCCCGGCCATACCTCTTCTCCAACAGTCTGCCACCT
GCTGTCGTTGGCTGCGCCTCCAAGGCCCTAGATCTGCTGATGGGGAGTAACACCATTGTC
CAGTCTATGGCTGCCAAGACCCAGAGGTTCCGTAGTAAGATGGAAGCTGCTGGCTTCACT
ATCTCAGGAGCCAGTCACCCCATCTGCCCTGTGATGCTGGGTGATGCCCGGCTGGCCTCT
CGCATGGCGGATGACATGCTGAAGAGAGGCATCTTTGTCATCGGGTTCAGCTACCCCGTG
GTCCCCAAGGGCAAGGCCCGGATCCGGGTACAGATCTCAGCAGTGCATAGCGAGGAAGAC
ATTGACCGCTGCGTGGAGGCCTTCGTGGAAGTGGGGCGACTGCACGGGGCACTGCCCTGA
Enzyme 2 GenBank Gene ID AF077740 Link Image
Enzyme 2 GeneCard ID GCAT Link Image
Enzyme 2 GenAtlas ID GCAT Link Image
Enzyme 2 HGNC ID HGNC:4188 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 22q13.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Edgar AJ, Polak JM: Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs. Eur J Biochem. 2000 Mar;267(6):1805-12. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 14717
Enzyme 3 Name Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c
Enzyme 3 Synonyms
  1. SubName: cDNA FLJ78080, highly similar to Human ALAS 5-aminolevulinate synthase
  2. SubName: cDNA, FLJ93603, highly similar to Homo sapiens aminolevulinate, delta-, synthase 2 (sideroblastic/hypochromic anemia) (ALAS2), nuclear gene encoding mitochondrial protein, mRNA
Enzyme 3 Gene Name ALAS2
Enzyme 3 Protein Sequence >Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c 
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG
DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ
EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH
FSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE
QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF
VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH
AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT
TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV
GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW
TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
Enzyme 3 Number of Residues 587
Enzyme 3 Molecular Weight 64632.9
Enzyme 3 Theoretical pI 8.19
Enzyme 3 GO Classification
Function
  • 5-aminolevulinate synthase activity
  • N-acyltransferase activity
  • N-succinyltransferase activity
  • acyltransferase activity
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • porphyrin metabolic process
  • tetrapyrrole biosynthetic process
  • tetrapyrrole metabolic process
Component
  • cell part
  • cytoplasmic part
  • intracellular part
  • mitochondrial matrix
  • mitochondrial part
Enzyme 3 General Function Involved in 5-aminolevulinate synthase activity
Enzyme 3 Specific Function Not Available
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 158254562 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A8K3F0 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A8K3F0_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1764 bp 
ATGGTGACTGCAGCCATGCTGCTACAGTGCTGCCCAGTGCTTGCCCGGGGCCCCACAAGC
CTCCTAGGCAAGGTGGTTAAGACTCACCAGTTCCTGTTTGGTATTGGACGCTGTCCCATC
CTGGCTACCCAAGGACCAAACTGTTCTCAAATCCACCTTAAGGCAACAAAGGCTGGAGGA
GATTCTCCATCTTGGGCGAAGGGCCACTGTCCCTTCATGCTGTCGGAACTCCAGGATGGG
AAGAGCAAGATTGTGCAGAAGGCAGCCCCAGAAGTCCAGGAAGATGTGAAGGCTTTCAAG
ACAGATCTGCCTAGCTCCCTGGTCTCAGTCAGCCTAAGGAAGCCATTTTCCGGTCCCCAG
GAGCAGGAGCAGATCTCTGGGAAGGTCACACACCTGATTCAGAACAATATGCCTGGAAAC
TATGTCTTCAGTTATGACCAGTTTTTCAGGGACAAGATCATGGAGAAGAAACAGGATCAC
ACCTACCGTGTGTTCAAGACTGTGAACCGCTGGGCTGATGCATATCCCTTTGCCCAACAT
TTCTCTGAGGCATCTGTGGCCTCAAAGGATGTGTCCGTCTGGTGTAGTAATGATTACCTG
GGCATGAGCCGACACCCTCAGGTCTTGCAAGCCACACAGGAGACCCTGCAGCGTCATGGT
GCTGGAGCTGGTGGCACCCGCAACATCTCAGGCACCAGTAAGTTTCATGTGGAGCTTGAG
CAGGAGCTGGCTGAGCTGCACCAGAAGGACTCAGCCCTGCTCTTCTCCTCCTGCTTTGTT
GCCAATGACTCTACTCTCTTCACCTTGGCCAAGATCCTGCCAGGGTGCGAGATTTACTCA
GACGCAGGCAACCATGCTTCCATGATCCAAGGTATCCGTAACAGTGGAGCAGCCAAGTTT
GTCTTCAGGCACAATGACCCTGACCACCTAAAGAAACTTCTAGAGAAGTCTAACCCTAAG
ATACCCAAAATTGTGGCCTTTGAGACTGTCCACTCCATGGATGGTGCCATCTGTCCCCTC
GAGGAGTTGTGTGATGTGTCCCACCAGTATGGGGCCCTGACCTTCGTGGATGAGGTCCAT
GCTGTAGGACTGTATGGGTCCCGGGGCGCTGGGATTGGGGAGCGTGATGGAATTATGCAT
AAGATTGACATCATCTCTGGAACTCTTGGCAAGGCCTTTGGCTGTGTGGGCGGCTACATT
GCCAGCACCCGTGACTTGGTGGACATGGTGCGCTCCTATGCTGCAGGCTTCATCTTTACC
ACTTCTCTGCCCCCCATGGTGCTCTCTGGAGCTCTAGAATCTGTGCGGCTGCTCAAGGGA
GAGGAGGGCCAAGCCCTGAGGCGAGCCCACCAGCGCAATGTCAAGCACATGCGCCAGCTA
CTCATGGACAGGGGCCTTCCTGTCATCCCCTGCCCCAGCCACATCATCCCCATCCGGGTG
GGCAATGCAGCACTCAACAGCAAGCTCTGTGATCTCCTGCTCTCCAAGCATGGCATCTAT
GTGCAGGCCATCAACTACCCAACTGTCCCCCGGGGTGAAGAGCTCCTGCGCTTGGCACCC
TCCCCCCACCACAGCCCTCAGATGATGGAAGATTTTGTGGAGAAGCTGCTGCTGGCTTGG
ACTGCGGTGGGGCTGCCCCTCCAGGATGTGTCTGTGGCTGCCTGCAATTTCTGTCGCCGT
CCTGTACACTTTGAGCTCATGAGTGAGTGGGAACGTTCCTACTTCGGGAACATGGGGCCC
CAGTATGTCACCACCTATGCCTGA
Enzyme 3 GenBank Gene ID AK290565 Link Image
Enzyme 3 GeneCard ID ALAS2 Link Image
Enzyme 3 GenAtlas ID ALAS2 Link Image
Enzyme 3 HGNC ID HGNC:397 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available