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 5-Aminolevulinic acid (HMDB01149)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-12 12:03:07
Accession Number HMDB01149
Secondary Accession Numbers Not Available
Common Name 5-Aminolevulinic acid
Description An intermediate in heme synthesis. This is the first compound in the porphyrin synthesis pathway. It is produced by the enzyme ALA synthase, from glycine and succinyl CoA. This reaction is known as the Shemin pathway. Aminolevulinic acid plus blue light illumination using a blue light photodynamic therapy illuminator is indicated for the treatment of minimally to moderately thick actinic keratoses of the face or scalp.
Synonyms
  1. 5-amino-4-oxo-Pentanoate
  2. 5-amino-4-oxo-Pentanoic acid
  3. 5-Amino-4-oxopentanoate
  4. 5-Amino-4-oxopentanoic acid
  5. 5-Amino-4-oxovalerate
  6. 5-Amino-4-oxovaleric acid
  7. 5-amino-Levulinate
  8. 5-amino-Levulinic acid
  9. 5-aminolaevulinate
  10. 5-Aminolaevulinic acid
  11. 5-Aminolevulinate
  12. Aladerm
  13. Amino-levulinic acid
  14. Aminolevulinate
  15. Aminolevulinic acid
  16. delta-aminolevulinate
  17. delta-Aminolevulinic acid
  18. Kerastick
Chemical IUPAC Name 5-amino-4-oxo-pentanoic acid
Chemical Formula C5H9NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
  • Amino Ketones
  • Keto-Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • ketone
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
Biofunction
  • Component of Glycine, serine and threonine metabolism
  • Component of Porphyrin and chlorophyll metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 131.130
Monoisotopic Molecular Weight 131.058243
Isomeric SMILES NCC(=O)CCC(O)=O
Canonical SMILES NCC(=O)CCC(O)=O
KEGG Compound ID C00430 Link Image
BioCyc ID 5-AMINO-LEVULINATE Link Image
BiGG ID 34963 Link Image
Wikipedia Link 5-Aminolevulinic acid Link Image
NuGOwiki Link HMDB01149 Link Image
Metagene Link HMDB01149 Link Image
METLIN ID 6037 Link Image
PubChem Compound 137 Link Image
PubChem Substance 11367038 Link Image
ChEBI ID 17549 Link Image
CAS Registry Number 106-60-5
InChI Identifier InChI=1/C5H9NO3/c6-3-4(7)1-2-5(8)9/h1-3,6H2,(H,8,9)
Synthesis Reference Goli?ski J., D?browski Z., Obukowicz B., Kami?ski J., Be?dowicz M., Kwa?ny M.: "Synthesis of 5-aminolevulinic acid (5-ALA)", ICRI Annual Report '99, 2000, 119-122.
Melting Point (Experimental) 156-158 oC
Experimental Water Solubility 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)] Source: PhysProp
Predicted Water Solubility 173.0 mg/mL [Predicted by ALOGPS]; 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -4.40 [MEYLAN,WM & HOWARD,PH (1995)]; -1.5 [Predicted by PubChem via XLOGP]; -2.85 [Predicted by ALOGPS] 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 Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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 (Predicted from LogP)
  • mitochondria
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Bladder —
Fibroblasts —
Kidney —
Skin —
Spleen —
Stratum Corneum —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 0.26 +/- 0.16 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Lee C, Qiao X, Goeger DE, Anderson KE: Fluorometric measurement of 5-aminolevulinic acid in serum. Clin Chim Acta. 2004 Sep;347(1-2):183-8. [PubMed Link Image]
Biofluid Blood
Value 0.35 +/- 0.09 uM
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.28 +/- 0.57 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.45 +/- 0.72 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.97 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
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
Porphyrin Metabolism SMP00024 Link Image map00860 Link Image
General References
  1. Murata K, Sakai T, Morita Y, Iwata T, Dakeishi M: Critical dose of lead affecting delta-aminolevulinic acid levels. J Occup Health. 2003 Jul;45(4):209-14. [PubMed Link Image]
  2. Lu L, Lin G, Xu M, Zou H, Wang Q: [Re-assessment of indicators for screening lead poisoning] Zhonghua Yu Fang Yi Xue Za Zhi. 1999 Sep;33(5):275-8. [PubMed Link Image]
  3. Landry JL, Gelet A, Bouvier R, Dubernard JM, Martin X, Colombel M: Detection of bladder dysplasia using 5-aminolaevulinic acid-induced porphyrin fluorescence. BJU Int. 2003 May;91(7):623-6. [PubMed Link Image]
  4. Sassa S: Diagnosis and therapy of acute intermittent porphyria. Blood Rev. 1996 Mar;10(1):53-8. [PubMed Link Image]
  5. Tauber S, Stepp H, Meier R, Bone A, Hofstetter A, Stief C: Integral spectrophotometric analysis of 5-aminolaevulinic acid-induced fluorescence cytology of the urinary bladder. BJU Int. 2006 May;97(5):992-6. [PubMed Link Image]
  6. Bhardwaj RK, Herrera-Ruiz D, Sinko PJ, Gudmundsson OS, Knipp G: Delineation of human peptide transporter 1 (hPepT1)-mediated uptake and transport of substrates with varying transporter affinities utilizing stably transfected hPepT1/Madin-Darby canine kidney clones and Caco-2 cells. J Pharmacol Exp Ther. 2005 Sep;314(3):1093-100. Epub 2005 May 18. [PubMed Link Image]
  7. Tschudy DP, Valsamis M, Magnussen CR: Acute intermittent porphyria: clinical and selected research aspects. Ann Intern Med. 1975 Dec;83(6):851-64. [PubMed Link Image]
  8. Lipinski M, Jeromin L: Comparison of the bladder tumour antigen test with photodynamic diagnosis in patients with pathologically confirmed recurrent superficial urinary bladder tumours. BJU Int. 2002 May;89(7):757-9. [PubMed Link Image]
  9. Zareba G, Chmielnicka J: Disturbances in heme biosynthesis in rabbits after administration per os of low doses of tin or lead. Biol Trace Elem Res. 1992 Aug;34(2):115-22. [PubMed Link Image]
  10. Srivastava G, Borthwick IA, Maguire DJ, Elferink CJ, Bawden MJ, Mercer JF, May BK: Regulation of 5-aminolevulinate synthase mRNA in different rat tissues. J Biol Chem. 1988 Apr 15;263(11):5202-9. [PubMed Link Image]
  11. Maines MD, Mayer RD: Inhibition of testicular cytochrome P-450-dependent steroid biosynthesis by cis-platinum. Reversal by human chorionic gonadotropin. J Biol Chem. 1985 May 25;260(10):6063-8. [PubMed Link Image]
  12. Santos MA, Belo VG, Santos G: Effectiveness of photodynamic therapy with topical 5-aminolevulinic acid and intense pulsed light versus intense pulsed light alone in the treatment of acne vulgaris: comparative study. Dermatol Surg. 2005 Aug;31(8 Pt 1):910-5. [PubMed Link Image]
  13. Gederaas OA, Rasch MH, Berg K, Lagerberg JW, Dubbelman TM: Photodynamically induced effects in colon carcinoma cells (WiDr) by endogenous photosensitizers generated by incubation with 5-aminolaevulinic acid. J Photochem Photobiol B. 1999 Apr;49(2-3):162-70. [PubMed Link Image]
  14. Lee S, Kollias N, McAuliffe DJ, Flotte TJ, Doukas AG: Topical drug delivery in humans with a single photomechanical wave. Pharm Res. 1999 Nov;16(11):1717-21. [PubMed Link Image]
  15. van den Akker JT, Boot K, Vernon DI, Brown SB, Groenendijk L, van Rhoon GC, Sterenborg HJ: Effect of elevating the skin temperature during topical ALA application on in vitro ALA penetration through mouse skin and in vivo PpIX production in human skin. Photochem Photobiol Sci. 2004 Mar;3(3):263-7. Epub 2004 Feb 13. [PubMed Link Image]
  16. Lerda D: Study of sperm characteristics in persons occupationally exposed to lead. Am J Ind Med. 1992;22(4):567-71. [PubMed Link Image]
  17. Winkler A, Muller-Goymann CC: Comparative permeation studies for delta-aminolevulinic acid and its n-butylester through stratum corneum and artificial skin constructs. Eur J Pharm Biopharm. 2002 May;53(3):281-7. [PubMed Link Image]
  18. Hexyl aminolevulinate: 5-ALA hexylester, 5-ALA hexylesther, aminolevulinic acid hexyl ester, hexaminolevulinate, hexyl 5-aminolevulinate, P 1206. Drugs R D. 2005;6(4):235-8. [PubMed Link Image]
  19. Collaud S, Jichlinski P, Marti A, Aymon D, Gurny R, Lange N: An open pharmacokinetic study of hexylaminolevulinate-induced photodiagnosis after intravesical administration. Drugs R D. 2006;7(3):173-86. [PubMed Link Image]
  20. Fritsch C, Batz J, Bolsen K, Schulte KW, Zumdick M, Ruzicka T, Goerz G: Ex vivo application of delta-aminolevulinic acid induces high and specific porphyrin levels in human skin tumors: possible basis for selective photodynamic therapy. Photochem Photobiol. 1997 Jul;66(1):114-8. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. 5-aminolevulinate synthase, erythroid-specific, mitochondrial
  2. 5-aminolevulinate synthase, nonspecific, mitochondrial
  3. Delta-aminolevulinic acid dehydratase
  4. Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c
  5. cDNA FLJ78014, highly similar to Homo sapiens aminolevulinate, delta-, dehydratase (ALAD), transcript variant 1, mRNA
Enzyme 1 [top]
Enzyme 1 ID 5246
Enzyme 1 Name 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Enzyme 1 Synonyms
  1. ALAS-E
  2. 5-aminolevulinic acid synthase 2
  3. Delta-ALA synthase 2
  4. Delta-aminolevulinate synthase 2
Enzyme 1 Gene Name ALAS2
Enzyme 1 Protein Sequence >5-aminolevulinate synthase, erythroid-specific, mitochondrial 
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG
DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ
EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH
FSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE
QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF
VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH
AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT
TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV
GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW
TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
Enzyme 1 Number of Residues 587
Enzyme 1 Molecular Weight 64632.9
Enzyme 1 Theoretical pI 8.19
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 3220249 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P22557 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HEM0_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID AF068624 Link Image
Enzyme 1 GeneCard ID ALAS2 Link Image
Enzyme 1 GenAtlas ID ALAS2 Link Image
Enzyme 1 HGNC ID HGNC:397 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
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. Cox TC, Bawden MJ, Martin A, May BK: Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 1991 Jul;10(7):1891-902. [PubMed Link Image]
  3. Surinya KH, Cox TC, May BK: Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene. J Biol Chem. 1998 Jul 3;273(27):16798-809. [PubMed Link Image]
  4. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  5. Cox TC, Bottomley SS, Wiley JS, Bawden MJ, Matthews CS, May BK: X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase. N Engl J Med. 1994 Mar 10;330(10):675-9. [PubMed Link Image]
  6. Cotter PD, Baumann M, Bishop DF: Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency. Proc Natl Acad Sci U S A. 1992 May 1;89(9):4028-32. [PubMed Link Image]
  7. Furuyama K, Uno R, Urabe A, Hayashi N, Fujita H, Kondo M, Sassa S, Yamamoto M: R411C mutation of the ALAS2 gene encodes a pyridoxine-responsive enzyme with low activity. Br J Haematol. 1998 Dec;103(3):839-41. [PubMed Link Image]
  8. Harigae H, Furuyama K, Kudo K, Hayashi N, Yamamoto M, Sassa S, Sasaki T: A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia. Am J Hematol. 1999 Oct;62(2):112-4. [PubMed Link Image]
  9. Cotter PD, May A, Li L, Al-Sabah AI, Fitzsimons EJ, Cazzola M, Bishop DF: Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. Blood. 1999 Mar 1;93(5):1757-69. [PubMed Link Image]
  10. Cazzola M, May A, Bergamaschi G, Cerani P, Ferrillo S, Bishop DF: Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation. Blood. 2002 Dec 1;100(12):4236-8. Epub 2002 Aug 8. [PubMed Link Image]
  11. Hurford MT, Marshall-Taylor C, Vicki SL, Zhou JZ, Silverman LM, Rezuke WN, Altman A, Tsongalis GJ: A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia. Clin Chim Acta. 2002 Jul;321(1-2):49-53. [PubMed Link Image]
  12. Whatley SD, Ducamp S, Gouya L, Grandchamp B, Beaumont C, Badminton MN, Elder GH, Holme SA, Anstey AV, Parker M, Corrigall AV, Meissner PN, Hift RJ, Marsden JT, Ma Y, Mieli-Vergani G, Deybach JC, Puy H: C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload. Am J Hum Genet. 2008 Sep;83(3):408-14. Epub 2008 Sep 4. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5251
Enzyme 2 Name 5-aminolevulinate synthase, nonspecific, mitochondrial
Enzyme 2 Synonyms
  1. ALAS-H
  2. 5-aminolevulinic acid synthase 1
  3. Delta-ALA synthase 1
  4. Delta-aminolevulinate synthase 1
Enzyme 2 Gene Name ALAS1
Enzyme 2 Protein Sequence >5-aminolevulinate synthase, nonspecific, mitochondrial 
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE
TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS
SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE
RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI
TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL
HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND
VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG
ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM
LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN
TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE
LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
Enzyme 2 Number of Residues 640
Enzyme 2 Molecular Weight 70580.3
Enzyme 2 Theoretical pI 8.57
Enzyme 2 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 2 General Function Involved in 5-aminolevulinate synthase activity
Enzyme 2 Specific Function Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2)
Enzyme 2 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 2 Reactions
  • succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 [RN:R00830]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 28583 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P13196 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HEM1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID X56351 Link Image
Enzyme 2 GeneCard ID ALAS1 Link Image
Enzyme 2 GenAtlas ID ALAS1 Link Image
Enzyme 2 HGNC ID HGNC:396 Link Image
Enzyme 2 Chromosome Location 3
Enzyme 2 Locus 3p21.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13082
Enzyme 3 Name Delta-aminolevulinic acid dehydratase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name Not Available
Enzyme 3 Protein Sequence >Delta-aminolevulinic acid dehydratase 
MPPTSSTPSLSRPGLGQAGKPDTGSHPPPTISTSIFLSCFPTIPLSRPRTTGPSHSYQSI
SHPRSCRDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERG
SAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLA
EVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDA
AKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMLYLDIVREVKDKHPDL
PLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE
Enzyme 3 Number of Residues 359
Enzyme 3 Molecular Weight 39049.4
Enzyme 3 Theoretical pI 7.72
Enzyme 3 GO Classification
Function
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • cation binding
  • hydro-lyase activity
  • ion binding
  • lyase activity
  • metal ion binding
  • porphobilinogen synthase activity
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • tetrapyrrole biosynthetic process
Component
—
Enzyme 3 General Function Involved in porphobilinogen synthase activity
Enzyme 3 Specific Function 2 5-aminolevulinate = porphobilinogen + 2 H(2)O
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 2 5-aminolevulinate = porphobilinogen + 2 H2O [RN:R00036]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 47077495 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q6ZMU0 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q6ZMU0_HUMAN Link Image
Enzyme 3 PDB ID 1E51 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1080 bp 
ATGCCTCCAACCTCATCTACCCCATCTTTGTCACGCCCTGGGCTTGGCCAGGCAGGGAAG
CCAGACACTGGATCCCATCCTCCTCCCACCATCTCCACTTCCATATTTCTTTCCTGCTTC
CCAACCATCCCTCTCAGTCGCCCCCGCACCACTGGCCCTTCCCACAGCTACCAATCCATA
TCCCACCCCCGCTCTTGCAGGGATGTTCCTGATGACATACAGCCTATCACCAGCCTCCCA
GGAGTGGCCAGGTATGGTGTGAAGCGGCTGGAAGAGATGCTGAGGCCCTTGGTGGAAGAG
GGCCTACGCTGTGTCTTGATCTTTGGCGTCCCCAGCAGAGTTCCCAAGGACGAGCGGGGT
TCCGCAGCTGACTCCGAGGAGTCCCCAGCTATTGAGGCAATCCATCTGTTGAGGAAGACC
TTCCCCAACCTCCTGGTGGCCTGTGATGTCTGCCTGTGTCCCTACACCTCCCATGGTCAC
TGCGGGCTCCTGAGTGAAAACGGAGCATTCCGGGCTGAGGAGAGCCGCCAGCGGCTGGCT
GAGGTGGCATTGGCGTATGCCAAGGCAGGATGTCAGGTGGTAGCCCCGTCGGACATGATG
GATGGACGCGTGGAAGCCATCAAAGAGGCCCTGATGGCACATGGACTTGGCAACAGGGTA
TCGGTGATGAGCTACAGTGCCAAATTTGCTTCCTGTTTCTATGGCCCTTTCCGGGATGCA
GCTAAGTCAAGCCCAGCTTTTGGGGACCGCCGCTGCTACCAGCTGCCCCCTGGAGCACGA
GGCCTGGCTCTCCGAGCTGTGGACCGGGATGTACGGGAAGGAGCTGACATGCTCATGGTG
AAGCCGGGAATGCTCTACCTGGACATCGTGCGGGAGGTAAAGGATAAGCACCCTGACCTC
CCTCTCGCCGTGTACCACGTCTCTGGAGAGTTTGCCATGCTGTGGCATGGAGCCCAGGCC
GGGGCATTTGATCTCAAGGCTGCCGTACTGGAGGCCATGACTGCCTTCCGCAGAGCAGGT
GCTGACATCATCATCACCTACTACACACCGCAGCTGCTGCAGTGGCTGAAGGAGGAATGA
Enzyme 3 GenBank Gene ID AK131490 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs Not Available
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 14717
Enzyme 4 Name Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c
Enzyme 4 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 4 Gene Name ALAS2
Enzyme 4 Protein Sequence >Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c 
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG
DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ
EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH
FSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE
QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF
VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH
AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT
TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV
GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW
TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
Enzyme 4 Number of Residues 587
Enzyme 4 Molecular Weight 64632.9
Enzyme 4 Theoretical pI 8.19
Enzyme 4 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 4 General Function Involved in 5-aminolevulinate synthase activity
Enzyme 4 Specific Function Not Available
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 158254562 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A8K3F0 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8K3F0_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 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 4 GenBank Gene ID AK290565 Link Image
Enzyme 4 GeneCard ID ALAS2 Link Image
Enzyme 4 GenAtlas ID ALAS2 Link Image
Enzyme 4 HGNC ID HGNC:397 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 15248
Enzyme 5 Name cDNA FLJ78014, highly similar to Homo sapiens aminolevulinate, delta-, dehydratase (ALAD), transcript variant 1, mRNA
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name Not Available
Enzyme 5 Protein Sequence >cDNA FLJ78014, highly similar to Homo sapiens aminolevulinate, delta-, dehydratase (ALAD), transcript variant 1, mRNA 
MPPTSSTPSLSRPGLGQAGKPDTGSHPPPTISTSIFLSCFPTIPLSRPRTTGPSHSYQSI
SHPRSCRDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERG
SAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLA
EVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDA
AKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDL
PLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE
Enzyme 5 Number of Residues 359
Enzyme 5 Molecular Weight 39034
Enzyme 5 Theoretical pI 7.72
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Coenzyme transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 158254412 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A8K375 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A8K375_HUMAN Link Image
Enzyme 5 PDB ID 1E51 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1080 bp 
ATGCCTCCAACCTCATCTACCCCATCTTTGTCACGCCCTGGGCTTGGCCAGGCAGGGAAG
CCAGACACTGGATCCCATCCTCCTCCCACCATCTCCACTTCCATATTTCTTTCCTGCTTC
CCAACCATCCCTCTCAGTCGCCCCCGCACCACTGGCCCTTCCCACAGCTACCAATCCATA
TCCCACCCCCGCTCTTGCAGGGATGTTCCTGATGACATACAGCCTATCACCAGCCTCCCA
GGAGTGGCCAGGTATGGTGTGAAGCGGCTGGAAGAGATGCTGAGGCCCTTGGTGGAAGAG
GGCCTACGCTGTGTCTTGATCTTTGGCGTCCCCAGCAGAGTTCCCAAGGACGAGCGGGGT
TCCGCAGCTGACTCCGAGGAGTCCCCAGCTATTGAGGCAATCCATCTGTTGAGGAAGACC
TTCCCCAACCTCCTGGTGGCCTGTGATGTCTGCCTGTGTCCCTACACCTCCCATGGTCAC
TGCGGGCTCCTGAGTGAAAACGGAGCATTCCGGGCTGAGGAGAGCCGCCAGCGGCTGGCT
GAGGTGGCATTGGCGTATGCCAAGGCAGGATGTCAGGTGGTAGCCCCGTCGGACATGATG
GATGGACGCGTGGAAGCCATCAAAGAGGCCCTGATGGCACATGGACTTGGCAACAGGGTA
TCGGTGATGAGCTACAGTGCCAAATTTGCTTCCTGTTTCTATGGCCCTTTCCGGGATGCA
GCTAAGTCAAGCCCAGCTTTTGGGGACCGCCGCTGCTACCAGCTGCCCCCTGGAGCACGA
GGCCTGGCTCTCCGAGCTGTGGACCGGGATGTACGGGAAGGAGCTGACATGCTCATGGTG
AAGCCGGGAATGCCCTACCTGGACATCGTGCGGGAGGTAAAGGACAAGCACCCTGACCTC
CCTCTCGCCGTGTACCACGTCTCTGGAGAGTTTGCCATGCTGTGGCATGGAGCCCAGGCC
GGGGCATTTGATCTCAAGGCTGCCGTACTGGAGGCCATGACTGCCTTCCGCAGAGCAGGT
GCTGACATCATCATCACCTACTACACACCGCAGCTGCTGCAGTGGCTGAAGGAGGAATGA
Enzyme 5 GenBank Gene ID AK290490 Link Image
Enzyme 5 GeneCard ID A8K375 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs Not Available
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available