| General Information |
| MoonProt ID | 126 |
| First appeared in release | 1.0 |
| Name(s) | Delta-aminolevulinic acid dehydratase
Porphobilinogen synthase
ALADH
Gene Name: ALAD |
| UniProt ID | P13716 (HEM2_HUMAN) Reviewed |
| GO terms | GO: 0006778 porphyrin-containing compound metabolic process GO: 0006779 porphyrin-containing compound biosynthetic process
GO: 0006782 protoporphyrinogen IX biosynthetic process
GO: 0006783 heme biosynthetic process
GO: 0008152 metabolic process
GO: 0033014 tetrapyrrole biosynthetic process
GO: 0044281 small molecule metabolic process
GO: 0051260 protein homooligomerization
GO:0071353 cellular response to interleukin-4
GO: 0003824 catalytic activity
GO: 0004655 prophobilinogen synthase activity
GO: 0008270 zinc ion binding
GO: 0016829 lyase activity
GO: 0032791 lead ion binding
GO: 0042802 identical protein binding
GO: 0046872 metal ion binding
GO: 0005829 cytosol |
| Organisms for which functions have been demonstrated | Homo sapiens (human, a mammal) |
| Sequence length | 330 |
| FASTA sequence | >sp|P13716|HEM2_HUMAN Delta-aminolevulinic acid dehydratase OS=Homo sapiens GN=ALAD PE=1 SV=1
MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE
|
| Structure Information |
| PDB ID | 1E51 1PV8 |
| Quaternary structure | |
| SCOP | TIM beta/alpha-barrel |
| CATH | 3.20.20.70 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-13, 329-330 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | 5-aminolaevulinate dehydratase, enzyme
converts 2 (5-aminolevulinate) to porphobilinogen +2H20.
Porphyrin-containing compound metabolism, protoporphyrin-IX biosynthesis |
| References for function | Gibbs, P.N.B., and Jordan, M. Identification of lysine at the active site of human 5-aminolaevulinate dehydratase. (1986) Biochem J. 236, 447-451. Wetmur, J.G., Bishop, D.F., Cantelmo, C., and Desnick, R.J. Human sigma-aminolevulinate dehydratase: Nucleotide sequence of a full-length cDNA clone. (1986) Proc Natl Acad Sci. 83, 7703-7707.
PMID: 3092810. |
| E.C. number | 4.2.1.24 |
| Location of functional site(s) | |
| Cellular location of function | Cytosol |
| Comments | |
| Function 2 |
| Function description | proteasome inhibitor
Noncompetitively blocks proteolysis of certain protein substrates. |
| References for function | Li, X., Gu, M., and Etlinger, J.D. Isoaltion and characterization of a Novel Endogenous Inhibitor of the Proteasome. (1991) Biohcem. 30, 9709-9715.
PMID: 1911759.
Guo, G.G., Gu, M., and Etlinger, J.D. 204-kDa Proteasome Inhibitor (CF-2) is Identical to Aminolevulinic Acid Dehydratase. (1994), J Biol Chem. 269, 12399-12402.
PMID: 8175643. |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | cytosol |
| Comments | |