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*Now available with Java™ 1.5!*
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| Family: |
PORPHOBILINOGEN SYNTHASE (PTHR11458)
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| Subfamilies: |
1
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| PANTHER Links: |
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| Abstract: |
Delta-aminolevulinic acid dehydratase (EC: 4.2.1.24) (ALAD) [PMID:2656410] catalyzes the second step in the biosynthesis of heme, the condensation of two molecules of 5-aminolevulinate to form porphobilinogen. The enzyme is an oligomer composed of eight identical subunits. Each of the subunits binds an atom of zinc or of magnesium (in plants). A lysine has been implicated in the catalytic mechanism [PMID:3092810]. The sequence of the region in the vicinity of the active site residue is conserved in ALAD from various prokaryotic and eukaryotic species. Inactivating mutations in the human enzyme are responsible for an inherited porphyria, and enzyme inactivation has also been implicated in acute lead poisoning. The enzyme has also been reported to be a regulatory component within the 26S proteasome.
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| InterPro Accession: |
IPR001731
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| PANTHER Molecular Function: |
Lyase
 Dehydratase
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| PANTHER Biological Process: |
Coenzyme and prosthetic group metabolism
Porphyrin metabolism
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| Pathway Categories: |
Heme biosynthesis
porphobilinogen synthase
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| Training Sequences: |
30
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| HMM Length |
325
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| Downloads: |
HMM (HMMER format) |
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Total |
Celera |
FlyBase |
NCBI |
| H. sapiens |
2
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1
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0 |
1
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| M. musculus |
2
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1
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0 |
1
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| R. norvegicus |
2
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1
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0 |
1
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| D. melanogaster |
1
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0 |
1
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0 |
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