P78974 (HEM2_SCHPO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Delta-aminolevulinic acid dehydratase Short name=ALADH EC=4.2.1.24 Alternative name(s): Porphobilinogen synthase | ||||
| Gene names |
| ||||
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) | ||||
| Taxonomic identifier | 284812 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces |
Protein attributes
| Sequence length | 329 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen By similarity. |
| Catalytic activity | 2 5-aminolevulinate = porphobilinogen + 2 H2O. |
| Cofactor | Binds 1 zinc ion per monomer By similarity. |
| Pathway | |
| Subunit structure | Homooctamer By similarity. |
| Sequence similarities | Belongs to the ALADH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Heme biosynthesis Porphyrin biosynthesis |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | heme biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleusInferred from direct assay. Source: GeneDB_Spombe |
| Molecular function | lead ion binding Inferred from sequence or structural similarity. Source: UniProtKB porphobilinogen synthase activityInferred from sequence or structural similarity. Source: UniProtKB zinc ion bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 329 | 329 | Delta-aminolevulinic acid dehydratase | PRO_0000140533 | |||||
Sites | |||||||||
| Active site | 199 | 1 | Schiff-base intermediate with substrate By similarity | ||||||
| Active site | 252 | 1 | Schiff-base intermediate with substrate By similarity | ||||||
| Metal binding | 122 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 124 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 132 | 1 | Zinc; catalytic By similarity | ||||||
| Binding site | 209 | 1 | Substrate 1 By similarity | ||||||
| Binding site | 221 | 1 | Substrate 1 By similarity | ||||||
| Binding site | 279 | 1 | Substrate 2 By similarity | ||||||
| Binding site | 318 | 1 | Substrate 2 By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 60 | 1 | N → H in AAB41236. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. Nurse P.Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843. |
| [2] | Choi J.K., Levin H. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-329. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU329670 Genomic DNA. Translation: CAB55847.1. U83568 mRNA. Translation: AAB41236.1. |
| PIR | T37891. |
| RefSeq | NP_593917.1. NM_001019346.1. |
3D structure databases | |
| ProteinModelPortal | P78974. |
| SMR | P78974. Positions 4-328. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P78974. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | SPAC1805.06c.1; SPAC1805.06c.1:pep; SPAC1805.06c. |
| GeneID | 2542373. |
| GenomeReviews | Gene locus hem2 in contig CU329670_GR. |
| KEGG | spo:SPAC1805.06c. |
| NMPDR | fig|4896.1.peg.3887. |
Organism-specific databases | |
| GeneDB_Spombe | SPAC1805.06c. |
Phylogenomic databases | |
| eggNOG | fuNOG07497. |
| GeneTree | EFGT00050000001802. |
| HOGENOM | HBG285270. |
| OMA | XDERGSA. |
| OrthoDB | EOG454D75. |
Enzyme and pathway databases | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-001561-MONOMER. |
Gene expression databases | |
| ArrayExpress | P78974. |
Family and domain databases | |
| InterPro | IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| KO | K01698. |
| PANTHER | PTHR11458. AlaD_dehydratase. 1 hit. |
| Pfam | PF00490. ALAD. 1 hit. [Graphical view] |
| PIRSF | PIRSF001415. Porphbilin_synth. 1 hit. |
| PRINTS | PR00144. DALDHYDRTASE. |
| SMART | SM01004. ALAD. 1 hit. [Graphical view] |
| PROSITE | PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HEM2_SCHPO | ||||||||
| Accession | Primary (citable) accession number: P78974 Secondary accession number(s): Q9UTG9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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