Reviewed,
UniProtKB/Swiss-Prot Q6GG37 (HEM2_STAAR)
Last modified
June 16, 2009.
Version 33.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Delta-aminolevulinic acid dehydratase Short name=ALADH Short name=ALAD EC=4.2.1.24 Alternative name(s): Porphobilinogen synthase | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 282458 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 324 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 5-aminolevulinate = porphobilinogen + 2 H2O. |
| Cofactor | Zinc By similarity. |
| Pathway | |
| Subunit structure | Homooctamer By similarity. |
| Sequence similarities | Belongs to the ALADH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Porphyrin biosynthesis |
| Ligand | Zinc |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | porphyrin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | porphobilinogen synthase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| BX571856 Genomic DNA. Translation: CAG40739.1. | |
| RefSeq | YP_041135.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2860701. |
| GenomeReviews | Gene locus SAR1748 in contig BX571856_GR. |
| KEGG | sar:SAR1748. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q6GG37. |
| OMA | Q6GG37. AESTPQF. |
Enzyme and pathway databases | |
| BioCyc | SAUR282458:SAR1748-MON. |
Family and domain databases | |
| InterPro | IPR001731. 4pyrrol_synth_porphobiln_synth. IPR013785. Aldolase_TIM. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| PANTHER | PTHR11458. AlaD_dehydratase. 1 hit. |
| Pfam | PF00490. ALAD. 1 hit. [Graphical view] |
| PIRSF | PIRSF001415. Porphbilin_synth. 1 hit. |
| PRINTS | PR00144. DALDHYDRTASE. |
| ProDom | PD002304. AlaD_dehydratase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HEM2_STAAR | ||||||||
| Accession | Primary (citable) accession number: Q6GG37 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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