Reviewed,
UniProtKB/Swiss-Prot Q9PLU4 (HEM2_CHLMU)
Last modified
November 3, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 | Chlamydia muridarum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83560 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia |
Protein attributes
| Sequence length | 333 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. |
| Pathway | |
| Subunit structure | Homooctamer By similarity. |
| Sequence similarities | Belongs to the ALADH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Porphyrin biosynthesis |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | porphyrin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | metal ion binding Inferred from electronic annotation. Source: InterPro porphobilinogen synthase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. Fraser C.M.Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg. |
Cross-references
Sequence databases | |
|---|---|
| AE002160 Genomic DNA. Translation: AAF38895.1. | |
| PIR | B81751. |
| RefSeq | NP_296385.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B4K based on UniProtKB Q59643. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1245524. |
| GenomeReviews | Gene locus TC_0001 in contig AE002160_GR. |
| KEGG | cmu:TC0001. |
| TIGR | TC_0001. |
Phylogenomic databases | |
| HOGENOM | Q9PLU4. |
| OMA | PELGVIT. |
Enzyme and pathway databases | |
| BioCyc | CMUR243161:TC_0001-MON. |
| BRENDA | 4.2.1.24. 256349. |
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_CHLMU | ||||||||
| Accession | Primary (citable) accession number: Q9PLU4 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with


