Reviewed,
UniProtKB/Swiss-Prot Q8KCJ0 (HEM2_CHLTE)
Last modified
January 19, 2010.
Version 44.
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 | Chlorobium tepidum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1097 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum |
Protein attributes
| Sequence length | 328 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 5-aminolevulinate = porphobilinogen + 2 H2O. |
| Enzyme regulation | Stimulated by magnesium, inhibited by zinc. |
| Pathway | |
| Subunit structure | Homooctamer By similarity. |
| Miscellaneous | Does not seem to have a metal requirement for activity. |
| Sequence similarities | Belongs to the ALADH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Heme biosynthesis Porphyrin biosynthesis |
| Ligand | Magnesium |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW porphobilinogen synthase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE006470 Genomic DNA. Translation: AAM72659.1. |
| RefSeq | NP_662317.1. |
3D structure databases | |
| SMR | Q8KCJ0. Positions 10-328. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1005979. |
| GenomeReviews | Gene locus CT1431 in contig AE006470_GR. |
| KEGG | cte:CT1431. |
| NMPDR | fig|194439.1.peg.1411. |
| TIGR | CT1431. |
Phylogenomic databases | |
| HOGENOM | HBG285270. |
| OMA | DPFTSHG. |
Enzyme and pathway databases | |
| BioCyc | CTEP194439:CT_1431-MONOMER. |
| BRENDA | 4.2.1.24. 189605. |
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. |
| PROSITE | PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HEM2_CHLTE | ||||||||
| Accession | Primary (citable) accession number: Q8KCJ0 | ||||||||
| 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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