B6IB27 (B6IB27_ECOSE) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 27.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Submitted name: Putative dethiobiotin synthase EMBL BAG77238.1 | ||
| Gene names |
| ||
| Organism | Escherichia coli (strain SE11) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 409438 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 231 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring By similarity. SAAS SAAS004472 |
| Catalytic activity | ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin. SAAS SAAS004472 |
| Cofactor | Magnesium By similarity. SAAS SAAS004472 |
| Pathway | Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2. SAAS SAAS004472 |
| Subcellular location | Cytoplasm By similarity SAAS SAAS004472. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Biotin biosynthesis SAAS SAAS004472 |
| Cellular component | Cytoplasm SAAS SAAS004472 |
| Ligand | ATP-binding SAAS SAAS004472 Magnesium SAAS SAAS004472 Metal-binding SAAS SAAS004472 Nucleotide-binding |
| Molecular function | Ligase SAAS SAAS004472 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | biotin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW dethiobiotin synthase activityInferred from electronic annotation. Source: InterPro magnesium ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult." Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M. DNA Res. 15:375-386(2008) [PubMed: 18931093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP009240 Genomic DNA. Translation: BAG77238.1. |
| RefSeq | YP_002292989.1. NC_011415.1. |
3D structure databases | |
| ProteinModelPortal | B6IB27. |
| SMR | B6IB27. Positions 2-220. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B6IB27. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000109198; EBESCP00000103617; EBESCG00000107818. |
| GeneID | 7000092. |
| GenomeReviews | Gene locus ECSE_1714 in contig AP009240_GR. |
| KEGG | ecy:ECSE_1714. |
| PATRIC | 18421928. VBIEscCol83070_1861. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000010427. |
| HOGENOM | HBG650065. |
| OMA | INPGLSH. |
| ProtClustDB | PRK12374. |
Family and domain databases | |
| HAMAP | MF_00336. BioD. [Tree] |
| InterPro | IPR002586. CbiA_P_synth. IPR004472. DTB_synth_BioD. [Graphical view] |
| KO | K01935. |
| Pfam | PF01656. CbiA. 1 hit. [Graphical view] |
| PIRSF | PIRSF006755. DTB_synth. 1 hit. |
| TIGRFAMs | TIGR00347. BioD. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | B6IB27_ECOSE | ||||||||
| Accession | Primary (citable) accession number: B6IB27 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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