A8A5M0 (BIOH_ECOHS) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 40.
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: Pimelyl-[acyl-carrier protein] methyl ester esterase EC=3.1.1.85 Alternative name(s): Biotin synthesis protein BioH Carboxylesterase BioH | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 331112 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 256 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters By similarity. HAMAP-Rule MF_01260 |
| Catalytic activity | Pimelyl-[acyl-carrier protein] methyl ester + H2O = pimelyl-[acyl-carrier protein] + methanol. HAMAP-Rule MF_01260 |
| Pathway | Cofactor biosynthesis; biotin biosynthesis. HAMAP-Rule MF_01260 |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the AB hydrolase superfamily. Carboxylesterase BioH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Biotin biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase Serine esterase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | biotin biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | carboxylesterase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 256 | 256 | Pimelyl-[acyl-carrier protein] methyl ester esterase HAMAP-Rule MF_01260 | PRO_1000067265 | |||||
Regions | |||||||||
| Region | 82 – 83 | 2 | Substrate binding By similarity | ||||||
| Region | 143 – 147 | 5 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 82 | 1 | Nucleophile By similarity | ||||||
| Active site | 207 | 1 | By similarity | ||||||
| Active site | 235 | 1 | By similarity | ||||||
| Binding site | 22 | 1 | Substrate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 235 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000802 Genomic DNA. Translation: ABV07824.1. |
| RefSeq | YP_001460207.1. NC_009800.1. |
3D structure databases | |
| ProteinModelPortal | A8A5M0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 331112.EcHS_A3609. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABV07824; ABV07824; EcHS_A3609. |
| GeneID | 5594704. |
| KEGG | ecx:EcHS_A3609. |
| PATRIC | 18317174. VBIEscCol77814_3515. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0596. |
| HOGENOM | HOG000028062. |
| KO | K02170. |
| OMA | LICELIS. |
| ProtClustDB | PRK10349. |
Enzyme and pathway databases | |
| BioCyc | ECOL331112:GHHI-3648-MONOMER. |
| UniPathway | UPA00078. |
Family and domain databases | |
| HAMAP | MF_01260. Carboxylester. |
| InterPro | IPR010076. BioH. [Graphical view] |
| TIGRFAMs | TIGR01738. bioH. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | BIOH_ECOHS | ||||||||
| Accession | Primary (citable) accession number: A8A5M0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
