HAMAP rule MF_01260
General rule information
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| Accession | MF_01260 |
| Dates | 26-JUL-2005 (Created)
1-JUN-2023 (Last updated, Version 26) |
| Name | Carboxylester |
| Scope(s) |
Bacteria Pseudomonadota |
| Template(s) | P13001 (BIOH_ECOLI); Q9K197 (BIOH_NEIMB); Q8GHL1 (BIOH_SERMA); [ Recover all ] |
| Triggered by |
HAMAP; MF_01260 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | BIOH |
| Protein name | RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase; EC=3.1.1.85; AltName: Full=Biotin synthesis protein BioH; AltName: Full=Carboxylesterase BioH; |
| Gene name | Name=bioH; |
Comments
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| 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. |
| CATALYTIC ACTIVITY | Reaction=6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6- carboxyhexanoyl-[ACP] + H(+) + methanol; Xref=Rhea:RHEA:42700, Rhea:RHEA-COMP:9955, Rhea:RHEA-COMP:10186, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:78846, ChEBI:CHEBI:82735; EC=3.1.1.85; |
| PATHWAY | Cofactor biosynthesis; biotin biosynthesis. |
| SUBUNIT | Monomer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the AB hydrolase superfamily. Carboxylesterase BioH family. |
Keywords
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Gene Ontology
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| GO:0052689; Molecular function:carboxylic ester hydrolase activity |
| GO:0009102; Biological process:biotin biosynthetic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF00561; Abhydrolase_1; 1; |
| Pfam | PF00975; Thioesterase; 1; |
| PRINTS | PR00111; ABHYDROLASE; 1; |
| PRINTS | PR00412; EPOXHYDRLASE; 1; |
| NCBIfam | TIGR01738; BioH; 1; |
Features
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| From: BIOH_ECOLI (P13001) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 82 | 83 | /ligand="substrate" | S-[LM] | ||||||||
| BINDING | 143 | 147 | /ligand="substrate" | F-x-x-x-[QD] | ||||||||
| ACT_SITE | 82 | 82 | /note="Nucleophile" | S | ||||||||
| ACT_SITE | 207 | 207 | D | |||||||||
| ACT_SITE | 235 | 235 | H | |||||||||
| BINDING | 22 | 22 | /ligand="substrate" | W | ||||||||
| BINDING | 235 | 235 | /ligand="substrate" | H | ||||||||
Additional information
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| Size range | 239-312 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: MF_00835 (BioC) |
| Comments | Longer C-terminal in NEIMA; sequence not shown in alignment and not taken into account in size range |