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HAMAP rule MF_00013
General rule information
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| Accession | MF_00013 |
| Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 45) |
| Name | LipB |
| Scope(s) |
Bacteria Archaea Plastid |
| Template(s) | P60720 (LIPB_ECOLI); P9WK83 (LIPB_MYCTU); [ Recover all ] |
| Triggered by |
HAMAP; MF_00013 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | LIPB |
| case <OC:Bacteria> | |
| Protein name | RecName: Full=Octanoyltransferase; EC=2.3.1.181; AltName: Full=Lipoate-protein ligase B; AltName: Full=Lipoyl/octanoyl transferase; AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase; |
| else | |
| Protein name | RecName: Full=Probable octanoyltransferase; EC=2.3.1.181; AltName: Full=Lipoate-protein ligase B; AltName: Full=Lipoyl/octanoyl transferase; AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase; |
| end case | |
| Gene name | Name=lipB; |
Comments
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| FUNCTION | Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. |
| CATALYTIC ACTIVITY | Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)- octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA- COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181; |
| PATHWAY | Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein]: step 1/2. |
| case <OC:Bacteria> or <OC:Archaea> | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| end case | |
| case <OG:Chloroplast> | |
| SUBCELLULAR LOCATION | Plastid, chloroplast. |
| end case | |
| MISCELLANEOUS | In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes. |
| SIMILARITY | Belongs to the LipB family. |
Keywords
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| case <OC:Bacteria> or <OC:Archaea> | |
| Cytoplasm | |
| end case | |
| Transferase | |
| Acyltransferase | |
Gene Ontology
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| GO:0016746; Molecular function:acyltransferase activity | |
| case <OG:Chloroplast> | |
| GO:0009507; Cellular component:chloroplast | |
| end case | |
| case <OCellular component:Bacteria> or <OC:Archaea> | |
| GO:0005737; Cellular component:cytoplasm | |
| end case | |
Cross-references
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| PROSITE | PS51733; BPL_LPL_CATALYTIC; 1; |
| PROSITE | PS01313; LIPB; 1; |
| Pfam | PF03099; BPL_LplA_LipB; 1; |
| NCBIfam | TIGR00214; LipB; 1; |
Features
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| From: LIPB_MYCTU (P9WK83) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 76 | 83 | /ligand="substrate" | R-G-G-x(2)-[TS]-x-H | ||||||||
| BINDING | 145 | 147 | /ligand="substrate" | [AS]-x-[GA] | ||||||||
| BINDING | 158 | 160 | /ligand="substrate" | G-x-[ASG] | ||||||||
| ACT_SITE | 176 | 176 | /note="Acyl-thioester intermediate" | C | ||||||||
| SITE | 142 | 142 | /note="Lowers pKa of active site Cys" | K | ||||||||
Additional information
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| Size range | 180-330 amino acids |
| Related rules |
None |
| Fusion | Nter: <Unknown> Cter: <Nudix> |
| Comments | Unknown N-terminal domains in Deinococcus radiodurans and Porphyromonas gingivalis. Nudix-like C-terminal domain in Myxococcus xanthus. |