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Annotation rule MF_00013 |
General rule information
[?]
Accession |
MF_00013 |
Dates |
1-JUN-2001 (Created) 20-NOV-2019 (Last updated, Version 41) |
Scope |
Bacteria
Archaea
Plastid |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Bacteria>
Protein name |
RecName:
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Full=Octanoyltransferase;
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EC 2.3.1.181;
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AltName:
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Full=Lipoate-protein ligase B;
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AltName:
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Full=Lipoyl/octanoyl transferase;
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AltName:
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Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
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else
Protein name |
RecName:
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Full=Probable octanoyltransferase;
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EC 2.3.1.181;
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AltName:
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Full=Lipoate-protein ligase B;
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AltName:
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Full=Lipoyl/octanoyl transferase;
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AltName:
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Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
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end case
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 |
RHEA:17665: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
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. |
case <OC:Bacteria> or <OC:Archaea>
end case
GO:0016746; Molecular function: transferase activity, transferring acyl groups.
case <OG:Chloroplast>
end case
case <OC:Bacteria> or <OC:Archaea>
end case
From: LIPB_MYCTU (P9WK83) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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REGION
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76
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83
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Substrate binding
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|
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R-G-G-x(2)-[TS]-x-H
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REGION
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145
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147
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Substrate binding
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[AS]-x-[GA]
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REGION
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158
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160
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Substrate binding
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G-x-[ASG]
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ACT_SITE
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176
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176
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Acyl-thioester intermediate
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C
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SITE
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142
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142
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Lowers pKa of active site Cys
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K
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Additional information
[?]
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. |