 |
|
| HAMAP annotation rule: MF_00013 |
| Accession |
MF_00013 |
| Dates |
1-JUN-2001 (Created) 22-SEP-2011 (Last updated, Version 34) |
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; |
|
end case
case <OC:Archaea> or <OG:Chloroplast>
| 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
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 (By similarity).
CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein = protein N(6)-(octanoyl)lysine + [acyl-carrier-protein].
PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
case <OG:Chloroplast>
SUBCELLULAR LOCATION: Plastid, chloroplast.
end case
case not <OG:Chloroplast>
SUBCELLULAR LOCATION: Cytoplasm (Potential).
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 (By similarity).
SIMILARITY: Belongs to the LipB family.
case not <OG:Chloroplast>
end case
GO:0016746; Molecular function: transferase activity, transferring acyl groups.
case <OG:Chloroplast>
end case
case not <OG:Chloroplast>
end case
| From: LIPB_MYCTU (Q10404) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| ACT_SITE |
|
176 |
|
176 |
|
Acyl-thioester intermediate (By similarity) |
|
C |
|
|
| SITE |
|
142 |
|
142 |
|
Lowers pKa of active site Cys (By similarity) |
|
K |
|
|
| Size range: |
191-286 amino acids |
| Related UniRules: |
None |
| Template: |
P60720 (LIPB_ECOLI); Q10404 (LIPB_MYCTU): [Recover all] |
| Scope: |
Bacteria
Archaea
Plastid |
| Fusion: |
Nter: <Unknown>; Cter: <Nudix> |
| Duplicate: |
in PICTO |
| Plasmid encoded: |
None |
| Comments: |
Unknown N-terminal domains in DEIRA and PORGI. Nudix-like C-terminal domain in MYXXA. Possible wrong start in VIBCH and XYLFA. Shorter N-terminus in SALCH. |
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