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HAMAP annotation rule: MF_00013

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Accession MF_00013
Dates 1-JUN-2001 (Created)
25-NOV-2009 (Last updated, Version 29)
Data class Protein
Names LipB



Identifier LIPB

case <OC:Bacteria>
Protein name
RecName: Full=Octanoyltransferase;
EC=2.3.1.181;
AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
AltName: Full=Lipoyl/octanoyl transferase;
AltName: Full=Lipoate-protein ligase B;
end case


case <OC:Archaea> or <OG:Chloroplast>
Protein name
RecName: Full=Probable octanoyltransferase;
EC=2.3.1.181;
AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
AltName: Full=Lipoyl/octanoyl transferase;
AltName: Full=Lipoate-protein ligase B;
end case

Gene name lipB
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.
PROSITE PS01313; LIPB; 1;
Pfam PF03099; BPL_LipA_LipB; 1;
TIGRFAMs TIGR00214; lipB; 1;

case not <OG:Chloroplast>
end case

GO:0008415; Molecular function: acyltransferase activity.

case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case


case not <OG:Chloroplast>
GO:0005737; Cellular component: cytoplasm.
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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