HAMAP rule MF_01815
General rule information
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Accession | MF_01815 |
Dates | 30-JUL-2003 (Created)
1-JUN-2023 (Last updated, Version 43) |
Name | FabH |
Scope(s) |
Bacteria Plastid |
Template(s) | P0A6R0 (FABH_ECOLI); O34746 (FABH1_BACSU); O07600 (FABH2_BACSU); P0A3C5 (FABH_STRPN); Q54206 (FABH_STRGA); Q4URQ0 (FABH_XANC8); C0LNR0 (FABH_LISM4); P9WNG3 (FABH_MYCTU); P68795 (FABH_STAAM); Q9F6D4 (FABH_STRLI); [ Recover all ] |
Triggered by |
HAMAP; MF_01815 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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case not <OC:Mycobacterium> | |
Identifier | FABH |
Protein name | RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase III; Short=Beta-ketoacyl-ACP synthase III; Short=KAS III; EC=2.3.1.180; AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3; AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III; |
Gene name | Name=fabH; |
else case <OC:Mycobacterium> | |
Identifier | FABH |
Protein name | RecName: Full=Mycobacterial beta-ketoacyl-[acyl-carrier-protein] synthase III; Short=Beta-ketoacyl-ACP synthase III; Short=KAS III; EC=2.3.1.301; AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3; AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III; |
Gene name | Name=fabH; |
end case |
Comments
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FUNCTION | Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. |
case not <OC:Mycobacterium> | |
CATALYTIC ACTIVITY | Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA- COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; |
else case <OC:Mycobacterium> | |
CATALYTIC ACTIVITY | Reaction=dodecanoyl-CoA + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl- [ACP] + CO2 + CoA; Xref=Rhea:RHEA:43640, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9645, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; EC=2.3.1.301; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43641; |
end case | |
PATHWAY | Lipid metabolism; fatty acid biosynthesis. |
case <OC:Mycobacterium> | |
PATHWAY | Lipid metabolism; mycolic acid biosynthesis. |
end case | |
SUBUNIT | Homodimer. |
case <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Plastid, chloroplast. |
end case | |
case not <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Cytoplasm. |
end case | |
DOMAIN | The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH. |
SIMILARITY | Belongs to the thiolase-like superfamily. FabH family. |
Keywords
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Acyltransferase | |
case not <OG:Chloroplast> | |
Cytoplasm | |
end case | |
Fatty acid biosynthesis | |
Fatty acid metabolism | |
Lipid biosynthesis | |
Lipid metabolism | |
Multifunctional enzyme | |
Transferase |
Gene Ontology
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GO:0033818; Molecular function:beta-ketoacyl-acyl-carrier-protein synthase III activity | |
GO:0006633; Biological process:fatty acid biosynthetic process | |
case <OG:Chloroplast> | |
GO:0009507; Cellular component:chloroplast | |
end case | |
case not <OG:Chloroplast> | |
GO:0005737; Cellular component:cytoplasm | |
end case |
Cross-references
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NCBIfam | TIGR00747; FabH; 1; |
Features
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From: FABH_ECOLI (P0A6R0) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 112 | 112 | C | |||||||||
ACT_SITE | 244 | 244 | H | |||||||||
ACT_SITE | 274 | 274 | N | |||||||||
REGION | 245 | 249 | /note="ACP-binding" | [QS]-[AP]-N-x-R |
Additional information
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Size range | 309-364 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |
Comments | In many organisms this enzyme can accept branched-chain acyl-CoAs (EC 2.3.1.300) in addition to acetyl-CoA. Mycobacterial enzyme acts on medium- and long-chain acyl-CoAs (EC 2.3.1.301) and has no activity with acetyl-CoA or branched-chain acyl-CoAs. |