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HAMAP rule MF_01815

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General rule information [?]

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 [?]

Identifier, protein and gene names [?]

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 [?]

FUNCTIONCatalyzes 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
PATHWAYLipid metabolism; fatty acid biosynthesis.
case <OC:Mycobacterium>
PATHWAYLipid metabolism; mycolic acid biosynthesis.
end case
SUBUNITHomodimer.
case <OG:Chloroplast>
SUBCELLULAR LOCATIONPlastid, chloroplast.
end case
case not <OG:Chloroplast>
SUBCELLULAR LOCATIONCytoplasm.
end case
DOMAINThe last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
SIMILARITYBelongs to the thiolase-like superfamily. FabH family.

Keywords [?]


Gene Ontology [?]

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 [?]

NCBIfam TIGR00747; FabH; 1;

Features [?]

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 [?]

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.



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