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HAMAP rule MF_01838

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General rule information [?]

Accession MF_01838
Dates 11-MAR-2005 (Created)
17-FEB-2023 (Last updated, Version 27)
Name FabV_reductase
Scope
Bacteria
Templates Q62L02 (FABV_BURMA); Q9KRA3 (FABV1_VIBCH); Q97LU2 (FABV_CLOAB); Q73Q47 (FABV_TREDE); Q2P9J6 (FABV_XANOM); Q8Z9U1 (FABV_YERPE); Q9HZP8 (FABV_PSEAE): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
FABV
case <OC:Bacillota> or <OC:Spirochaetota>
Protein name
RecName: Full=Trans-2-enoyl-CoA reductase [NADH];
Short=TER;
EC 1.3.1.44;
else
Protein name
RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH];
Short=ENR;
EC 1.3.1.9;
end case
Gene name
fabV

Comments [?]

case <OC:Bacillota> or <OC:Spirochaetota>
Function Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to a coenzyme A (CoA).
Catalytic activity RHEA:18177: a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) + NADH
EC 1.3.1.44
else
Function Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).
Catalytic activity RHEA:10240: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH
EC 1.3.1.9
end case
Pathway Lipid metabolism; fatty acid biosynthesis.
Subunit Monomer.
Similarity Belongs to the TER reductase family.

Keywords [?]


Gene Ontology [?]

case <OC:Bacillota> or <OC:Spirochaetota>
GO:0050343; Molecular function: trans-2-enoyl-CoA reductase (NAD+) activity.
else
GO:0004318; Molecular function: enoyl-[acyl-carrier-protein] reductase (NADH) activity.
end case
GO:0051287; Molecular function: NAD binding.
GO:0006633; Biological process: fatty acid biosynthetic process.

Cross-references [?]

Pfam PF07055; Eno-Rase_FAD_bd; 1;

Features [?]

From: FABV_CLOAB (Q97LU2)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     47     52       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     G-x-S-[STN]-x-[YF]  
BINDING     74     75       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     [YLF]-E  
BINDING     111     112       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     D-[AGV]  
BINDING     139     140       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     [VLIA]-A  
BINDING     274     276       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     [LIV]-x-T  
ACT_SITE     235     235       Proton donor     Y  
BINDING     225     225       /ligand="substrate     Y  
BINDING     244     244       /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540     K  
SITE     75     75       Plays an important role in discriminating NADH against NADPH     E  

Additional information [?]

Size range 389-406 amino acids
Related rules None
Fusion None