HAMAP rule MF_01032
General rule information
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Accession | MF_01032 |
Dates | 10-SEP-2002 (Created)
1-JUN-2023 (Last updated, Version 32) |
Name | LeuD_type2 |
Scope(s) |
Bacteria Archaea |
Template(s) | P04787 (LEUD1_SALTY); Q58667 (HACB_METJA); [ Recover all ] |
Triggered by |
HAMAP; MF_01032 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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case <FTTag:HACNmotif> | |
Identifier | HACB |
Protein name | RecName: Full=Methanogen homoaconitase small subunit; Short=HACN; EC=4.2.1.114; AltName: Full=Homoaconitate hydratase; |
Gene name | Name=hacB; |
else | |
Identifier | LEUD |
Protein name | RecName: Full=3-isopropylmalate dehydratase small subunit; EC=4.2.1.33; AltName: Full=Alpha-IPM isomerase; Short=IPMI; AltName: Full=Isopropylmalate isomerase; |
Gene name | Name=leuD; |
end case |
Comments
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case <FTTag:HACNmotif> | |
FUNCTION | Hydro-lyase with broad substrate specificity for cis- unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4- tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4- tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1- hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)- aconitate. All these reactions are part of the biosynthesis pathway of coenzyme B. |
CATALYTIC ACTIVITY | Reaction=(2R)-homocitrate = (2R,3S)-homoisocitrate; Xref=Rhea:RHEA:32303, ChEBI:CHEBI:15404, ChEBI:CHEBI:58884; EC=4.2.1.114; |
PATHWAY | Organic acid metabolism; 2-oxosuberate biosynthesis. |
SUBUNIT | Heterotetramer of 2 HacA and 2 HacB proteins. |
else | |
FUNCTION | Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. |
CATALYTIC ACTIVITY | Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate; Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121; EC=4.2.1.33; |
PATHWAY | Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. |
SUBUNIT | Heterodimer of LeuC and LeuD. |
end case | |
SIMILARITY | Belongs to the LeuD family. LeuD type 2 subfamily. |
Keywords
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case not <FTTag:HACNmotif> | |
Amino-acid biosynthesis | |
Branched-chain amino acid biosynthesis | |
Leucine biosynthesis | |
end case | |
Lyase |
Gene Ontology
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case <FTTag:HACNmotif> | |
GO:0004409; Molecular function:homoaconitate hydratase activity | |
GO:0019298; Biological process:coenzyme B biosynthetic process | |
else; https://www.ebi.ac.uk/QuickGO/term/else | |
GO:0003861; Molecular function:3-isopropylmalate dehydratase activity | |
GO:0009098; Biological process:leucine biosynthetic process | |
end case |
Cross-references
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Features
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From: HACB_METJA (Q58667) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri> | ||||||||||||
MOTIF | 24 | 27 | /note="YLRT" | HACNmotif | Y-L-R-T | |||||||
SITE | 26 | 26 | /note="Critical for substrate specificity" | R | ||||||||
end case |
Additional information
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Size range | 161-208 amino acids |
Related rules |
MF_01031 |
Fusion | Nter: None Cter: None |
Comments | The family member in THET2 is shown to function as a homoaconitase (for lysine biosynthesis), as well as one of the 2 copies found in METJA that catalyzes both the dehydration of (R)-homocitrate and the hydration of cis-homoaconitate for coenzyme B biosynthesis. The other copy in METJA functions both in leucine and isoleucine biosynthesis, since it catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate and between 2-methylmalate and 3-methylmalate. In Archaea, a motif that indicates the protein specificity has been determined (see PubMed=20170198): the presence of the YLRT motif likely indicates HACN activity, while proteins with the YLV(Y/I/M) sequence are IPMIs enzymes. |