HAMAP rule MF_02129
General rule information
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| Accession | MF_02129 |
| Dates | 4-MAY-2012 (Created)
19-NOV-2022 (Last updated, Version 10) |
| Name | L_carnitine_dehydrog |
| Scope(s) |
Bacteria |
| Template(s) | D7URM0 (LCDH_PSESP); D7UNT2 (LCDH_RHISP); Q9HTH8 (LCDH_PSEAE); [ Recover all ] |
| Triggered by |
HAMAP; MF_02129 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | LCDH |
| Protein name | RecName: Full=L-carnitine dehydrogenase; Short=L-CDH; Short=CDH; EC=1.1.1.108; |
| Gene name | Name=lcdH; |
Comments
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| FUNCTION | Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3- dehydrocarnitine. |
| CATALYTIC ACTIVITY | Reaction=carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH; Xref=Rhea:RHEA:19265, ChEBI:CHEBI:15378, ChEBI:CHEBI:17126, ChEBI:CHEBI:57540, ChEBI:CHEBI:57885, ChEBI:CHEBI:57945; EC=1.1.1.108; |
| PATHWAY | Amine and polyamine metabolism; carnitine metabolism. |
| SUBUNIT | Homodimer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. L- carnitine dehydrogenase subfamily. |
Keywords
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Gene Ontology
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| GO:0047728; Molecular function:carnitine 3-dehydrogenase activity |
| GO:0051287; Molecular function:NAD binding |
| GO:0042413; Biological process:carnitine catabolic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF00725; 3HCDH; 1; |
| Pfam | PF02737; 3HCDH_N; 1; |
| PIRSF | PIRSF000105; HCDH; 1; |
Features
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| From: LCDH_PSESP (D7URM0) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 14 | 19 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-x-G-x-x-G | ||||||||
Additional information
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| Size range | 307-364 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: <Unknown> |
| Comments | See Uanschou et al. Monatshefte f?r Chemie 136, 1365?1381 (2005), (http://www.springerlink.com/content/kn5531797l238128/fulltext.pdf) for a comparative genomic sequence analysis of L-carnitine dehydrogenase. RHILO possesses a longer C-terminus very rich in lysine residues. |