DB code: D00475
| CATH domain | 3.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1 | Catalytic domain |
|---|---|---|
| 3.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2 | Catalytic domain | |
| E.C. | 1.2.1.4 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2 | D00020 D00021 D00022 D00614 |
| 3.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1 | D00020 D00021 D00022 D00614 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
|---|---|---|---|
| Q56694 |
NADP-dependent fatty aldehyde dehydrogenase
|
EC
1.2.1.4
|
PF00171
(Aldedh)
[Graphical View] |
| KEGG enzyme name |
|---|
|
aldehyde dehydrogenase (NADP+)
NADP+-acetaldehyde dehydrogenase NADP+-dependent aldehyde dehydrogenase aldehyde dehydrogenase (NADP+) |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| Q56694 | ALDH_VIBHA | An aldehyde + NADP(+) + H(2)O = an acid + NADPH. | Homodimer. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00930 | Caprolactam degradation |
| Compound table | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||||
| KEGG-id | C00071 | C00006 | C00001 | C00174 | C00005 | C00080 | ||||||
| E.C. | ||||||||||||
| Compound | Aldehyde | NADP+ | H2O | Acid | NADPH | H+ | ||||||
| Type | carbohydrate | amide group,amine group,nucleotide | H2O | others | amide group,amine group,nucleotide | others | ||||||
| ChEBI |
18009 18009 |
15377 15377 |
16474 16474 |
15378 15378 |
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| PubChem |
5886 5886 |
22247451 962 22247451 962 |
5884 5884 |
1038 1038 |
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| 1cbzA01 |
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Unbound | Analogue:NAP | Unbound | Unbound | |||
| 1cbzB01 |
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Unbound | Analogue:NAP | Unbound | Unbound | |||
| 1cbzC01 |
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Unbound | Analogue:NAP | Unbound | Unbound | |||
| 1cbzD01 |
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Unbound | Analogue:NAP | Unbound | Unbound | |||
| 1co3A01 |
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Unbound | Bound:NAP | Unbound | Unbound | |||
| 1co3B01 |
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Unbound | Bound:NAP | Unbound | Unbound | |||
| 1co3C01 |
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Unbound | Bound:NAP | Unbound | Unbound | |||
| 1co3D01 |
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Unbound | Bound:NAP | Unbound | Unbound | |||
| 1eyyA01 |
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Unbound | Analogue:NAP | Unbound | Unbound | |||
| 1eyyB01 |
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Unbound | Analogue:NAP | Unbound | Unbound | |||
| 1eyyC01 |
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Unbound | Analogue:NAP | Unbound | Unbound | |||
| 1eyyD01 |
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Unbound | Analogue:NAP | Unbound | Unbound | |||
| 1ez0A01 |
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Unbound | Bound:NAP | Unbound | Unbound | |||
| 1ez0B01 |
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Unbound | Bound:NAP | Unbound | Unbound | |||
| 1ez0C01 |
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Unbound | Bound:NAP | Unbound | Unbound | |||
| 1ez0D01 |
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Unbound | Bound:NAP | Unbound | Unbound | |||
| 1cbzA02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1cbzB02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1cbzC02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1cbzD02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1co3A02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1co3B02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1co3C02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1co3D02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1eyyA02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1eyyB02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1eyyC02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1eyyD02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1ez0A02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1ez0B02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1ez0C02 |
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Unbound | Unbound | Unbound | Unbound | |||
| 1ez0D02 |
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Unbound | Unbound | Unbound | Unbound | |||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;Q56694 & literature [7] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1cbzA01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1cbzB01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1cbzC01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1cbzD01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1co3A01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1co3B01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1co3C01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1co3D01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1eyyA01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1eyyB01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1eyyC01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1eyyD01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1ez0A01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1ez0B01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1ez0C01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1ez0D01 |
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ASN 147;GLU 253;HIS 450 | ||||
| 1cbzA02 |
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CYS 289 | ||||
| 1cbzB02 |
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CYS 289 | ||||
| 1cbzC02 |
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CYS 289 | ||||
| 1cbzD02 |
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CYS 289 | ||||
| 1co3A02 |
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CYS 289 | ||||
| 1co3B02 |
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CYS 289 | ||||
| 1co3C02 |
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CYS 289 | ||||
| 1co3D02 |
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CYS 289 | ||||
| 1eyyA02 |
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CYS 289 | ||||
| 1eyyB02 |
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CYS 289 | ||||
| 1eyyC02 |
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CYS 289 | ||||
| 1eyyD02 |
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CYS 289 | ||||
| 1ez0A02 |
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CYS 289 | ||||
| 1ez0B02 |
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CYS 289 | ||||
| 1ez0C02 |
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CYS 289 | ||||
| 1ez0D02 |
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CYS 289 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[5]
|
p.859-860 | |
|
[6]
|
p.14411-14413, p.14414-14418 | |
|
[7]
|
p.34-36 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8527447 |
| Journal | Biochemistry |
| Year | 1995 |
| Volume | 34 |
| Pages | 16725-32 |
| Authors | Vedadi M, Szittner R, Smillie L, Meighen E |
| Title | Involvement of cysteine 289 in the catalytic activity of an NADP(+)-specific fatty aldehyde dehydrogenase from Vibrio harveyi. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8897616 |
| Journal | Protein Sci |
| Year | 1996 |
| Volume | 5 |
| Pages | 2130-2 |
| Authors | Croteau N, Vedadi M, Delarge M, Meighen E, Abu-Abed M, Howell PL, Vrielink A |
| Title | Crystallization and preliminary X-ray analysis of aldehyde dehydrogenase from Vibrio harveyi. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9059630 |
| Journal | Adv Exp Med Biol |
| Year | 1997 |
| Volume | 414 |
| Pages | 269-75 |
| Authors | Vedadi M, Croteau N, Delarge M, Vrielink A, Meighen E |
| Title | Structural and functional studies of a NADP(+)-specific aldehyde dehydrogenase from the luminescent marine bacterium Vibrio harveyi. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10471295 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 11440-7 |
| Authors | Zhang L, Ahvazi B, Szittner R, Vrielink A, Meighen E |
| Title | Change of nucleotide specificity and enhancement of catalytic efficiency in single point mutants of Vibrio harveyi aldehyde dehydrogenase. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) |
| Medline ID | 20363527 |
| PubMed ID | 10903148 |
| Journal | Biochem J |
| Year | 2000 |
| Volume | 349 Pt 3 |
| Pages | 853-61 |
| Authors | Ahvazi B, Coulombe R, Delarge M, Vedadi M, Zhang L, Meighen E, Vrielink A |
| Title | Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity. |
| Related PDB | 1ez0 1eyy 1co3 1cbz |
| Related UniProtKB | Q56694 |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11087393 |
| Journal | Biochemistry |
| Year | 2000 |
| Volume | 39 |
| Pages | 14409-18 |
| Authors | Zhang L, Ahvazi B, Szittner R, Vrielink A, Meighen E |
| Title | A histidine residue in the catalytic mechanism distinguishes Vibrio harveyi aldehyde dehydrogenase from other members of the aldehyde dehydrogenase superfamily. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11306028 |
| Journal | Chem Biol Interact |
| Year | 2001 |
| Volume | 130-132 |
| Pages | 29-38 |
| Authors | Zhang L, Ahvazi B, Szittner R, Vrielink A, Meighen E |
| Title | Differences in nucleotide specificity and catalytic mechanism between Vibrio harveyi aldehyde dehydrogenase and other members of the aldehyde dehydrogenase superfamily. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to aldehyde dehydrogenase superfamily.
|
| Created | Updated |
|---|---|
| 2005-01-19 | 2009-02-26 |