NADP-dependent fatty aldehyde dehydrogenase
Details
- Name
- NADP-dependent fatty aldehyde dehydrogenase
- Synonyms
- 1.2.1.4
- Gene Name
- aldH
- Organism
- Vibrio harveyi
- Amino acid sequence
>lcl|BSEQ0012189|NADP-dependent fatty aldehyde dehydrogenase MNPQTDNVFYATNAFTGEALPLAFPVHTEVEVNQAATAAAKVARDFRRLNNSKRASLLRT IASELEARSDDIIARAHLETALPEVRLTGEIARTANQLRLFADVVNSGSYHQAILDTPNP TRAPLPKPDIRRQQIALGPVAVFGASNFPLAFSAAGGDTASALAAGCPVIVKGHTAHPGT SQIVAECIEQALKQEQLPQAIFTLLQGNQRALGQALVSHPEIKAVGFTGSVGGGRALFNL AHERPEPIPFYGELGAINPTFIFPSAMRAKADLADQFVASMTMGCGQFCTKPGVVFALNT PETQAFIETAQSLIRQQSPSTLLTPGIRDSYQSQVVSRGSDDGIDVTFSQAESPCVASAL FVTSSENWRKHPAWEEEIFGPQSLIVVCENVADMLSLSEMLAGSLTATIHATEEDYPQVS QLIPRLEEIAGRLVFNGWPTGVEVGYAMVHGGPYPASTHSASTSVGAEAIHRWLRPVAYQ ALPESLLPDSLKAENPLEIARAVDGKAAHS
- Number of residues
- 510
- Molecular Weight
- 54459.035
- Theoretical pI
- 5.43
- GO Classification
- Functionsaldehyde dehydrogenase (NADP+) activity
- General Function
- Aldehyde dehydrogenase (nadp+) activity
- Specific Function
- Catalyzes the oxidation of long-chain aliphatic aldehydes to acids. May be implicated in controlling luminescence as it catalyzes the oxidation of the fatty aldehyde substrate for the light-emitting reaction.
- Pfam Domain Function
- Aldedh (PF00171)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0006100|1533 bp ATGAACCCGCAAACCGACAACGTTTTTTACGCTACTAACGCCTTTACCGGTGAGGCGCTC CCTTTAGCTTTTCCTGTTCATACGGAAGTTGAGGTCAATCAAGCCGCAACTGCTGCTGCA AAAGTCGCACGCGATTTTCGCCGCTTAAATAACAGTAAGCGCGCTAGTCTGCTTCGCACG ATTGCCAGTGAATTAGAGGCAAGAAGTGATGACATTATCGCCCGAGCCCATTTAGAAACG GCGCTTCCCGAAGTACGCCTGACAGGAGAAATCGCTCGTACAGCGAATCAACTTCGCTTA TTCGCTGACGTAGTCAATTCTGGCAGTTATCACCAAGCCATTCTTGATACGCCAAACCCA ACTCGCGCCCCACTACCTAAGCCAGATATTCGTCGCCAACAAATTGCGCTGGGTCCTGTC GCGGTATTTGGAGCATCCAACTTTCCGTTGGCTTTCTCTGCTGCTGGTGGAGATACTGCT TCTGCCCTCGCAGCGGGTTGCCCGGTGATTGTAAAAGGTCATACTGCGCACCCAGGTACA AGCCAAATCGTTGCAGAGTGTATCGAGCAAGCGCTGAAACAAGAGCAACTACCACAAGCG ATTTTCACCTTGCTGCAAGGAAATCAGCGTGCTTTAGGACAAGCTCTAGTCAGCCATCCT GAAATAAAAGCGGTGGGCTTTACTGGATCGGTTGGTGGTGGACGCGCCCTGTTCAACCTA GCGCACGAGCGACCTGAGCCAATCCCGTTCTATGGTGAACTTGGTGCGATTAACCCGACG TTTATTTTCCCTTCTGCAATGAGAGCCAAAGCAGATTTAGCGGATCAATTTGTTGCCTCA ATGACCATGGGATGTGGGCAATTTTGTACAAAACCTGGCGTAGTGTTCGCGCTTAACACA CCGGAAACACAAGCGTTTATTGAAACCGCGCAATCCCTCATTCGCCAACAATCCCCTTCT ACTCTACTTACTCCCGGAATCCGTGATAGTTACCAATCACAGGTCGTCAGCCGAGGTTCT GACGACGGAATTGACGTCACTTTTTCTCAAGCGGAGTCCCCTTGTGTTGCCTCGGCTCTC TTTGTTACAAGCAGTGAAAATTGGCGCAAACATCCTGCGTGGGAAGAAGAGATTTTTGGT CCACAATCGTTGATCGTCGTTTGTGAAAATGTGGCTGATATGCTTTCGCTCAGTGAAATG CTAGCAGGATCGCTAACCGCGACAATTCATGCAACGGAAGAAGATTACCCACAAGTATCG CAGCTCATCCCTCGTTTGGAAGAGATTGCCGGACGACTGGTATTTAATGGTTGGCCGACA GGCGTAGAAGTTGGTTATGCCATGGTGCATGGCGGTCCATATCCCGCATCAACCCATTCG GCTTCGACTTCTGTTGGTGCCGAAGCCATTCATCGTTGGCTACGTCCGGTGGCTTATCAA GCGTTACCAGAAAGCTTACTGCCCGATTCGTTAAAAGCAGAAAATCCATTGGAGATCGCG CGCGCAGTAGATGGCAAAGCAGCTCACAGTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q56694 UniProtKB Entry Name ALDH_VIBHA GenBank Gene ID U39638 - General References
- Vedadi M, Szittner R, Smillie L, Meighen E: Involvement of cysteine 289 in the catalytic activity of an NADP(+)-specific fatty aldehyde dehydrogenase from Vibrio harveyi. Biochemistry. 1995 Dec 26;34(51):16725-32. [Article]
- Ahvazi B, Coulombe R, Delarge M, Vedadi M, Zhang L, Meighen E, Vrielink A: Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity. Biochem J. 2000 Aug 1;349 Pt 3:853-61. [Article]