Halohydrin dehalogenase
Details
- Name
- Halohydrin dehalogenase
- Synonyms
- Not Available
- Gene Name
- hheC
- Organism
- Agrobacterium tumefaciens
- Amino acid sequence
>lcl|BSEQ0012321|Halohydrin dehalogenase MSTAIVTNVKHFGGMGSALRLSEAGHTVACHDESFKQKDELEAFAETYPQLKPMSEQEPA ELIEAVTSAYGQVDVLVSNDIFAPEFQPIDKYAVEDYRGAVEALQIRPFALVNAVASQMK KRKSGHIIFITSATPFGPWKELSTYTSARAGACTLANALSKELGEYNIPVFAIGPNYLHS EDSPYFYPTEPWKTNPEHVAHVKKVTALQRLGTQKELGELVAFLASGSCDYLTGQVFWLA GGFPMIERWPGMPE
- Number of residues
- 254
- Molecular Weight
- 27951.525
- Theoretical pI
- 5.14
- GO Classification
- Functionsoxidoreductase activity
- General Function
- Oxidoreductase activity
- Specific Function
- Not Available
- Pfam Domain Function
- adh_short (PF00106)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0006472|765 bp ATGTCAACCGCAATTGTAACAAACGTTAAGCATTTTGGGGGAATGGGGTCTGCACTTCGT CTCTCGGAAGCAGGACATACAGTGGCTTGCCACGATGAAAGCTTCAAACAAAAGGACGAA CTTGAAGCCTTTGCCGAAACCTATCCACAACTCAAACCAATGTCGGAACAAGAACCAGCG GAACTCATCGAGGCAGTTACCTCCGCTTATGGTCAAGTTGATGTACTTGTGAGCAACGAC ATATTCGCACCAGAGTTCCAACCCATAGATAAATACGCTGTAGAGGACTATCGCGGTGCG GTCGAGGCGCTACAAATTAGACCATTTGCACTGGTCAACGCCGTTGCAAGTCAAATGAAG AAGCGCAAAAGCGGACATATTATCTTTATTACCTCTGCAACGCCCTTCGGGCCTTGGAAG GAACTTTCTACCTACACGTCAGCCCGAGCAGGTGCATGCACCTTGGCAAATGCCCTTTCG AAGGAACTCGGTGAATACAACATTCCGGTGTTCGCAATAGGACCCAATTATCTTCACAGT GAAGATAGTCCCTACTTCTACCCCACAGAACCGTGGAAAACGAATCCAGAACACGTTGCC CATGTCAAAAAAGTCACTGCGCTCCAGCGGTTAGGTACACAGAAAGAATTGGGAGAACTC GTCGCGTTTCTCGCGTCTGGTAGTTGTGACTATCTGACCGGCCAGGTGTTCTGGTTGGCC GGCGGATTCCCAATGATCGAGCGTTGGCCTGGTATGCCCGAGTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q93D82 UniProtKB Entry Name Q93D82_RHIRD GenBank Gene ID AF397296 - General References
- van Hylckama Vlieg JE, Tang L, Lutje Spelberg JH, Smilda T, Poelarends GJ, Bosma T, van Merode AE, Fraaije MW, Janssen DB: Halohydrin dehalogenases are structurally and mechanistically related to short-chain dehydrogenases/reductases. J Bacteriol. 2001 Sep;183(17):5058-66. [Article]
- de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW: Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site. EMBO J. 2003 Oct 1;22(19):4933-44. [Article]
- de Jong RM, Tiesinga JJ, Villa A, Tang L, Janssen DB, Dijkstra BW: Structural basis for the enantioselectivity of an epoxide ring opening reaction catalyzed by halo alcohol dehalogenase HheC. J Am Chem Soc. 2005 Sep 28;127(38):13338-43. [Article]
- Schallmey M, Floor RJ, Hauer B, Breuer M, Jekel PA, Wijma HJ, Dijkstra BW, Janssen DB: Biocatalytic and structural properties of a highly engineered halohydrin dehalogenase. Chembiochem. 2013 May 10;14(7):870-81. doi: 10.1002/cbic.201300005. Epub 2013 Apr 12. [Article]
- Schallmey M, Jekel P, Tang L, Majeric Elenkov M, Hoffken HW, Hauer B, Janssen DB: A single point mutation enhances hydroxynitrile synthesis by halohydrin dehalogenase. Enzyme Microb Technol. 2015 Mar;70:50-7. doi: 10.1016/j.enzmictec.2014.12.009. Epub 2014 Dec 24. [Article]