Gamma-butyrobetaine dioxygenase
Details
- Name
- Gamma-butyrobetaine dioxygenase
- Synonyms
- 1.14.11.1
- BBH
- BBOX
- Gamma-BBH
- Gamma-butyrobetaine hydroxylase
- Gamma-butyrobetaine,2-oxoglutarate dioxygenase
- Gene Name
- BBOX1
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0011587|Gamma-butyrobetaine dioxygenase MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDV NIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSEL QLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHT WQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQK LKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISR HLEGAYADWDVVMSRLRILRQRVENGN
- Number of residues
- 387
- Molecular Weight
- 44714.6
- Theoretical pI
- 6.73
- GO Classification
- Functionsgamma-butyrobetaine dioxygenase activity / iron ion binding / zinc ion bindingProcessesbranched-chain amino acid catabolic process / carnitine biosynthetic process / cellular nitrogen compound metabolic process / small molecule metabolic processComponentscytosol / extracellular exosome / mitochondrion
- General Function
- Zinc ion binding
- Specific Function
- Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011588|Gamma-butyrobetaine dioxygenase (BBOX1) ATGGCTTGTACCATCCAAAAGGCAGAAGCACTTGACGGGGCTCATTTGATGCAGATCCTC TGGTATGATGAGGAAGAGTCTCTCTACCCAGCTGTATGGTTGAGAGACAACTGTCCGTGC TCTGATTGCTACCTGGATTCTGCAAAAGCACGGAAACTTCTAGTGGAAGCTCTTGATGTG AACATTGGAATTAAAGGCTTGATATTTGACAGAAAAAAGGTGTACATCACATGGCCCGAT GAGCATTACAGTGAATTCCAGGCTGATTGGCTGAAGAAAAGATGCTTTTCCAAGCAGGCC AGAGCAAAGCTCCAAAGAGAATTGTTTTTTCCAGAATGCCAATACTGGGGCTCAGAGCTC CAGCTACCCACTTTGGATTTTGAAGATGTTTTAAGATATGATGAACACGCATACAAGTGG CTCTCCACCCTCAAGAAAGTAGGCATAGTAAGACTCACCGGAGCATCTGACAAACCAGGA GAAGTTTCAAAACTTGGGAAAAGGATGGGTTTCCTCTATCTCACATTTTATGGACATACT TGGCAAGTGCAAGACAAAATCGATGCAAACAATGTGGCTTACACAACTGGGAAGCTAAGC TTTCACACTGATTATCCAGCCCTCCATCATCCACCTGGGGTTCAGCTTCTTCACTGCATA AAGCAAACAGTCACAGGGGGTGATTCAGAAATTGTAGATGGGTTTAATGTGTGCCAAAAA CTAAAGAAAAATAATCCTCAGGCATTCCAGATTTTGTCCTCTACCTTTGTGGACTTTACA GACATTGGAGTGGATTACTGTGATTTTTCTGTACAATCAAAACATAAAATTATAGAGTTA GATGATAAAGGCCAAGTGGTTCGCATCAACTTCAATAACGCAACTAGGGACACAATATTT GATGTGCCTGTTGAAAGAGTTCAGCCTTTTTATGCTGCTCTGAAGGAGTTTGTTGACCTC ATGAACAGCAAAGAATCCAAGTTTACCTTCAAGATGAATCCAGGTGATGTGATTACTTTT GATAACTGGCGCTTACTTCATGGCCGACGTAGCTATGAAGCAGGAACTGAGATATCCCGC CATCTAGAAGGAGCTTATGCTGACTGGGATGTGGTCATGTCAAGGCTTCGTATCTTAAGG CAGAGGGTGGAGAATGGAAACTGA
- Chromosome Location
- 11
- Locus
- 11p14.2
- External Identifiers
Resource Link UniProtKB ID O75936 UniProtKB Entry Name BODG_HUMAN GenBank Protein ID 3746805 GenBank Gene ID AF082868 GenAtlas ID BBOX1 HGNC ID HGNC:964 - General References
- Vaz FM, van Gool S, Ofman R, Ijlst L, Wanders RJ: Carnitine biosynthesis: identification of the cDNA encoding human gamma-butyrobetaine hydroxylase. Biochem Biophys Res Commun. 1998 Sep 18;250(2):506-10. [Article]
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- Tars K, Rumnieks J, Zeltins A, Kazaks A, Kotelovica S, Leonciks A, Sharipo J, Viksna A, Kuka J, Liepinsh E, Dambrova M: Crystal structure of human gamma-butyrobetaine hydroxylase. Biochem Biophys Res Commun. 2010 Aug 6;398(4):634-9. doi: 10.1016/j.bbrc.2010.06.121. Epub 2010 Jul 1. [Article]