Homoprotocatechuate 2,3-dioxygenase
Details
- Name
- Homoprotocatechuate 2,3-dioxygenase
- Kind
- protein
- Synonyms
- Not Available
- Gene Name
- Not Available
- UniProtKB Entry
- Q45135TrEMBL
- Organism
- Brevibacterium fuscum
- NCBI Taxonomy ID
- 47914
- Amino acid sequence
>lcl|BSEQ0022426|Homoprotocatechuate 2,3-dioxygenase MSNEIPKPVAPAPDILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFI HHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGCRTERRKDGFVKGIGDALRVED PLGFPYEFFFETTHVERLHMRYDLYSAGELVRLDHFNQVTPDVPRGRKYLEDLGFRVTED IQDDEGTTYAAWMHRKGTVHDTALTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDR IERGPGRHGVSNAFYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPV VPSWYTEASKVLDLDGNVQEIIERTDDSELEVTIGADGFSFTRAGDEDGSYHGQASKGFK LGNQL
- Number of residues
- 365
- Molecular Weight
- 41699.11
- Theoretical pI
- 5.08
- GO Classification
- Functionsdioxygenase activity / metal ion binding
- General Function
- Not Available
- Specific Function
- dioxygenase activity
- Pfam Domain Function
- Glyoxalase (PF00903)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0004930|1098 bp ATGAGCAACGAAATCCCCAAGCCAGTCGCACCAGCACCGGATATCCTGCGCTGCGCCTAC GCCGAACTGGTCGTCACCGACCTGGCCAAGTCCCGCAACTTCTACGTGGACGTCCTGGGC CTGCACGTATCCTACGAGGACGAGAACCAGATCTACCTGCGCTCCTTCGAGGAGTTCATC CACCACAACCTGGTCCTGACCAAGGGTCCGGTCGCCGCGCTGAAGGCCATGGCATTCCGC GTGCGCACCCCTGAGGACGTCGACAAGGCCGAGGCCTACTACCAGGAGCTGGGCTGCCGC ACCGAGCGCCGCAAGGACGGCTTCGTCAAGGGCATCGGCGACGCCCTGCGCGTGGAGGAT CCGCTGGGCTTCCCGTACGAGTTCTTCTTCGAGACCACCCACGTCGAACGCCTGCACATG CGCTACGACCTGTACTCGGCCGGCGAACTGGTCCGCCTGGACCACTTCAACCAGGTGACC CCGGACGTGCCGCGCGGCCGCAAGTACCTCGAGGACCTGGGCTTCCGCGTCACCGAGGAC ATCCAGGACGATGAGGGCACCACCTACGCAGCCTGGATGCACCGCAAGGGCACCGTGCAC GACACCGCCCTGACCGGCGGCAACGGCCCGCGCCTGCACCACGTGGCCTTCTCCACCCAT GAGAAGCACAACATCATCCAGATCTGCGACAAGATGGGCGCCCTGCGCATCTCGGACCGG ATCGAGCGCGGCCCGGGCCGCCACGGCGTCTCCAACGCGTTCTACCTGTACATCCTGGAT CCGGACAACCACCGCATCGAGATCTACACCCAGGACTACTACACCGGCGACCCGGACAAC CCGACCATCACCTGGAACGTCCACGACAACCAGCGCCGCGACTGGTGGGGCAACCCGGTT GTGCCTTCGTGGTACACCGAGGCCTCCAAGGTCCTGGACCTGGACGGCAACGTGCAGGAG ATCATCGAGCGCACCGACGACTCCGAACTGGAAGTCACCATCGGCGCCGACGGCTTCTCC TTCACCCGCGCGGGCGACGAGGACGGCTCGTACCACGGCCAGGCTTCGAAGGGCTTCAAG CTGGGCAACCAGCTCTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q45135 UniProtKB Entry Name Q45135_9MICO GenBank Gene ID U58132 PDB ID(s) 1F1X, 1Q0C, 1Q0O, 2IG9, 2IGA, 3BZA, 3ECJ, 3ECK, 3OJJ, 3OJK, 3OJN, 3OJT, 4GHC, 4GHD, 4GHE, 4GHF, 4GHG, 4GHH, 4Z6L, 4Z6M, 4Z6N, 4Z6O, 4Z6P, 4Z6Q, 4Z6R, 4Z6S, 4Z6T, 4Z6U, 4Z6V, 4Z6W, 4Z6Z, 5BWG, 5BWH - General References
- Vetting MW, Wackett LP, Que L Jr, Lipscomb JD, Ohlendorf DH: Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. J Bacteriol. 2004 Apr;186(7):1945-58. [Article]
- Kovaleva EG, Lipscomb JD: Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science. 2007 Apr 20;316(5823):453-7. [Article]
- Kovaleva EG, Lipscomb JD: Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase. Biochemistry. 2008 Oct 28;47(43):11168-70. doi: 10.1021/bi801459q. Epub 2008 Oct 1. [Article]
- Emerson JP, Kovaleva EG, Farquhar ER, Lipscomb JD, Que L Jr: Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state. Proc Natl Acad Sci U S A. 2008 May 27;105(21):7347-52. doi: 10.1073/pnas.0711179105. Epub 2008 May 20. [Article]
- Fielding AJ, Kovaleva EG, Farquhar ER, Lipscomb JD, Que L Jr: A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase. J Biol Inorg Chem. 2011 Feb;16(2):341-55. doi: 10.1007/s00775-010-0732-0. Epub 2010 Dec 14. [Article]
- Kovaleva EG, Lipscomb JD: Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation. Biochemistry. 2012 Nov 6;51(44):8755-63. doi: 10.1021/bi301115c. Epub 2012 Oct 29. [Article]
- Kovaleva EG, Rogers MS, Lipscomb JD: Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200. Biochemistry. 2015 Sep 1;54(34):5329-39. doi: 10.1021/acs.biochem.5b00709. Epub 2015 Aug 19. [Article]
- Meier KK, Rogers MS, Kovaleva EG, Mbughuni MM, Bominaar EL, Lipscomb JD, Munck E: A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mossbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods. Inorg Chem. 2015 Nov 2;54(21):10269-80. doi: 10.1021/acs.inorgchem.5b01576. Epub 2015 Oct 20. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 2-(3,4-Dihydroxyphenyl)Acetic Acid experimental unknown target Details