Homoprotocatechuate 2,3-dioxygenase

Details

Name
Homoprotocatechuate 2,3-dioxygenase
Synonyms
Not Available
Gene Name
Not Available
Organism
Brevibacterium fuscum
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
Functions
dioxygenase activity / metal ion binding
General Function
Metal ion binding
Specific Function
Not Available
Pfam Domain Function
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
ResourceLink
UniProtKB IDQ45135
UniProtKB Entry NameQ45135_9MICO
GenBank Gene IDU58132
General References
  1. 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]
  2. Kovaleva EG, Lipscomb JD: Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science. 2007 Apr 20;316(5823):453-7. [Article]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB017022-(3,4-Dihydroxyphenyl)Acetic AcidexperimentalunknownDetails