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
Functions
dioxygenase activity / metal ion binding
General Function
Not Available
Specific Function
dioxygenase activity
Pfam Domain Function
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
ResourceLink
UniProtKB IDQ45135
UniProtKB Entry NameQ45135_9MICO
GenBank Gene IDU58132
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
  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]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
2-(3,4-Dihydroxyphenyl)Acetic AcidexperimentalunknowntargetDetails