Conserved Protein Domain Family
Gallate_dioxygenase_C

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cd07923: Gallate_dioxygenase_C 
The C-terminal domain of Gallate Dioxygenase, which catalyzes the oxidization and subsequent ring-opening of gallate
Gallate Dioxygenase catalyzes the oxidization and subsequent ring-opening of gallate, an intermediate in the degradation of the aromatic compound, syringate. The reaction product of gallate dioxygenase is 4-oxalomesaconate. The amino acid sequence of the N-terminal and C-terminal regions of gallate dioxygenase exhibits homology with the sequence of the PCA 4,5-dioxygenase B (catalytic) and A subunits, respectively. This model represents the C-terminal domain, which is similar to the A subunit of PCA 4,5-dioxygenase (or LigAB). The enzyme is estimated to be a homodimer according to the Escherichia coli enzyme. Since enzymes in this subfamily have fused A and B subunits, the dimer interface may resemble the tetramer interface of classical LigAB enzymes. This enzyme belongs to the class III extradiol dioxygenase family, composed of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.
Statistics
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PSSM-Id: 153393
View PSSM: cd07923
Aligned: 8 rows
Threshold Bit Score: 157.213
Threshold Setting Gi: 121608345
Created: 21-Apr-2009
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
putative N- andputative dimer
Feature 1:putative N- and C-terminal domain interface [polypeptide binding site]
Evidence:
  • Comment:based on similarity to other members of the family
  • Comment:The interface between the N- and C-terminal domains of this subfamily may be equivalent to the dimer interface of Sphingomonas paucimobilis LigAB.
  • Comment:The active site may be located at the interface between the N- and C-terminal domains for members of this subfamily. Most active site residues are from the N-terminal domain (similar to the B subunit of Sphingomonas paucimobilis LigAB).

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                 #  #  #    #                             #  #     ####  #    ##  #  ## 
Q5NTE5       314 RAVKGFRINHFLHRLIEPDFRKRFVEDPEGLFAESDLTEEEKSLIRNRDWIGMIHYGVIFFMLEKMAAVLGIGNIDVYAA 393 Sphingomonas pa...
Q1LGZ5       317 TSVRAYRINRYLHQLIDPAFRERFRADPLATYDEAALTPEERDMITRRDWRGMIHYGVIFFMLEKLGAVCGVSNLHIYAA 396 Ralstonia metal...
Q1R0S3       314 RSRKGYRINRFLHRLIEPDWRERFLADPEALFDEAALSEEERRLIRERDWRGMIHYGVIFFLLEKLGAVIGTSNLHIYAA 393 Chromohalobacte...
ZP_02884489   21 QSMKAMRLNRFFWQMREAAARTLWLANREAAYDAAGLTPEERTLVDNADWIGLIRYGVCFFVLEKFARVVKITNLGMYAS 100 Burkholderia gr...
Q8PP09        21 TSNRALRLNRFFWHMIRAPWRDRFLQDAEVLMQEADLTEQEKALIRARDWLGLVQYGANFFVIEKFARVVRMTNLQVYAI 100 Xanthomonas axo...
YP_001238264 314 RSQANFRINDFLHRLVIPAHRKRFIEEFDALADEYRLTQEERELIRNRRWIEMIRRGVSFFMLEKMAAVIGVSNPEVYAA 393 Bradyrhizobium ...
YP_996152      5 YVSHPGRSYVLLWNMIRAESRHEYIEDGEKAMTDAGLTDEEKDMIRRLDWIGLVRYGANFFVLEKYARVVKTPNLVVYAL 84  Verminephrobact...
ZP_05876302  315 NAHRAYRLNDFLHRLIEPAHRERFKQEPKALFTEFGLTEQEQTMVAEKQWIEMIRYGVSFFLLEKLGAVVGVPNPHIYAS 394 Vibrio furnissi...
Feature 1                      
Q5NTE5       394 FRGLSVPEFQKTRN 407 Sphingomonas paucimobilis
Q1LGZ5       397 MRGQSLEDFQKTRN 410 Ralstonia metallidurans CH34
Q1R0S3       394 MRGESLEEFQKTRN 407 Chromohalobacter salexigens DSM 3043
ZP_02884489  101 MRGETLEAFLKTRK 114 Burkholderia graminis C4D1M
Q8PP09       101 MRGESFEDFMQTRR 114 Xanthomonas axonopodis pv. citri
YP_001238264 394 FRGETLEAFLKTRK 407 Bradyrhizobium sp. BTAi1
YP_996152     85 MRGQTFEEFMQTRQ 98  Verminephrobacter eiseniae EF01-2
ZP_05876302  395 MRGEDIDTFQKSRN 408 Vibrio furnissii CIP 102972

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