hypothetical protein Rv2728c [Mycobacterium tuberculosis H37Rv]
Protein Classification
class III extradiol ring-cleavage dioxygenase family protein( domain architecture ID 729)
class III extradiol ring-cleavage dioxygenase family protein may catalyze the incorporation of both atoms of molecular oxygen into substrates resulting in the cleavage of aromatic rings
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Extradiol_Dioxygenase_3B_like super family | cl00599 | Subunit B of Class III Extradiol ring-cleavage dioxygenases; Dioxygenases catalyze the ... |
7-229 | 1.19e-25 | |||||
Subunit B of Class III Extradiol ring-cleavage dioxygenases; Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups, whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Extradiol dioxygenases can be further divided into three classes. Class I and II enzymes are evolutionary related and show sequence similarity, with the two-domain class II enzymes evolving from the class I enzyme through gene duplication. Class III enzymes are different in sequence and structure and usually have two subunits, designated A and B. This model represents the catalytic subunit B of extradiol dioxygenase class III enzymes. Enzymes belonging to this family include Protocatechuate 4,5-dioxygenase (LigAB), 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarB), 4,5-DOPA Dioxygenase, 2,3-dihydroxyphenylpropionate 1,2-dioxygenase, and 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase (HPCD). There are also some family members that do not show the typical dioxygenase activity. The actual alignment was detected with superfamily member cd07951: Pssm-ID: 444999 [Multi-domain] Cd Length: 256 Bit Score: 100.43 E-value: 1.19e-25
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| Name | Accession | Description | Interval | E-value | |||||
| ED_3B_N_AMMECR1 | cd07951 | The N-terminal domain, an extradiol dioxygenase class III subunit B-like domain, of unknown ... |
7-229 | 1.19e-25 | |||||
The N-terminal domain, an extradiol dioxygenase class III subunit B-like domain, of unknown proteins containing a C-terminal AMMECR1 domain; This subfamily is composed of uncharacterized proteins containing an N-terminal domain with similarity to the catalytic B subunit of class III extradiol dioxygenases and a C-terminal AMMECR1-like domain. This model represents the N-terminal domain. Class III extradiol dioxygenases use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon, however, proteins in this subfamily do not contain a potential metal binding site and may not exhibit class III extradiol dioxygenase-like activity. The AMMECR1 protein was proposed to be a regulatory factor that is potentially involved in the development of AMME contiguous gene deletion syndrome. Pssm-ID: 153388 [Multi-domain] Cd Length: 256 Bit Score: 100.43 E-value: 1.19e-25
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| COG3885 | COG3885 | Aromatic ring-opening dioxygenase, LigB subunit [Secondary metabolites biosynthesis, transport ... |
127-224 | 4.27e-05 | |||||
Aromatic ring-opening dioxygenase, LigB subunit [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443093 [Multi-domain] Cd Length: 273 Bit Score: 43.27 E-value: 4.27e-05
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| Name | Accession | Description | Interval | E-value | |||||
| ED_3B_N_AMMECR1 | cd07951 | The N-terminal domain, an extradiol dioxygenase class III subunit B-like domain, of unknown ... |
7-229 | 1.19e-25 | |||||
The N-terminal domain, an extradiol dioxygenase class III subunit B-like domain, of unknown proteins containing a C-terminal AMMECR1 domain; This subfamily is composed of uncharacterized proteins containing an N-terminal domain with similarity to the catalytic B subunit of class III extradiol dioxygenases and a C-terminal AMMECR1-like domain. This model represents the N-terminal domain. Class III extradiol dioxygenases use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon, however, proteins in this subfamily do not contain a potential metal binding site and may not exhibit class III extradiol dioxygenase-like activity. The AMMECR1 protein was proposed to be a regulatory factor that is potentially involved in the development of AMME contiguous gene deletion syndrome. Pssm-ID: 153388 [Multi-domain] Cd Length: 256 Bit Score: 100.43 E-value: 1.19e-25
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| COG3885 | COG3885 | Aromatic ring-opening dioxygenase, LigB subunit [Secondary metabolites biosynthesis, transport ... |
127-224 | 4.27e-05 | |||||
Aromatic ring-opening dioxygenase, LigB subunit [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443093 [Multi-domain] Cd Length: 273 Bit Score: 43.27 E-value: 4.27e-05
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| ED_3B_like | cd07952 | Uncharacterized class III extradiol dioxygenases; This subfamily is composed of proteins of ... |
121-225 | 2.82e-03 | |||||
Uncharacterized class III extradiol dioxygenases; This subfamily is composed of proteins of unknown function with similarity to the catalytic B subunit of class III extradiol dioxygenases. Class III extradiol dioxygenases use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. They play key roles in the degradation of aromatic compounds. Pssm-ID: 153389 Cd Length: 256 Bit Score: 38.06 E-value: 2.82e-03
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