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Conserved domains on  [gi|2535555261|ref|WP_292363362|]
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class III extradiol ring-cleavage dioxygenase, partial [Methylophaga sp. UBA1464]

Protein Classification

DODA-type extradiol aromatic ring-opening family dioxygenase( domain architecture ID 10164192)

DODA-type extradiol aromatic ring-opening family dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into substrates resulting in the cleavage of aromatic rings, similar to 4,5-DOPA extradiol dioxygenase, which opens the cyclic ring of 4,5-dihydroxy-phenylalanine (DOPA) to form betalamic acid

CATH:  3.40.830.10
EC:  1.13.11.-
Gene Ontology:  GO:0051213|GO:0046872|GO:0016701|GO:0008270
PubMed:  16849108|15264822
SCOP:  3000690

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
45_DOPA_Dioxygenase cd07363
The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both ...
 1-93 1.48e-33

The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine; This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


:

Pssm-ID: 153375  Cd Length: 253  Bit Score: 116.86  E-value: 1.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555261   1 GQALQTLGDQSLLLIGSGFSFHNMRAFFTPETDEAKTMNESFEDWLLETccdenLTETEREQRLINWQSAPYARYCHPRE 80
Cdd:cd07363   142 GRALAPLRDEGVLIIGSGSSVHNLRALRWGGPAPPPPWALEFDDWLKDA-----LTAGDLDALLDYWEKAPHARRAHPTE 216

                          90
                  ....*....|...
gi 2535555261  81 EHLLPLHVCYGFA 93
Cdd:cd07363   217 EHLLPLLVALGAA 229
 
Name Accession Description Interval E-value
45_DOPA_Dioxygenase cd07363
The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both ...
 1-93 1.48e-33

The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine; This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


Pssm-ID: 153375  Cd Length: 253  Bit Score: 116.86  E-value: 1.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555261   1 GQALQTLGDQSLLLIGSGFSFHNMRAFFTPETDEAKTMNESFEDWLLETccdenLTETEREQRLINWQSAPYARYCHPRE 80
Cdd:cd07363   142 GRALAPLRDEGVLIIGSGSSVHNLRALRWGGPAPPPPWALEFDDWLKDA-----LTAGDLDALLDYWEKAPHARRAHPTE 216

                          90
                  ....*....|...
gi 2535555261  81 EHLLPLHVCYGFA 93
Cdd:cd07363   217 EHLLPLLVALGAA 229
LigB COG3384
Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites ...
 1-93 5.89e-31

Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442611  Cd Length: 260  Bit Score: 110.26  E-value: 5.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555261   1 GQALQTLGDQSLLLIGSGFSFHNMRAFFT-PETDEAKTMNESFEDWLLETCcdenltETEREQRLINWQSAPYARYCHPR 79
Cdd:COG3384   146 GRALAPLRDEGVLIIGSGSLVHNLRALRWgPGDAIPSPWAEEFDDWLLEAL------AAGDHDALLDYRPAPYARLAHPT 219

                          90
                  ....*....|....
gi 2535555261  80 EEHLLPLHVCYGFA 93
Cdd:COG3384   220 EEHLLPLLVALGAA 233
PRK10628 PRK10628
LigB family dioxygenase; Provisional
 1-86 2.59e-05

LigB family dioxygenase; Provisional


Pssm-ID: 182598  Cd Length: 246  Bit Score: 41.63  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555261   1 GQALQTLGDQSLLLIGSGFSFHNMRAFFTPETDEAKTMNESFEDWLletccDENLT--ETEREQRLINWQSAPYARYCHP 78
Cdd:PRK10628  131 GRKLAALRDEGIMLVASGNVVHNLRTVKWHGDSSPYPWAESFNQFV-----KANLTwqGPVEQHPLVNYLQHEGGALSNP 205


                  ....*...
gi 2535555261  79 REEHLLPL 86
Cdd:PRK10628  206 TPEHYLPL 213
 
Name Accession Description Interval E-value
45_DOPA_Dioxygenase cd07363
The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both ...
 1-93 1.48e-33

The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine; This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


Pssm-ID: 153375  Cd Length: 253  Bit Score: 116.86  E-value: 1.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555261   1 GQALQTLGDQSLLLIGSGFSFHNMRAFFTPETDEAKTMNESFEDWLLETccdenLTETEREQRLINWQSAPYARYCHPRE 80
Cdd:cd07363   142 GRALAPLRDEGVLIIGSGSSVHNLRALRWGGPAPPPPWALEFDDWLKDA-----LTAGDLDALLDYWEKAPHARRAHPTE 216

                          90
                  ....*....|...
gi 2535555261  81 EHLLPLHVCYGFA 93
Cdd:cd07363   217 EHLLPLLVALGAA 229
LigB COG3384
Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites ...
 1-93 5.89e-31

Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442611  Cd Length: 260  Bit Score: 110.26  E-value: 5.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555261   1 GQALQTLGDQSLLLIGSGFSFHNMRAFFT-PETDEAKTMNESFEDWLLETCcdenltETEREQRLINWQSAPYARYCHPR 79
Cdd:COG3384   146 GRALAPLRDEGVLIIGSGSLVHNLRALRWgPGDAIPSPWAEEFDDWLLEAL------AAGDHDALLDYRPAPYARLAHPT 219

                          90
                  ....*....|....
gi 2535555261  80 EEHLLPLHVCYGFA 93
Cdd:COG3384   220 EEHLLPLLVALGAA 233
PRK10628 PRK10628
LigB family dioxygenase; Provisional
 1-86 2.59e-05

LigB family dioxygenase; Provisional


Pssm-ID: 182598  Cd Length: 246  Bit Score: 41.63  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555261   1 GQALQTLGDQSLLLIGSGFSFHNMRAFFTPETDEAKTMNESFEDWLletccDENLT--ETEREQRLINWQSAPYARYCHP 78
Cdd:PRK10628  131 GRKLAALRDEGIMLVASGNVVHNLRTVKWHGDSSPYPWAESFNQFV-----KANLTwqGPVEQHPLVNYLQHEGGALSNP 205


                  ....*...
gi 2535555261  79 REEHLLPL 86
Cdd:PRK10628  206 TPEHYLPL 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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