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Conserved domains on  [gi|1063697018|ref|NP_001322794|]
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2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily protein [Arabidopsis thaliana]

Protein Classification

2OG-Fe(II) oxygenase( domain architecture ID 10614554)

2OG-Fe(II) oxygenase belonging to the large and diverse Fe(II)- and 2-oxoglutarate (2-OG)-dependent dioxygenase superfamily that share a common reaction mechanism, using Fe(II) and the cosubstrate 2-OG in the active site to activate oxygen, resulting in the two-electron oxidation of the target substrate

CATH:  2.60.120.620
EC:  1.14.11.-
Gene Ontology:  GO:0008198|GO:0016705
PubMed:  11276424

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 87-149 1.70e-07

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


:

Pssm-ID: 463943  Cd Length: 94  Bit Score: 48.53  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063697018  87 GASIGWHSDDNRS-------------YL-KQRDFASGE--------PVTVAPSAGDVIMYTADDRNIHSVDEVTDGERLT 144
Cdd:pfam13640   9 GGFYKPHLDFFEGaegggqrrltvvlYLnDWEEEEGGElvlydgdgVEDIKPKKGRLVLFPSSELSLHEVLPVTGGERWS 88


                  ....*
gi 1063697018 145 LALWF 149
Cdd:pfam13640  89 ITGWF 93
 
Name Accession Description Interval E-value
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 87-149 1.70e-07

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 48.53  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063697018  87 GASIGWHSDDNRS-------------YL-KQRDFASGE--------PVTVAPSAGDVIMYTADDRNIHSVDEVTDGERLT 144
Cdd:pfam13640   9 GGFYKPHLDFFEGaegggqrrltvvlYLnDWEEEEGGElvlydgdgVEDIKPKKGRLVLFPSSELSLHEVLPVTGGERWS 88


                  ....*
gi 1063697018 145 LALWF 149
Cdd:pfam13640  89 ITGWF 93
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 55-149 2.89e-05

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 43.92  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063697018   55 ELTERLKEKIEETFG--CEYELFIEFTGLISWCKGASIGWHSD----DNRS-----YLKQrDFASGE----------PVT 113
Cdd:smart00702  49 LVIERIRQRLADFLGllAGLPLSAEDAQVARYGPGGHYGPHVDnflyGDRIatfilYLND-VEEGGElvfpglrlmvVAT 127

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1063697018  114 VAPSAGDVIM-YTADDRNIHSVDEVTDGERLTLALWF 149
Cdd:smart00702 128 VKPKKGDLLFfPSGHGRSLHGVCPVTRGSRWAITGWI 164
 
Name Accession Description Interval E-value
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 87-149 1.70e-07

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 48.53  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063697018  87 GASIGWHSDDNRS-------------YL-KQRDFASGE--------PVTVAPSAGDVIMYTADDRNIHSVDEVTDGERLT 144
Cdd:pfam13640   9 GGFYKPHLDFFEGaegggqrrltvvlYLnDWEEEEGGElvlydgdgVEDIKPKKGRLVLFPSSELSLHEVLPVTGGERWS 88


                  ....*
gi 1063697018 145 LALWF 149
Cdd:pfam13640  89 ITGWF 93
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 55-149 2.89e-05

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 43.92  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063697018   55 ELTERLKEKIEETFG--CEYELFIEFTGLISWCKGASIGWHSD----DNRS-----YLKQrDFASGE----------PVT 113
Cdd:smart00702  49 LVIERIRQRLADFLGllAGLPLSAEDAQVARYGPGGHYGPHVDnflyGDRIatfilYLND-VEEGGElvfpglrlmvVAT 127

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1063697018  114 VAPSAGDVIM-YTADDRNIHSVDEVTDGERLTLALWF 149
Cdd:smart00702 128 VKPKKGDLLFfPSGHGRSLHGVCPVTRGSRWAITGWI 164
 
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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