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Conserved domains on  [gi|42572777|ref|NP_974484|]
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2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily protein [Arabidopsis thaliana]

Protein Classification

2OG-Fe(II) oxygenase family protein( domain architecture ID 10504650)

2OG-Fe(II) oxygenase family protein similar to 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
Gene Ontology:  GO:0016705
PubMed:  8703429

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
143-238 3.53e-06

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.


:

Pssm-ID: 397334 [Multi-domain]  Cd Length: 101  Bit Score: 44.75  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777   143 HYDYGIFTVLtdpmflspysYQefslmSSHSYLQIYHpsKNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPE 222
Cdd:pfam03171  25 HTDASILTIL----------LQ-----DDVGGLQVFK--DGKWIDVPPLPGALVVNIGDQLELLSNGRYKSVLHRVLPVN 87
                          90
                  ....*....|....*.
gi 42572777   223 KldHVSRETFVVFLHP 238
Cdd:pfam03171  88 K--GKERISIAFFLRP 101
PcbC super family cl34623
Isopenicillin N synthase and related dioxygenases [Secondary metabolites biosynthesis, ...
27-240 1.56e-05

Isopenicillin N synthase and related dioxygenases [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3491:

Pssm-ID: 442714 [Multi-domain]  Cd Length: 320  Bit Score: 45.57  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777  27 DLQEDDDDAFTNLGG---------AFKELGFC----MRELGLSIARLCDREIGgglLEESLLDSCTAKG----RLIHYHS 89
Cdd:COG3491 109 ELPPDDPDAGPPLYGpnqwpeelpGFREAVLAyyaaLEALGRRLLRAFALALG---LPEDYFDDLFDDPnsilRLIHYPP 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777  90 AADkyALRESQRRnqsgnrvsskrrvqnAAEqelnrrngaglsgshfnlwqqwHYDYGIFTVLtdpmflspysyqefsLM 169
Cdd:COG3491 186 QPA--PPPPGQVG---------------AGA----------------------HTDYGLLTLL---------------LQ 211
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572777 170 SSHSYLQIYHPSkNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPekLDHVSRETFVVFLHPKW 240
Cdd:COG3491 212 DDVGGLQVLTRD-GEWIDAPPVPGAFVVNIGDMLERWTNGRLRSTPHRVVNP--AAGRERYSIPFFLHPNP 279
 
Name Accession Description Interval E-value
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
143-238 3.53e-06

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.


Pssm-ID: 397334 [Multi-domain]  Cd Length: 101  Bit Score: 44.75  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777   143 HYDYGIFTVLtdpmflspysYQefslmSSHSYLQIYHpsKNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPE 222
Cdd:pfam03171  25 HTDASILTIL----------LQ-----DDVGGLQVFK--DGKWIDVPPLPGALVVNIGDQLELLSNGRYKSVLHRVLPVN 87
                          90
                  ....*....|....*.
gi 42572777   223 KldHVSRETFVVFLHP 238
Cdd:pfam03171  88 K--GKERISIAFFLRP 101
PcbC COG3491
Isopenicillin N synthase and related dioxygenases [Secondary metabolites biosynthesis, ...
27-240 1.56e-05

Isopenicillin N synthase and related dioxygenases [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442714 [Multi-domain]  Cd Length: 320  Bit Score: 45.57  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777  27 DLQEDDDDAFTNLGG---------AFKELGFC----MRELGLSIARLCDREIGgglLEESLLDSCTAKG----RLIHYHS 89
Cdd:COG3491 109 ELPPDDPDAGPPLYGpnqwpeelpGFREAVLAyyaaLEALGRRLLRAFALALG---LPEDYFDDLFDDPnsilRLIHYPP 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777  90 AADkyALRESQRRnqsgnrvsskrrvqnAAEqelnrrngaglsgshfnlwqqwHYDYGIFTVLtdpmflspysyqefsLM 169
Cdd:COG3491 186 QPA--PPPPGQVG---------------AGA----------------------HTDYGLLTLL---------------LQ 211
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572777 170 SSHSYLQIYHPSkNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPekLDHVSRETFVVFLHPKW 240
Cdd:COG3491 212 DDVGGLQVLTRD-GEWIDAPPVPGAFVVNIGDMLERWTNGRLRSTPHRVVNP--AAGRERYSIPFFLHPNP 279
PTZ00273 PTZ00273
oxidase reductase; Provisional
143-223 4.93e-04

oxidase reductase; Provisional


Pssm-ID: 140299 [Multi-domain]  Cd Length: 320  Bit Score: 41.28  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777  143 HYDYGIFTVLtdpmflspysYQEfslmsSHSYLQIYHPSkNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPE 222
Cdd:PTZ00273 200 HTDYGIITLL----------YQD-----SVGGLQVRNLS-GEWMDVPPLEGSFVVNIGDMMEMWSNGRYRSTPHRVVNTG 263

                 .
gi 42572777  223 K 223
Cdd:PTZ00273 264 V 264
 
Name Accession Description Interval E-value
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
143-238 3.53e-06

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.


Pssm-ID: 397334 [Multi-domain]  Cd Length: 101  Bit Score: 44.75  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777   143 HYDYGIFTVLtdpmflspysYQefslmSSHSYLQIYHpsKNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPE 222
Cdd:pfam03171  25 HTDASILTIL----------LQ-----DDVGGLQVFK--DGKWIDVPPLPGALVVNIGDQLELLSNGRYKSVLHRVLPVN 87
                          90
                  ....*....|....*.
gi 42572777   223 KldHVSRETFVVFLHP 238
Cdd:pfam03171  88 K--GKERISIAFFLRP 101
PcbC COG3491
Isopenicillin N synthase and related dioxygenases [Secondary metabolites biosynthesis, ...
27-240 1.56e-05

Isopenicillin N synthase and related dioxygenases [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442714 [Multi-domain]  Cd Length: 320  Bit Score: 45.57  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777  27 DLQEDDDDAFTNLGG---------AFKELGFC----MRELGLSIARLCDREIGgglLEESLLDSCTAKG----RLIHYHS 89
Cdd:COG3491 109 ELPPDDPDAGPPLYGpnqwpeelpGFREAVLAyyaaLEALGRRLLRAFALALG---LPEDYFDDLFDDPnsilRLIHYPP 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777  90 AADkyALRESQRRnqsgnrvsskrrvqnAAEqelnrrngaglsgshfnlwqqwHYDYGIFTVLtdpmflspysyqefsLM 169
Cdd:COG3491 186 QPA--PPPPGQVG---------------AGA----------------------HTDYGLLTLL---------------LQ 211
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572777 170 SSHSYLQIYHPSkNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPekLDHVSRETFVVFLHPKW 240
Cdd:COG3491 212 DDVGGLQVLTRD-GEWIDAPPVPGAFVVNIGDMLERWTNGRLRSTPHRVVNP--AAGRERYSIPFFLHPNP 279
PTZ00273 PTZ00273
oxidase reductase; Provisional
143-223 4.93e-04

oxidase reductase; Provisional


Pssm-ID: 140299 [Multi-domain]  Cd Length: 320  Bit Score: 41.28  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572777  143 HYDYGIFTVLtdpmflspysYQEfslmsSHSYLQIYHPSkNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPE 222
Cdd:PTZ00273 200 HTDYGIITLL----------YQD-----SVGGLQVRNLS-GEWMDVPPLEGSFVVNIGDMMEMWSNGRYRSTPHRVVNTG 263

                 .
gi 42572777  223 K 223
Cdd:PTZ00273 264 V 264
 
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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