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Conserved domains on  [gi|999645|pdb|1MMO|B]
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Chain B, METHANE MONOOXYGENASE HYDROLASE (BETA CHAIN)

Protein Classification

aromatic/alkene monooxygenase hydroxylase subunit beta( domain architecture ID 10099412)

aromatic/alkene monooxygenase hydroxylase (AAMH) subunit beta is a component of an AAMH multicomponent enzyme system, such as alkene monooxygenase that catalyzes the O2- and NADH-dependent epoxidation of alkenes to their corresponding epoxides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAMH_B cd01058
Aromatic and Alkene Monooxygenase Hydroxylase, subunit B, ferritin-like diiron-binding domain; ...
 37-363 2.05e-96

Aromatic and Alkene Monooxygenase Hydroxylase, subunit B, ferritin-like diiron-binding domain; Aromatic and Alkene Monooxygenase Hydroxylases, subunit B (AAMH_B). Subunit B (beta) of the soluble hydroxylase of multicomponent, aromatic and alkene monooxygenases are members of a superfamily of ferritin-like iron-storage proteins. AAMH exists as a hexamer (an alpha2-beta2-gamma2 homodimer) with each alpha-subunit housing one nonheme diiron center embedded in a four-helix bundle. The N-terminal domain of the alpha- and noncatalytic beta-subunits possess nearly identical folds; the beta-subunit lacks the C-terminal domain found in the alpha-subunit. Methane monooxygenase is a multicomponent enzyme found in methanotrophic bacteria that catalyzes the hydroxylation of methane and higher alkenes (as large as octane). Phenol monooxygenase, found in a diverse group of bacteria, catalyses the hydroxylation of phenol, chloro- and methyl-phenol and naphthol. Both enzyme systems consist of three components: the hydroxylase, a coupling protein and a reductase. In the MMO hydroxylase, dioxygen and substrate interact with the diiron center in a hydrophobic cavity at the active site. The reductase component and protein coupling factor provide electrons from NADH for reducing the oxidized binuclear iron-oxo cluster to its reduced form. Reaction with dioxygen produces a peroxy-bridged complex and dehydration leads to the formation of complex Q, which is thought to be the oxygenating species that carries out the insertion of an oxygen atom into a C-H bond of the substrate. The toluene monooxygenase systems, toluene 2-, 3-, and 4-monooxygenase, are similar to MMO but with an additional component, a Rieske-type ferredoxin. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Alkane omega-hydroxylase (AlkB) and xylene monooxygenase are members of a distinct class of integral membrane diiron proteins and are not included in this CD.


:

Pssm-ID: 153116  Cd Length: 304  Bit Score: 289.55  E-value: 2.05e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B       37 RWKRLTEYEALTVYAQPNADWIAGGLDWGDWtqKFHGGRPSWGNETTELRTVDWFKHRDPLRRWHAPYVKDKAEEWRYTD 116
Cdd:cd01058   1 RRRRPSEYEDVTRYQQPTPDRQPTPNWHYRP--LFDNGRPLYDRESTALRMSDWYAFRDPRQFWYRTYVQMRAEQERYVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      117 RFLQGYSADGQIRAMNPTWRTsSCNRYWGAFLFNEYGLFNAHSQGAREALSDVTRVSLAFWGFDKIDIAQMIQLERGFLA 196
Cdd:cd01058  79 RLFEFAEKRGLAEALSPEWRE-FLARYLGPLRHVEHGLQMANAYVAQYAPSTTITNAAAFQAMDKLRIAQDIAYRGLELD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      197 KIVPGFDesTAVPKAEWTNGEVYKSARLAVEGLWQeVFDWNESAFSVHAVYDALFGQFVRREfFQRLAPRFGDNLTPFFI 276
Cdd:cd01058 158 GNTPGFD--GDAAKEAWEEDPAWQGLRELVEKLLV-TYDWGEAFVAQNLVFDPLVGELVRRE-LDRLAASNGDTLTPLLT 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      277 NQAQTYFQIAKQGVQDLYYnCLGDDpefSDYNRTVMRNWTGKWLEPTIAALRDFMGLFAklpagttdkeeitASLYRVVD 356
Cdd:cd01058 234 EFMLDDAQRHRRWTDALVK-TAAED---SPHNRALLQGWLEKWRPRALAALAALAIALS-------------ASLPAAVA 296


                ....*..
1MMO_B      357 DWIEDYA 363
Cdd:cd01058 297 AARADLA 303
 
Name Accession Description Interval E-value
AAMH_B cd01058
Aromatic and Alkene Monooxygenase Hydroxylase, subunit B, ferritin-like diiron-binding domain; ...
 37-363 2.05e-96

Aromatic and Alkene Monooxygenase Hydroxylase, subunit B, ferritin-like diiron-binding domain; Aromatic and Alkene Monooxygenase Hydroxylases, subunit B (AAMH_B). Subunit B (beta) of the soluble hydroxylase of multicomponent, aromatic and alkene monooxygenases are members of a superfamily of ferritin-like iron-storage proteins. AAMH exists as a hexamer (an alpha2-beta2-gamma2 homodimer) with each alpha-subunit housing one nonheme diiron center embedded in a four-helix bundle. The N-terminal domain of the alpha- and noncatalytic beta-subunits possess nearly identical folds; the beta-subunit lacks the C-terminal domain found in the alpha-subunit. Methane monooxygenase is a multicomponent enzyme found in methanotrophic bacteria that catalyzes the hydroxylation of methane and higher alkenes (as large as octane). Phenol monooxygenase, found in a diverse group of bacteria, catalyses the hydroxylation of phenol, chloro- and methyl-phenol and naphthol. Both enzyme systems consist of three components: the hydroxylase, a coupling protein and a reductase. In the MMO hydroxylase, dioxygen and substrate interact with the diiron center in a hydrophobic cavity at the active site. The reductase component and protein coupling factor provide electrons from NADH for reducing the oxidized binuclear iron-oxo cluster to its reduced form. Reaction with dioxygen produces a peroxy-bridged complex and dehydration leads to the formation of complex Q, which is thought to be the oxygenating species that carries out the insertion of an oxygen atom into a C-H bond of the substrate. The toluene monooxygenase systems, toluene 2-, 3-, and 4-monooxygenase, are similar to MMO but with an additional component, a Rieske-type ferredoxin. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Alkane omega-hydroxylase (AlkB) and xylene monooxygenase are members of a distinct class of integral membrane diiron proteins and are not included in this CD.


Pssm-ID: 153116  Cd Length: 304  Bit Score: 289.55  E-value: 2.05e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B       37 RWKRLTEYEALTVYAQPNADWIAGGLDWGDWtqKFHGGRPSWGNETTELRTVDWFKHRDPLRRWHAPYVKDKAEEWRYTD 116
Cdd:cd01058   1 RRRRPSEYEDVTRYQQPTPDRQPTPNWHYRP--LFDNGRPLYDRESTALRMSDWYAFRDPRQFWYRTYVQMRAEQERYVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      117 RFLQGYSADGQIRAMNPTWRTsSCNRYWGAFLFNEYGLFNAHSQGAREALSDVTRVSLAFWGFDKIDIAQMIQLERGFLA 196
Cdd:cd01058  79 RLFEFAEKRGLAEALSPEWRE-FLARYLGPLRHVEHGLQMANAYVAQYAPSTTITNAAAFQAMDKLRIAQDIAYRGLELD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      197 KIVPGFDesTAVPKAEWTNGEVYKSARLAVEGLWQeVFDWNESAFSVHAVYDALFGQFVRREfFQRLAPRFGDNLTPFFI 276
Cdd:cd01058 158 GNTPGFD--GDAAKEAWEEDPAWQGLRELVEKLLV-TYDWGEAFVAQNLVFDPLVGELVRRE-LDRLAASNGDTLTPLLT 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      277 NQAQTYFQIAKQGVQDLYYnCLGDDpefSDYNRTVMRNWTGKWLEPTIAALRDFMGLFAklpagttdkeeitASLYRVVD 356
Cdd:cd01058 234 EFMLDDAQRHRRWTDALVK-TAAED---SPHNRALLQGWLEKWRPRALAALAALAIALS-------------ASLPAAVA 296


                ....*..
1MMO_B      357 DWIEDYA 363
Cdd:cd01058 297 AARADLA 303
Phenol_Hydrox pfam02332
Methane/Phenol/Toluene Hydroxylase; Bacterial phenol hydroxylase is a multicomponent enzyme ...
 67-301 6.04e-59

Methane/Phenol/Toluene Hydroxylase; Bacterial phenol hydroxylase is a multicomponent enzyme that catabolizes phenol and some of its methylated derivatives. This Pfam family contains both the P1 and P3 polypeptides of phenol hydroxylase and the alpha and beta chain of methane hydroxylase protein A.


Pssm-ID: 426724  Cd Length: 229  Bit Score: 190.93  E-value: 6.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B         67 WTQKFHGGRPSWGneTTELRTVDWFKHRDPLRRWHAPYVKDKAEEWRYTDRFLQGYSADGQIRAMNPTWRTSSCnRYWGA 146
Cdd:pfam02332   1 WTPSYVDGDPSYP--YTALRMSDWYAFRDPDRLTYRTYVKMQAEKEERVYGVLDAAERSGLFARLDPAWREVLK-LHLGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B        147 FLFNEYGLFNAHSQGAREALSDVTRVSLAFWGFDKIDIAQMIQLERGFLAKIVPG-FDESTAvpKAEWTNGEVYKSARLA 225
Cdd:pfam02332  78 LRHLEYGAQMANAYLARYGPGTAIRNAATFQALDELRHAQIITYLGLELAKAYPGaFDGSLD--KAAWLNDPAWQPLRRL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MMO_B        226 VEGLwQEVFDWNESAFSVHAVYDALFGQFVRREfFQRLAPRFGDNLTPFFINQAQTYFQIAKQGVQDLYYNCLGDD 301
Cdd:pfam02332 156 VEDI-LVAYDWFEALVALNLVFEPLLTNLLFVA-FMEVAAANGDFLTPTLISSAQSDEARHARWGDALLKFLLEDD 229
 
Name Accession Description Interval E-value
AAMH_B cd01058
Aromatic and Alkene Monooxygenase Hydroxylase, subunit B, ferritin-like diiron-binding domain; ...
 37-363 2.05e-96

Aromatic and Alkene Monooxygenase Hydroxylase, subunit B, ferritin-like diiron-binding domain; Aromatic and Alkene Monooxygenase Hydroxylases, subunit B (AAMH_B). Subunit B (beta) of the soluble hydroxylase of multicomponent, aromatic and alkene monooxygenases are members of a superfamily of ferritin-like iron-storage proteins. AAMH exists as a hexamer (an alpha2-beta2-gamma2 homodimer) with each alpha-subunit housing one nonheme diiron center embedded in a four-helix bundle. The N-terminal domain of the alpha- and noncatalytic beta-subunits possess nearly identical folds; the beta-subunit lacks the C-terminal domain found in the alpha-subunit. Methane monooxygenase is a multicomponent enzyme found in methanotrophic bacteria that catalyzes the hydroxylation of methane and higher alkenes (as large as octane). Phenol monooxygenase, found in a diverse group of bacteria, catalyses the hydroxylation of phenol, chloro- and methyl-phenol and naphthol. Both enzyme systems consist of three components: the hydroxylase, a coupling protein and a reductase. In the MMO hydroxylase, dioxygen and substrate interact with the diiron center in a hydrophobic cavity at the active site. The reductase component and protein coupling factor provide electrons from NADH for reducing the oxidized binuclear iron-oxo cluster to its reduced form. Reaction with dioxygen produces a peroxy-bridged complex and dehydration leads to the formation of complex Q, which is thought to be the oxygenating species that carries out the insertion of an oxygen atom into a C-H bond of the substrate. The toluene monooxygenase systems, toluene 2-, 3-, and 4-monooxygenase, are similar to MMO but with an additional component, a Rieske-type ferredoxin. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Alkane omega-hydroxylase (AlkB) and xylene monooxygenase are members of a distinct class of integral membrane diiron proteins and are not included in this CD.


Pssm-ID: 153116  Cd Length: 304  Bit Score: 289.55  E-value: 2.05e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B       37 RWKRLTEYEALTVYAQPNADWIAGGLDWGDWtqKFHGGRPSWGNETTELRTVDWFKHRDPLRRWHAPYVKDKAEEWRYTD 116
Cdd:cd01058   1 RRRRPSEYEDVTRYQQPTPDRQPTPNWHYRP--LFDNGRPLYDRESTALRMSDWYAFRDPRQFWYRTYVQMRAEQERYVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      117 RFLQGYSADGQIRAMNPTWRTsSCNRYWGAFLFNEYGLFNAHSQGAREALSDVTRVSLAFWGFDKIDIAQMIQLERGFLA 196
Cdd:cd01058  79 RLFEFAEKRGLAEALSPEWRE-FLARYLGPLRHVEHGLQMANAYVAQYAPSTTITNAAAFQAMDKLRIAQDIAYRGLELD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      197 KIVPGFDesTAVPKAEWTNGEVYKSARLAVEGLWQeVFDWNESAFSVHAVYDALFGQFVRREfFQRLAPRFGDNLTPFFI 276
Cdd:cd01058 158 GNTPGFD--GDAAKEAWEEDPAWQGLRELVEKLLV-TYDWGEAFVAQNLVFDPLVGELVRRE-LDRLAASNGDTLTPLLT 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B      277 NQAQTYFQIAKQGVQDLYYnCLGDDpefSDYNRTVMRNWTGKWLEPTIAALRDFMGLFAklpagttdkeeitASLYRVVD 356
Cdd:cd01058 234 EFMLDDAQRHRRWTDALVK-TAAED---SPHNRALLQGWLEKWRPRALAALAALAIALS-------------ASLPAAVA 296


                ....*..
1MMO_B      357 DWIEDYA 363
Cdd:cd01058 297 AARADLA 303
Phenol_Hydrox pfam02332
Methane/Phenol/Toluene Hydroxylase; Bacterial phenol hydroxylase is a multicomponent enzyme ...
 67-301 6.04e-59

Methane/Phenol/Toluene Hydroxylase; Bacterial phenol hydroxylase is a multicomponent enzyme that catabolizes phenol and some of its methylated derivatives. This Pfam family contains both the P1 and P3 polypeptides of phenol hydroxylase and the alpha and beta chain of methane hydroxylase protein A.


Pssm-ID: 426724  Cd Length: 229  Bit Score: 190.93  E-value: 6.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B         67 WTQKFHGGRPSWGneTTELRTVDWFKHRDPLRRWHAPYVKDKAEEWRYTDRFLQGYSADGQIRAMNPTWRTSSCnRYWGA 146
Cdd:pfam02332   1 WTPSYVDGDPSYP--YTALRMSDWYAFRDPDRLTYRTYVKMQAEKEERVYGVLDAAERSGLFARLDPAWREVLK-LHLGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MMO_B        147 FLFNEYGLFNAHSQGAREALSDVTRVSLAFWGFDKIDIAQMIQLERGFLAKIVPG-FDESTAvpKAEWTNGEVYKSARLA 225
Cdd:pfam02332  78 LRHLEYGAQMANAYLARYGPGTAIRNAATFQALDELRHAQIITYLGLELAKAYPGaFDGSLD--KAAWLNDPAWQPLRRL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MMO_B        226 VEGLwQEVFDWNESAFSVHAVYDALFGQFVRREfFQRLAPRFGDNLTPFFINQAQTYFQIAKQGVQDLYYNCLGDD 301
Cdd:pfam02332 156 VEDI-LVAYDWFEALVALNLVFEPLLTNLLFVA-FMEVAAANGDFLTPTLISSAQSDEARHARWGDALLKFLLEDD 229
 
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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