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Conserved domains on  [gi|694057548|ref|WP_032404245|]
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MULTISPECIES: aromatic-ring-hydroxylating dioxygenase subunit beta [Rhodococcus]

Protein Classification

aromatic-ring-hydroxylating dioxygenase subunit beta( domain architecture ID 10090121)

aromatic-ring-hydroxylating dioxygenase subunit beta is part of the hydroxylase component of a dioxygenase multicomponent enzyme system that catalyzes the oxidation or hydroxylation of aromatic compounds; the beta subunit may be responsible for substrate specificity and/or may have a structural role

CATH:  3.10.450.50
EC:  1.14.-.-
Gene Ontology:  GO:0006725|GO:0019439
SCOP:  4001024

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 19-171 1.30e-51

3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 444268  Cd Length: 162  Bit Score: 162.32  E-value: 1.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  19 RDVEAFIYREARLADEHNYDEWEGLWADDAIYWVPIGHGNEEDPGSDISVIFDHRRRISTRLKQLRTGHRYAQTPQSKTR 98
Cdd:COG5517    9 AEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENRDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWAEDPPSRTR 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694057548  99 RVISNAEIRSIDGNEATVEANFVIVEHRP-RATEFWSGRVTYGLRRTEGSLMMFRKKVNLINSDEVLPTLAFLI 171
Cdd:COG5517   89 HLVSNVRVEETDGGEIEVRSNFLVYRTRRdGQTDLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSYPL 162
 
Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 19-171 1.30e-51

3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 444268  Cd Length: 162  Bit Score: 162.32  E-value: 1.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  19 RDVEAFIYREARLADEHNYDEWEGLWADDAIYWVPIGHGNEEDPGSDISVIFDHRRRISTRLKQLRTGHRYAQTPQSKTR 98
Cdd:COG5517    9 AEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENRDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWAEDPPSRTR 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694057548  99 RVISNAEIRSIDGNEATVEANFVIVEHRP-RATEFWSGRVTYGLRRTEGSLMMFRKKVNLINSDEVLPTLAFLI 171
Cdd:COG5517   89 HLVSNVRVEETDGGEIEVRSNFLVYRTRRdGQTDLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSYPL 162
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 19-167 6.08e-37

Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase.The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. Aromatic-ring-hydroxylating dioxygenases oxidize aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates. The active site of these enzymes however is in the alpha sub-unit. No functional role has been attributed to the beta sub-unit except for a structural role.


Pssm-ID: 238357  Cd Length: 160  Bit Score: 125.06  E-value: 6.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  19 RDVEAFIYREARLADEHNYDEWEGLWADDAIYWVPIGHGNE---EDPGSDISVIFDH-RRRISTRLKQLRTGHRYAQTPQ 94
Cdd:cd00667    4 AEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPARENRErrdEDPGLELSAIYDDdRRMLEDRVVRLRTGRAWSEDPP 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694057548  95 SKTRRVISNAEIRSIDGNEATVEANFVIVEHRP-RATEFWSGRVTYGLRRTEGSLMMFRKKVNLINSdeVLPTL 167
Cdd:cd00667   84 SRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLdGESDVFAGGRYDDLRRSEDGLRIASRRVVLDND--RIPTV 155
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 27-160 3.22e-24

Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone dehydratase.


Pssm-ID: 425916  Cd Length: 144  Bit Score: 91.97  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548   27 REARLADEHNYDEWEGLWADDAIYWVPIGHGN---EEDPGSDISVIF-DHRRRISTRLKQLRTGHRYAQTPQSKTRRVIS 102
Cdd:pfam00866   1 REARLLDDRDWDAWLALLAEDIHYWMPQREDRqrrDRDPQREESAIFdDDRAGLEDRVFRIRTGRAWAEDPPSRTRHLVS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  103 NAEIRSID-GNEATVEANFVIVEHRPRATE-FWSGRVTYGLRRTEGSLMMFRKKVNLINS 160
Cdd:pfam00866  81 NVRVEETEaDGELEVRSNFIVYRNRLERQVdSFAGRRTDVLRRSGDGFKIARRTILLDNS 140
PRK10069 PRK10069
3-phenylpropionate/cinnamic acid dioxygenase subunit beta;
18-160 1.95e-19

3-phenylpropionate/cinnamic acid dioxygenase subunit beta;


Pssm-ID: 236647  Cd Length: 183  Bit Score: 80.46  E-value: 1.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  18 IRDVEAFIYREARLADEHNYDEWEGLWADDAIYWVPIgHGNEE----------DPGSDISVIFDHRRRISTRLKQLRTGH 87
Cdd:PRK10069  19 HHEISQFLYREARLLDEWRYDDWLALLAEDIHYTMPM-RTTVNaqrrdrregvQTPPTMAWFDDNKDQLERRVARLETGM 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694057548  88 RYAQTPQSKTRRVISNAEIRSIDG-NEATVEANFVIVEHR-PRATEFWSGRVTYGLRRTEGSLMMFRKKVNLINS 160
Cdd:PRK10069  98 AWAEEPPSRLRHLITNVRVEETDIpDEFAVRSNFLLYRSRgERDEDFLVGRREDVLRREGDGWRLARRRIVLDQA 172
 
Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 19-171 1.30e-51

3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 444268  Cd Length: 162  Bit Score: 162.32  E-value: 1.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  19 RDVEAFIYREARLADEHNYDEWEGLWADDAIYWVPIGHGNEEDPGSDISVIFDHRRRISTRLKQLRTGHRYAQTPQSKTR 98
Cdd:COG5517    9 AEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENRDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWAEDPPSRTR 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694057548  99 RVISNAEIRSIDGNEATVEANFVIVEHRP-RATEFWSGRVTYGLRRTEGSLMMFRKKVNLINSDEVLPTLAFLI 171
Cdd:COG5517   89 HLVSNVRVEETDGGEIEVRSNFLVYRTRRdGQTDLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSYPL 162
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 19-167 6.08e-37

Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase.The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. Aromatic-ring-hydroxylating dioxygenases oxidize aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates. The active site of these enzymes however is in the alpha sub-unit. No functional role has been attributed to the beta sub-unit except for a structural role.


Pssm-ID: 238357  Cd Length: 160  Bit Score: 125.06  E-value: 6.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  19 RDVEAFIYREARLADEHNYDEWEGLWADDAIYWVPIGHGNE---EDPGSDISVIFDH-RRRISTRLKQLRTGHRYAQTPQ 94
Cdd:cd00667    4 AEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPARENRErrdEDPGLELSAIYDDdRRMLEDRVVRLRTGRAWSEDPP 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694057548  95 SKTRRVISNAEIRSIDGNEATVEANFVIVEHRP-RATEFWSGRVTYGLRRTEGSLMMFRKKVNLINSdeVLPTL 167
Cdd:cd00667   84 SRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLdGESDVFAGGRYDDLRRSEDGLRIASRRVVLDND--RIPTV 155
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 27-160 3.22e-24

Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone dehydratase.


Pssm-ID: 425916  Cd Length: 144  Bit Score: 91.97  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548   27 REARLADEHNYDEWEGLWADDAIYWVPIGHGN---EEDPGSDISVIF-DHRRRISTRLKQLRTGHRYAQTPQSKTRRVIS 102
Cdd:pfam00866   1 REARLLDDRDWDAWLALLAEDIHYWMPQREDRqrrDRDPQREESAIFdDDRAGLEDRVFRIRTGRAWAEDPPSRTRHLVS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  103 NAEIRSID-GNEATVEANFVIVEHRPRATE-FWSGRVTYGLRRTEGSLMMFRKKVNLINS 160
Cdd:pfam00866  81 NVRVEETEaDGELEVRSNFIVYRNRLERQVdSFAGRRTDVLRRSGDGFKIARRTILLDNS 140
PRK10069 PRK10069
3-phenylpropionate/cinnamic acid dioxygenase subunit beta;
18-160 1.95e-19

3-phenylpropionate/cinnamic acid dioxygenase subunit beta;


Pssm-ID: 236647  Cd Length: 183  Bit Score: 80.46  E-value: 1.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  18 IRDVEAFIYREARLADEHNYDEWEGLWADDAIYWVPIgHGNEE----------DPGSDISVIFDHRRRISTRLKQLRTGH 87
Cdd:PRK10069  19 HHEISQFLYREARLLDEWRYDDWLALLAEDIHYTMPM-RTTVNaqrrdrregvQTPPTMAWFDDNKDQLERRVARLETGM 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694057548  88 RYAQTPQSKTRRVISNAEIRSIDG-NEATVEANFVIVEHR-PRATEFWSGRVTYGLRRTEGSLMMFRKKVNLINS 160
Cdd:PRK10069  98 AWAEEPPSRLRHLITNVRVEETDIpDEFAVRSNFLLYRSRgERDEDFLVGRREDVLRREGDGWRLARRRIVLDQA 172
NTF2_like cd00531
Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 ...
 21-148 2.79e-11

Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 family, Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases, and the beta subunit of Ring hydroxylating dioxygenases. This family is a classic example of divergent evolution wherein the proteins have many common structural details but diverge greatly in their function. For example, nuclear transport factor 2 (NTF2) mediates the nuclear import of RanGDP and binds to both RanGDP and FxFG repeat-containing nucleoporins while Ketosteroid isomerases catalyze the isomerization of delta-5-3-ketosteroid to delta-4-3-ketosteroid, by intramolecular transfer of the C4-beta proton to the C6-beta position. While the function of the beta sub-unit of the Ring hydroxylating dioxygenases is not known, Scytalone Dehydratases catalyzes two reactions in the biosynthetic pathway that produces fungal melanin. Members of the NTF2-like superfamily are widely distributed among bacteria, archaea and eukaryotes.


Pssm-ID: 238296 [Multi-domain]  Cd Length: 124  Bit Score: 57.52  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548  21 VEAFIYREARLADEHNYDEWEGLWADDAiYWVPIGHGNEEDPgsdisviFDHRRRISTRLKQLRTGhryaqtpQSKTRRV 100
Cdd:cd00531    1 AEQFLYRYARLLDAGDREWLALLYADDA-YFEPPGGDGLIYP-------DDGREAIEDRVRRLPFG-------PSRTRHL 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 694057548 101 ISNAEIRSIDGNEATVEANFVIVEHRP-RATEFWSGRVTYGLRRTEGSL 148
Cdd:cd00531   66 VSNVDVQPGDDGEGVVVSVFGVLRTRGdGEQDVFAGGQTFVLRPQGGGG 114
SnoaL_4 pfam13577
SnoaL-like domain; This family contains a large number of proteins that share the SnoaL fold.
 16-146 2.48e-08

SnoaL-like domain; This family contains a large number of proteins that share the SnoaL fold.


Pssm-ID: 433323 [Multi-domain]  Cd Length: 125  Bit Score: 50.02  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694057548   16 WDIRDVEAFIYREARLADEHNYDEWEGLWADDAIYWVPiGHGneedpgsdisvIFDHRRRISTRLKQLRTGHRYaqtpqs 95
Cdd:pfam13577   4 EDRAAIRDLVARYGRALDTGDWDELAALFTEDAVFDYG-GLG-----------VLEGRDAIVAGLRAALDGFLL------ 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 694057548   96 kTRRVISNAEIrSIDGNEATVEANFVIVEHRPRATEFW---SGRVTYGLRRTEG 146
Cdd:pfam13577  66 -TQHLLGNPVI-TVDGDTATGRAYLLATHVGPGDGGPEvlrGGRYEDEYVRTDG 117
 
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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