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Conserved domains on  [gi|490999989|ref|WP_004861712|]
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MULTISPECIES: benzoate 1,2-dioxygenase small subunit [Raoultella]

Protein Classification

nuclear transport factor 2 family protein( domain architecture ID 233)

nuclear transport factor 2 (NTF2) family protein, similar to Aspergillus flavus scytalone dehydratases, Pseudomonas putida benzene 1,2-dioxygenase subunit beta, and many other members with similar structural details but divergent functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTF2_like super family cl09109
Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 ...
 7-161 4.14e-79

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.


The actual alignment was detected with superfamily member TIGR03232:

Pssm-ID: 471850  Cd Length: 155  Bit Score: 231.24  E-value: 4.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989    7 VRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISLIYYPNREGLEDRVYRIKTERSGASTPEPR 86
Cdd:TIGR03232   1 IQAFLYREARLLDDEQWDDWLECYRADASFWMPAWDDDDQLTEDPQSEISLIYYPNRQGLEDRVFRIKTERSSATVPDTR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999989   87 TTHLISNVELLGENEQGVEVRYNWVTYNHRYQHTDAWFGSTCVTLTTCDGKPQILRKTVRLNNDYIRQVIDVYHI 161
Cdd:TIGR03232  81 TSHNISNVEIEEQDGDVITVRFNWHTLSFRYKTTDSYFGMSRYTIDFSGESPKIKSKYVVLKNDYINQVIDIYHI 155
 
Name Accession Description Interval E-value
benzo_1_2_benB TIGR03232
benzoate 1,2-dioxygenase, small subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to ...
 7-161 4.14e-79

benzoate 1,2-dioxygenase, small subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family should all act on benzoate, but several have additional known activities on various benozate analogs. Some members actually may be named more suitably according to such alternate an activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13).


Pssm-ID: 132276  Cd Length: 155  Bit Score: 231.24  E-value: 4.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989    7 VRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISLIYYPNREGLEDRVYRIKTERSGASTPEPR 86
Cdd:TIGR03232   1 IQAFLYREARLLDDEQWDDWLECYRADASFWMPAWDDDDQLTEDPQSEISLIYYPNRQGLEDRVFRIKTERSSATVPDTR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999989   87 TTHLISNVELLGENEQGVEVRYNWVTYNHRYQHTDAWFGSTCVTLTTCDGKPQILRKTVRLNNDYIRQVIDVYHI 161
Cdd:TIGR03232  81 TSHNISNVEIEEQDGDVITVRFNWHTLSFRYKTTDSYFGMSRYTIDFSGESPKIKSKYVVLKNDYINQVIDIYHI 155
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 3-160 1.51e-52

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: 164.35  E-value: 1.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   3 TLEQVRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISLIYYPNREGLEDRVYRIKTERSGAST 82
Cdd:cd00667    2 LQAEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPARENRERRDEDPGLELSAIYDDDRRMLEDRVVRLRTGRAWSED 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999989  83 PEPRTTHLISNVELLGENEQGVEVRYNWVTYNHRYQ-HTDAWFGSTCVTLTTCDGKPQILRKTVRLNNDYIRQVIDVYH 160
Cdd:cd00667   82 PPSRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLDgESDVFAGGRYDDLRRSEDGLRIASRRVVLDNDRIPTVNLSPF 160
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 1-161 6.26e-50

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


Pssm-ID: 444268  Cd Length: 162  Bit Score: 157.70  E-value: 6.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   1 MLTLEQVRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDkltRDPQREISLIYyPNREGLEDRVYRIKTERSGA 80
Cdd:COG5517    5 LELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENRD---TDPGLPLSLIY-DDRAMLEDRVARLRTGNAWA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989  81 STPEPRTTHLISNVELLGENEQGVEVRYNWVTYNHRYQHTDAWFGSTCV-TLTTCDGKPQILRKTVRLNNDYIRQVIDVY 159
Cdd:COG5517   81 EDPPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRRDGQTDLFVGRYEdRLRRTGGGLRIARRRVVLDNSVIPTKNLSY 160


                 ..
gi 490999989 160 HI 161
Cdd:COG5517  161 PL 162
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 14-154 1.25e-43

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


Pssm-ID: 425916  Cd Length: 144  Bit Score: 140.89  E-value: 1.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   14 EARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISLIYYPNREGLEDRVYRIKTERSGASTPEPRTTHLISN 93
Cdd:pfam00866   2 EARLLDDRDWDAWLALLAEDIHYWMPQREDRQRRDRDPQREESAIFDDDRAGLEDRVFRIRTGRAWAEDPPSRTRHLVSN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999989   94 VELLGENEQG-VEVRYNWVTYNHRYQHT-DAWFGSTCVTLTTCDGKPQILRKTVRLNNDYIRQ 154
Cdd:pfam00866  82 VRVEETEADGeLEVRSNFIVYRNRLERQvDSFAGRRTDVLRRSGDGFKIARRTILLDNSVIPS 144
PRK10069 PRK10069
3-phenylpropionate/cinnamic acid dioxygenase subunit beta;
6-117 1.13e-16

3-phenylpropionate/cinnamic acid dioxygenase subunit beta;


Pssm-ID: 236647  Cd Length: 183  Bit Score: 73.14  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   6 QVRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISL-----IYYPNREGLEDRVYRIKTERSGA 80
Cdd:PRK10069  21 EISQFLYREARLLDEWRYDDWLALLAEDIHYTMPMRTTVNAQRRDRREGVQTpptmaWFDDNKDQLERRVARLETGMAWA 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490999989  81 STPEPRTTHLISNVEL-LGENEQGVEVRYNWVTYNHRY 117
Cdd:PRK10069 101 EEPPSRLRHLITNVRVeETDIPDEFAVRSNFLLYRSRG 138
 
Name Accession Description Interval E-value
benzo_1_2_benB TIGR03232
benzoate 1,2-dioxygenase, small subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to ...
 7-161 4.14e-79

benzoate 1,2-dioxygenase, small subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family should all act on benzoate, but several have additional known activities on various benozate analogs. Some members actually may be named more suitably according to such alternate an activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13).


Pssm-ID: 132276  Cd Length: 155  Bit Score: 231.24  E-value: 4.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989    7 VRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISLIYYPNREGLEDRVYRIKTERSGASTPEPR 86
Cdd:TIGR03232   1 IQAFLYREARLLDDEQWDDWLECYRADASFWMPAWDDDDQLTEDPQSEISLIYYPNRQGLEDRVFRIKTERSSATVPDTR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999989   87 TTHLISNVELLGENEQGVEVRYNWVTYNHRYQHTDAWFGSTCVTLTTCDGKPQILRKTVRLNNDYIRQVIDVYHI 161
Cdd:TIGR03232  81 TSHNISNVEIEEQDGDVITVRFNWHTLSFRYKTTDSYFGMSRYTIDFSGESPKIKSKYVVLKNDYINQVIDIYHI 155
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 3-160 1.51e-52

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: 164.35  E-value: 1.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   3 TLEQVRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISLIYYPNREGLEDRVYRIKTERSGAST 82
Cdd:cd00667    2 LQAEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPARENRERRDEDPGLELSAIYDDDRRMLEDRVVRLRTGRAWSED 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999989  83 PEPRTTHLISNVELLGENEQGVEVRYNWVTYNHRYQ-HTDAWFGSTCVTLTTCDGKPQILRKTVRLNNDYIRQVIDVYH 160
Cdd:cd00667   82 PPSRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLDgESDVFAGGRYDDLRRSEDGLRIASRRVVLDNDRIPTVNLSPF 160
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 1-161 6.26e-50

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


Pssm-ID: 444268  Cd Length: 162  Bit Score: 157.70  E-value: 6.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   1 MLTLEQVRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDkltRDPQREISLIYyPNREGLEDRVYRIKTERSGA 80
Cdd:COG5517    5 LELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENRD---TDPGLPLSLIY-DDRAMLEDRVARLRTGNAWA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989  81 STPEPRTTHLISNVELLGENEQGVEVRYNWVTYNHRYQHTDAWFGSTCV-TLTTCDGKPQILRKTVRLNNDYIRQVIDVY 159
Cdd:COG5517   81 EDPPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRRDGQTDLFVGRYEdRLRRTGGGLRIARRRVVLDNSVIPTKNLSY 160


                 ..
gi 490999989 160 HI 161
Cdd:COG5517  161 PL 162
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 14-154 1.25e-43

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


Pssm-ID: 425916  Cd Length: 144  Bit Score: 140.89  E-value: 1.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   14 EARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISLIYYPNREGLEDRVYRIKTERSGASTPEPRTTHLISN 93
Cdd:pfam00866   2 EARLLDDRDWDAWLALLAEDIHYWMPQREDRQRRDRDPQREESAIFDDDRAGLEDRVFRIRTGRAWAEDPPSRTRHLVSN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490999989   94 VELLGENEQG-VEVRYNWVTYNHRYQHT-DAWFGSTCVTLTTCDGKPQILRKTVRLNNDYIRQ 154
Cdd:pfam00866  82 VRVEETEADGeLEVRSNFIVYRNRLERQvDSFAGRRTDVLRRSGDGFKIARRTILLDNSVIPS 144
anthran_1_2_B TIGR03231
anthranilate 1,2-dioxygenase, small subunit; Anthranilate (2-aminobenzoate) is an intermediate ...
 7-161 2.24e-40

anthranilate 1,2-dioxygenase, small subunit; Anthranilate (2-aminobenzoate) is an intermediate of tryptophan (Trp) biosynthesis and degradation. Members of this family are the small subunit of anthranilate 1,2-dioxygenase, which acts in Trp degradation by converting anthranilate to catechol. Closely related paralogs typically are the benzoate 1,2-dioxygenase small subunit, among the larger set of ring-hydroxylating dioxygenases. [Energy metabolism, Amino acids and amines]


Pssm-ID: 132275  Cd Length: 155  Bit Score: 133.10  E-value: 2.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989    7 VRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISLIYYPNREGLEDRVYRIKTERSGASTPEPR 86
Cdd:TIGR03231   1 VEQFLYRKAELCDAQDWDAYLDLFDEDSEFHLPQWISEHNYTRDPKRELSLIYYEDRSGLEDRVFRIRTGKAASTTPMPR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999989   87 TTHLISNVELLGENEQGVEVRYNWVTYNHRYQHTDAWFGSTCVTLTTCDGKPQILRKTVRLNNDYIRQVIDVYHI 161
Cdd:TIGR03231  81 TLHNIHNVRIAELEDGLLRVRVNWRTLFNRLGLEGCFYGHATYVLKPTGDSWLIRRKHSVLLNDKIDSVLDFYHL 155
PRK10069 PRK10069
3-phenylpropionate/cinnamic acid dioxygenase subunit beta;
6-117 1.13e-16

3-phenylpropionate/cinnamic acid dioxygenase subunit beta;


Pssm-ID: 236647  Cd Length: 183  Bit Score: 73.14  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   6 QVRQFLYYEARLLDDRQWDQWLTCYSPKVVFWMPAWGDDDKLTRDPQREISL-----IYYPNREGLEDRVYRIKTERSGA 80
Cdd:PRK10069  21 EISQFLYREARLLDEWRYDDWLALLAEDIHYTMPMRTTVNAQRRDRREGVQTpptmaWFDDNKDQLERRVARLETGMAWA 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490999989  81 STPEPRTTHLISNVEL-LGENEQGVEVRYNWVTYNHRY 117
Cdd:PRK10069 101 EEPPSRLRHLITNVRVeETDIPDEFAVRSNFLLYRSRG 138
NTF2_like cd00531
Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 ...
 7-148 2.51e-16

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: 70.62  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999989   7 VRQFLYYEARLLDdRQWDQWLTCYSPKVVFWMPAWGDddkltrdpqreiSLIYYPN-REGLEDRVYRIKTERsgastpeP 85
Cdd:cd00531    1 AEQFLYRYARLLD-AGDREWLALLYADDAYFEPPGGD------------GLIYPDDgREAIEDRVRRLPFGP-------S 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999989  86 RTTHLISNVELLGENEQGVEVRYNWVTYNHRYQHTDAWFGSTCV-TLTTCDGKPQILRKTVRLN 148
Cdd:cd00531   61 RTRHLVSNVDVQPGDDGEGVVVSVFGVLRTRGDGEQDVFAGGQTfVLRPQGGGGKIANRRFRLD 124
 
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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