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Conserved domains on  [gi|510826636|ref|WP_016199777|]
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1,2-phenylacetyl-CoA epoxidase subunit PaaC [Elizabethkingia meningoseptica]

Protein Classification

YdbO family protein( domain architecture ID 10007323)

YdbO family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YdbO COG3396
1,2-phenylacetyl-CoA epoxidase, catalytic subunit [Secondary metabolites biosynthesis, ...
1-248 1.15e-108

1,2-phenylacetyl-CoA epoxidase, catalytic subunit [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442623  Cd Length: 264  Bit Score: 314.05  E-value: 1.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   1 MNPLYNYLLKLADDGFIMGQRLAEWCGKGPYLEEDIALTNIALDELGQANNFYQYASRLTDDGKSEDDLAFLRYEHEYVN 80
Cdd:COG3396   17 RKALIRYLLRLADDELILAQRLSEWCGRAPTLEEDIALANIAQDELGHARLLYTLAEELEGAGRDEDDLAYLRDEGEFRN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636  81 AHWVELPNEDYAQTILKVYIFSVYQKLMYQALSKSADEDLSAIAQKSLKEVKYHYTHTSSWMRIFAQGTEESRERLVIAI 160
Cdd:COG3396   97 SLLVEQPNGDWADTIARQFLFDAAAILLLEALARSSDAPLAAIAAKICKEESYHLRHGEEWVIRLGDGTEESRERMQAAL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636 161 ENIWEYTKGLFAKVEGEDDLAALNIVPDTDELYEQFIAITKQDFQDFGLEYPENPFMQLKSRTGYHTEYFGYILCELQYM 240
Cdd:COG3396  177 DRLWPYTLELFGPDDVEEALAAAGIKVDNDELRQEWLATVVPVLEEAGLTVPDEPVARGGGRQGRHTEHLGYLLAEMQYL 256

                 ....*...
gi 510826636 241 QRAYPGCT 248
Cdd:COG3396  257 QRAYPGAT 264
 
Name Accession Description Interval E-value
YdbO COG3396
1,2-phenylacetyl-CoA epoxidase, catalytic subunit [Secondary metabolites biosynthesis, ...
1-248 1.15e-108

1,2-phenylacetyl-CoA epoxidase, catalytic subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442623  Cd Length: 264  Bit Score: 314.05  E-value: 1.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   1 MNPLYNYLLKLADDGFIMGQRLAEWCGKGPYLEEDIALTNIALDELGQANNFYQYASRLTDDGKSEDDLAFLRYEHEYVN 80
Cdd:COG3396   17 RKALIRYLLRLADDELILAQRLSEWCGRAPTLEEDIALANIAQDELGHARLLYTLAEELEGAGRDEDDLAYLRDEGEFRN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636  81 AHWVELPNEDYAQTILKVYIFSVYQKLMYQALSKSADEDLSAIAQKSLKEVKYHYTHTSSWMRIFAQGTEESRERLVIAI 160
Cdd:COG3396   97 SLLVEQPNGDWADTIARQFLFDAAAILLLEALARSSDAPLAAIAAKICKEESYHLRHGEEWVIRLGDGTEESRERMQAAL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636 161 ENIWEYTKGLFAKVEGEDDLAALNIVPDTDELYEQFIAITKQDFQDFGLEYPENPFMQLKSRTGYHTEYFGYILCELQYM 240
Cdd:COG3396  177 DRLWPYTLELFGPDDVEEALAAAGIKVDNDELRQEWLATVVPVLEEAGLTVPDEPVARGGGRQGRHTEHLGYLLAEMQYL 256

                 ....*...
gi 510826636 241 QRAYPGCT 248
Cdd:COG3396  257 QRAYPGAT 264
PaaA_PaaC pfam05138
Phenylacetic acid catabolic protein; This family includes proteins such as PaaA and PaaC that ...
2-249 1.67e-91

Phenylacetic acid catabolic protein; This family includes proteins such as PaaA and PaaC that are part of a catabolic pathway of phenylacetic acid. These proteins may form part of a dioxygenase complex.


Pssm-ID: 428329  Cd Length: 251  Bit Score: 269.83  E-value: 1.67e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636    2 NPLYNYLLKLADDGFIMGQRLAEWCGKGPYLEEDIALTNIALDELGQANNFYQYASRLTDDGKSEDDLAFLRYEHEYVNA 81
Cdd:pfam05138   4 RALIRYLLQLADSELILAQRLSEWCGRAPSLEEDIALANIAQDEIGHARLLYRYAEELEGEGRDEDDLAYLRDEGEFKNS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   82 HWVELPNEDYAQTILKVYIFSVYQKLMYQALSKSADEDLSAIAQKSLKEVKYHYTHTSSWMRIFAQGTEESRERLVIAIE 161
Cdd:pfam05138  84 LLFEQPNGDWADTGVRQFLVDGAAILLQEALCRSSYGPLAAAAAKICKEESYHLRHGAEWVIRLGDGTEESHRRMQEALD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636  162 NIWEYTKGLFAKVEGEDDLAALNIVPDTDELYEQFIAITKQDFQDFGLEYPENPFMQLKSRTGYHTEYFGYILCELQYMQ 241
Cdd:pfam05138 164 RLWPYTLEMFGPDDDDQALAAAGKAVDNDELRQAWLATVVPVLEEAGLTLPDSPWLRYGGRQGRHTEHLGYLLAEMQYLQ 243

                  ....*...
gi 510826636  242 RAYPGCTW 249
Cdd:pfam05138 244 RAYPGAAW 251
PA_CoA_Oxy3 TIGR02158
phenylacetate-CoA oxygenase, PaaI subunit; Phenylacetate-CoA oxygenase is comprised of a five ...
11-249 5.67e-80

phenylacetate-CoA oxygenase, PaaI subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131213  Cd Length: 237  Bit Score: 240.09  E-value: 5.67e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   11 LADDGFIMGQRLAEWCGKGPYLEEDIALTNIALDELGQANNFYQYASRLtdDGKSEDDLAFLRYEHEYVNAHWVELPNED 90
Cdd:TIGR02158   1 LGDDALVLAQRGGEWCGHAPELEEDIALANIALDLLGHARMFLSLAGQL--GGGDEDTLAFFRDEAEFRNLRLTELPNGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   91 YAQTILKVYIFSVYQKLMYQALSKSADEDLSAIAQKSLKEVKYHYTHTSSWMRIFAQGTEESRERLVIAIENIWEYTKGL 170
Cdd:TIGR02158  79 FALTIARQFLYDAYKVLLLEALTQSRDVPLAAIAAKALKEARYHLQHAKTWLERLGLGTEESHRRLQEALNELWPYTAEL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510826636  171 FAKVEGEDDLAALNIVPDTDELYEQFIAITKQDFQDFGLEYPENPFMQLKSRTGYHTEYFGYILCELQYMQRAYPGCTW 249
Cdd:TIGR02158 159 FEAGPIDEELAEAGIAVDPATLQAAWEKEVNAVLNEATLTLPQQTFYRSNGRNGEHTEHLGPLLAEMQELQRSHPGAQW 237
 
Name Accession Description Interval E-value
YdbO COG3396
1,2-phenylacetyl-CoA epoxidase, catalytic subunit [Secondary metabolites biosynthesis, ...
1-248 1.15e-108

1,2-phenylacetyl-CoA epoxidase, catalytic subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442623  Cd Length: 264  Bit Score: 314.05  E-value: 1.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   1 MNPLYNYLLKLADDGFIMGQRLAEWCGKGPYLEEDIALTNIALDELGQANNFYQYASRLTDDGKSEDDLAFLRYEHEYVN 80
Cdd:COG3396   17 RKALIRYLLRLADDELILAQRLSEWCGRAPTLEEDIALANIAQDELGHARLLYTLAEELEGAGRDEDDLAYLRDEGEFRN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636  81 AHWVELPNEDYAQTILKVYIFSVYQKLMYQALSKSADEDLSAIAQKSLKEVKYHYTHTSSWMRIFAQGTEESRERLVIAI 160
Cdd:COG3396   97 SLLVEQPNGDWADTIARQFLFDAAAILLLEALARSSDAPLAAIAAKICKEESYHLRHGEEWVIRLGDGTEESRERMQAAL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636 161 ENIWEYTKGLFAKVEGEDDLAALNIVPDTDELYEQFIAITKQDFQDFGLEYPENPFMQLKSRTGYHTEYFGYILCELQYM 240
Cdd:COG3396  177 DRLWPYTLELFGPDDVEEALAAAGIKVDNDELRQEWLATVVPVLEEAGLTVPDEPVARGGGRQGRHTEHLGYLLAEMQYL 256

                 ....*...
gi 510826636 241 QRAYPGCT 248
Cdd:COG3396  257 QRAYPGAT 264
PaaA_PaaC pfam05138
Phenylacetic acid catabolic protein; This family includes proteins such as PaaA and PaaC that ...
2-249 1.67e-91

Phenylacetic acid catabolic protein; This family includes proteins such as PaaA and PaaC that are part of a catabolic pathway of phenylacetic acid. These proteins may form part of a dioxygenase complex.


Pssm-ID: 428329  Cd Length: 251  Bit Score: 269.83  E-value: 1.67e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636    2 NPLYNYLLKLADDGFIMGQRLAEWCGKGPYLEEDIALTNIALDELGQANNFYQYASRLTDDGKSEDDLAFLRYEHEYVNA 81
Cdd:pfam05138   4 RALIRYLLQLADSELILAQRLSEWCGRAPSLEEDIALANIAQDEIGHARLLYRYAEELEGEGRDEDDLAYLRDEGEFKNS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   82 HWVELPNEDYAQTILKVYIFSVYQKLMYQALSKSADEDLSAIAQKSLKEVKYHYTHTSSWMRIFAQGTEESRERLVIAIE 161
Cdd:pfam05138  84 LLFEQPNGDWADTGVRQFLVDGAAILLQEALCRSSYGPLAAAAAKICKEESYHLRHGAEWVIRLGDGTEESHRRMQEALD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636  162 NIWEYTKGLFAKVEGEDDLAALNIVPDTDELYEQFIAITKQDFQDFGLEYPENPFMQLKSRTGYHTEYFGYILCELQYMQ 241
Cdd:pfam05138 164 RLWPYTLEMFGPDDDDQALAAAGKAVDNDELRQAWLATVVPVLEEAGLTLPDSPWLRYGGRQGRHTEHLGYLLAEMQYLQ 243

                  ....*...
gi 510826636  242 RAYPGCTW 249
Cdd:pfam05138 244 RAYPGAAW 251
PA_CoA_Oxy3 TIGR02158
phenylacetate-CoA oxygenase, PaaI subunit; Phenylacetate-CoA oxygenase is comprised of a five ...
11-249 5.67e-80

phenylacetate-CoA oxygenase, PaaI subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131213  Cd Length: 237  Bit Score: 240.09  E-value: 5.67e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   11 LADDGFIMGQRLAEWCGKGPYLEEDIALTNIALDELGQANNFYQYASRLtdDGKSEDDLAFLRYEHEYVNAHWVELPNED 90
Cdd:TIGR02158   1 LGDDALVLAQRGGEWCGHAPELEEDIALANIALDLLGHARMFLSLAGQL--GGGDEDTLAFFRDEAEFRNLRLTELPNGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510826636   91 YAQTILKVYIFSVYQKLMYQALSKSADEDLSAIAQKSLKEVKYHYTHTSSWMRIFAQGTEESRERLVIAIENIWEYTKGL 170
Cdd:TIGR02158  79 FALTIARQFLYDAYKVLLLEALTQSRDVPLAAIAAKALKEARYHLQHAKTWLERLGLGTEESHRRLQEALNELWPYTAEL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510826636  171 FAKVEGEDDLAALNIVPDTDELYEQFIAITKQDFQDFGLEYPENPFMQLKSRTGYHTEYFGYILCELQYMQRAYPGCTW 249
Cdd:TIGR02158 159 FEAGPIDEELAEAGIAVDPATLQAAWEKEVNAVLNEATLTLPQQTFYRSNGRNGEHTEHLGPLLAEMQELQRSHPGAQW 237
 
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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