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Conserved domains on  [gi|1285905149|gb|ATZ76324|]
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phenylacetate-CoA oxygenase subunit PaaB [uncultured Alphaproteobacteria bacterium]

Protein Classification

PaaB family protein( domain architecture ID 10007418)

PaaB family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaB COG3460
1,2-phenylacetyl-CoA epoxidase, PaaB subunit [Secondary metabolites biosynthesis, transport ...
 1-90 1.64e-39

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


:

Pssm-ID: 442683  Cd Length: 98  Bit Score: 126.22  E-value: 1.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285905149  1 MPLWEVFIRSRTGQSHRHVGSLHAADAALALQAARDVYTRRGEGNSIWVVPAASITASDPAERGMLFEPAESKIYRHPTF 80
Cdd:COG3460    9 WPLWEVFVRSKPGLPHRHVGSLHAPDAEMALQNARDVFTRREEGVSIWVVPSDAITASSPEEKDAFFDPAADKVYRHPTF 88

                         90
                 ....*....|
gi 1285905149 81 YTIPDDVGHM 90
Cdd:COG3460   89 YEVPEKVEHM 98
 
Name Accession Description Interval E-value
PaaB COG3460
1,2-phenylacetyl-CoA epoxidase, PaaB subunit [Secondary metabolites biosynthesis, transport ...
 1-90 1.64e-39

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


Pssm-ID: 442683  Cd Length: 98  Bit Score: 126.22  E-value: 1.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285905149  1 MPLWEVFIRSRTGQSHRHVGSLHAADAALALQAARDVYTRRGEGNSIWVVPAASITASDPAERGMLFEPAESKIYRHPTF 80
Cdd:COG3460    9 WPLWEVFVRSKPGLPHRHVGSLHAPDAEMALQNARDVFTRREEGVSIWVVPSDAITASSPEEKDAFFDPAADKVYRHPTF 88

                         90
                 ....*....|
gi 1285905149 81 YTIPDDVGHM 90
Cdd:COG3460   89 YEVPEKVEHM 98
PaaB pfam06243
Phenylacetic acid degradation B; Phenylacetic acid degradation protein B (PaaB) is thought to ...
 2-87 1.18e-38

Phenylacetic acid degradation B; Phenylacetic acid degradation protein B (PaaB) is thought to be part of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation.


Pssm-ID: 428844  Cd Length: 88  Bit Score: 123.53  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285905149  2 PLWEVFIRSRTGQSHRHVGSLHAADAALALQAARDVYTRRGEGNSIWVVPAASITASDPAERGMLFEPAESKIYRHPTFY 81
Cdd:pfam06243  3 PLWEVFVRSKRGLPHQHVGSLHAPDAEMALQNARDVYTRRNEGVSIWVVPSSDITASDPEEKEPFFEPADDKVYRHPTFY 82


                 ....*.
gi 1285905149 82 TIPDDV 87
Cdd:pfam06243 83 GVPEEV 88
PA_CoA_Oxy2 TIGR02157
phenylacetate-CoA oxygenase, PaaH subunit; Phenylacetate-CoA oxygenase is comprised of a five ...
 2-90 1.15e-34

phenylacetate-CoA oxygenase, PaaH 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: 274002  Cd Length: 90  Bit Score: 113.80  E-value: 1.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285905149  2 PLWEVFIRSRTGQSHRHVGSLHAADAALALQAARDVYTRRGEGNSIWVVPAASITASDPAERGMLFEPAESKIYRHPTFY 81
Cdd:TIGR02157  2 PLYEVFVRSKSGLPHQHVGSLHAPDEEMALMMARDNYTRREEGVSIWVVKASHIVASTPDEREEFFDPAEDKVYRHPTFY 81


                 ....*....
gi 1285905149 82 TIPDDVGHM 90
Cdd:TIGR02157 82 GIPDRVWHM 90
 
Name Accession Description Interval E-value
PaaB COG3460
1,2-phenylacetyl-CoA epoxidase, PaaB subunit [Secondary metabolites biosynthesis, transport ...
 1-90 1.64e-39

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


Pssm-ID: 442683  Cd Length: 98  Bit Score: 126.22  E-value: 1.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285905149  1 MPLWEVFIRSRTGQSHRHVGSLHAADAALALQAARDVYTRRGEGNSIWVVPAASITASDPAERGMLFEPAESKIYRHPTF 80
Cdd:COG3460    9 WPLWEVFVRSKPGLPHRHVGSLHAPDAEMALQNARDVFTRREEGVSIWVVPSDAITASSPEEKDAFFDPAADKVYRHPTF 88

                         90
                 ....*....|
gi 1285905149 81 YTIPDDVGHM 90
Cdd:COG3460   89 YEVPEKVEHM 98
PaaB pfam06243
Phenylacetic acid degradation B; Phenylacetic acid degradation protein B (PaaB) is thought to ...
 2-87 1.18e-38

Phenylacetic acid degradation B; Phenylacetic acid degradation protein B (PaaB) is thought to be part of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation.


Pssm-ID: 428844  Cd Length: 88  Bit Score: 123.53  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285905149  2 PLWEVFIRSRTGQSHRHVGSLHAADAALALQAARDVYTRRGEGNSIWVVPAASITASDPAERGMLFEPAESKIYRHPTFY 81
Cdd:pfam06243  3 PLWEVFVRSKRGLPHQHVGSLHAPDAEMALQNARDVYTRRNEGVSIWVVPSSDITASDPEEKEPFFEPADDKVYRHPTFY 82


                 ....*.
gi 1285905149 82 TIPDDV 87
Cdd:pfam06243 83 GVPEEV 88
PA_CoA_Oxy2 TIGR02157
phenylacetate-CoA oxygenase, PaaH subunit; Phenylacetate-CoA oxygenase is comprised of a five ...
 2-90 1.15e-34

phenylacetate-CoA oxygenase, PaaH 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: 274002  Cd Length: 90  Bit Score: 113.80  E-value: 1.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285905149  2 PLWEVFIRSRTGQSHRHVGSLHAADAALALQAARDVYTRRGEGNSIWVVPAASITASDPAERGMLFEPAESKIYRHPTFY 81
Cdd:TIGR02157  2 PLYEVFVRSKSGLPHQHVGSLHAPDEEMALMMARDNYTRREEGVSIWVVKASHIVASTPDEREEFFDPAEDKVYRHPTFY 81


                 ....*....
gi 1285905149 82 TIPDDVGHM 90
Cdd:TIGR02157 82 GIPDRVWHM 90
Htur_1727_fam TIGR04031
rSAM-partnered protein, Htur_1727 family; Members of this protein family show homology to the ...
 4-56 3.57e-03

rSAM-partnered protein, Htur_1727 family; Members of this protein family show homology to the putative PaaH (or PaaB) subunit of the phenylacetate-CoA oxygenase complex. However, all members are found in the Halobacteriales in the vicinity of a radical SAM protein homologous to the PqqE protein of pyroquinoline quinone (PQQ) biosynthesis. Members are well-conserved to about residue 75, but then become low-complexity and hypervariable.


Pssm-ID: 188546  Cd Length: 71  Bit Score: 32.98  E-value: 3.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1285905149  4 WEVFIRSRTGQSHRHVGSLHAADAALALQAARDVYTRRGEgnSIWVVPAASIT 56
Cdd:TIGR04031 17 WELFVREDSEDPLTHVGSVSAPSADIAREQACSLFAWYAE--DLWVCPADDVT 67
 
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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