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Conserved domains on  [gi|446311793|ref|WP_000389648|]
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MULTISPECIES: 1,2-phenylacetyl-CoA epoxidase subunit PaaB [Acinetobacter]

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 ...
 2-96 3.41e-54

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


:

Pssm-ID: 442683  Cd Length: 98  Bit Score: 163.58  E-value: 3.41e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446311793  2 EDKNNWSLYEVFVRSKQGLSHRHVGSLRAPDDEIALQHARDVYTRRNEGISIWVVRSELIKSSQPDEKAEFFDPSLDKVY 81
Cdd:COG3460   4 ASATEWPLWEVFVRSKPGLPHRHVGSLHAPDAEMALQNARDVFTRREEGVSIWVVPSDAITASSPEEKDAFFDPAADKVY 83

                        90
                ....*....|....*
gi 446311793 82 RHPTFYHIPDGIEHM 96
Cdd:COG3460  84 RHPTFYEVPEKVEHM 98
 
Name Accession Description Interval E-value
PaaB COG3460
1,2-phenylacetyl-CoA epoxidase, PaaB subunit [Secondary metabolites biosynthesis, transport ...
 2-96 3.41e-54

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


Pssm-ID: 442683  Cd Length: 98  Bit Score: 163.58  E-value: 3.41e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446311793  2 EDKNNWSLYEVFVRSKQGLSHRHVGSLRAPDDEIALQHARDVYTRRNEGISIWVVRSELIKSSQPDEKAEFFDPSLDKVY 81
Cdd:COG3460   4 ASATEWPLWEVFVRSKPGLPHRHVGSLHAPDAEMALQNARDVFTRREEGVSIWVVPSDAITASSPEEKDAFFDPAADKVY 83

                        90
                ....*....|....*
gi 446311793 82 RHPTFYHIPDGIEHM 96
Cdd:COG3460  84 RHPTFYEVPEKVEHM 98
PaaB pfam06243
Phenylacetic acid degradation B; Phenylacetic acid degradation protein B (PaaB) is thought to ...
 6-93 1.09e-51

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: 156.65  E-value: 1.09e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446311793   6 NWSLYEVFVRSKQGLSHRHVGSLRAPDDEIALQHARDVYTRRNEGISIWVVRSELIKSSQPDEKAEFFDPSLDKVYRHPT 85
Cdd:pfam06243  1 EWPLWEVFVRSKRGLPHQHVGSLHAPDAEMALQNARDVYTRRNEGVSIWVVPSSDITASDPEEKEPFFEPADDKVYRHPT 80


                 ....*...
gi 446311793  86 FYHIPDGI 93
Cdd:pfam06243 81 FYGVPEEV 88
PA_CoA_Oxy2 TIGR02157
phenylacetate-CoA oxygenase, PaaH subunit; Phenylacetate-CoA oxygenase is comprised of a five ...
 7-96 5.40e-49

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: 150.01  E-value: 5.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446311793   7 WSLYEVFVRSKQGLSHRHVGSLRAPDDEIALQHARDVYTRRNEGISIWVVRSELIKSSQPDEKAEFFDPSLDKVYRHPTF 86
Cdd:TIGR02157  1 WPLYEVFVRSKSGLPHQHVGSLHAPDEEMALMMARDNYTRREEGVSIWVVKASHIVASTPDEREEFFDPAEDKVYRHPTF 80

                         90
                 ....*....|
gi 446311793  87 YHIPDGIEHM 96
Cdd:TIGR02157 81 YGIPDRVWHM 90
 
Name Accession Description Interval E-value
PaaB COG3460
1,2-phenylacetyl-CoA epoxidase, PaaB subunit [Secondary metabolites biosynthesis, transport ...
 2-96 3.41e-54

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


Pssm-ID: 442683  Cd Length: 98  Bit Score: 163.58  E-value: 3.41e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446311793  2 EDKNNWSLYEVFVRSKQGLSHRHVGSLRAPDDEIALQHARDVYTRRNEGISIWVVRSELIKSSQPDEKAEFFDPSLDKVY 81
Cdd:COG3460   4 ASATEWPLWEVFVRSKPGLPHRHVGSLHAPDAEMALQNARDVFTRREEGVSIWVVPSDAITASSPEEKDAFFDPAADKVY 83

                        90
                ....*....|....*
gi 446311793 82 RHPTFYHIPDGIEHM 96
Cdd:COG3460  84 RHPTFYEVPEKVEHM 98
PaaB pfam06243
Phenylacetic acid degradation B; Phenylacetic acid degradation protein B (PaaB) is thought to ...
 6-93 1.09e-51

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: 156.65  E-value: 1.09e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446311793   6 NWSLYEVFVRSKQGLSHRHVGSLRAPDDEIALQHARDVYTRRNEGISIWVVRSELIKSSQPDEKAEFFDPSLDKVYRHPT 85
Cdd:pfam06243  1 EWPLWEVFVRSKRGLPHQHVGSLHAPDAEMALQNARDVYTRRNEGVSIWVVPSSDITASDPEEKEPFFEPADDKVYRHPT 80


                 ....*...
gi 446311793  86 FYHIPDGI 93
Cdd:pfam06243 81 FYGVPEEV 88
PA_CoA_Oxy2 TIGR02157
phenylacetate-CoA oxygenase, PaaH subunit; Phenylacetate-CoA oxygenase is comprised of a five ...
 7-96 5.40e-49

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: 150.01  E-value: 5.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446311793   7 WSLYEVFVRSKQGLSHRHVGSLRAPDDEIALQHARDVYTRRNEGISIWVVRSELIKSSQPDEKAEFFDPSLDKVYRHPTF 86
Cdd:TIGR02157  1 WPLYEVFVRSKSGLPHQHVGSLHAPDEEMALMMARDNYTRREEGVSIWVVKASHIVASTPDEREEFFDPAEDKVYRHPTF 80

                         90
                 ....*....|
gi 446311793  87 YHIPDGIEHM 96
Cdd:TIGR02157 81 YGIPDRVWHM 90
Htur_1727_fam TIGR04031
rSAM-partnered protein, Htur_1727 family; Members of this protein family show homology to the ...
 10-59 7.72e-07

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: 42.61  E-value: 7.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446311793  10 YEVFVRSKQGLSHRHVGSLRAPDDEIALQHARDVYTRRNEgiSIWVVRSE 59
Cdd:TIGR04031 17 WELFVREDSEDPLTHVGSVSAPSADIAREQACSLFAWYAE--DLWVCPAD 64
 
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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