NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15595316|ref|NP_248808|]
View 

hypothetical protein PA0118 [Pseudomonas aeruginosa PAO1]

Protein Classification

2-hydroxychromene-2-carboxylate isomerase( domain architecture ID 10122490)

2-hydroxychromene-2-carboxylate isomerase catalyzes the reversible glutathione-dependent isomerization of 2-hydroxychromene-2-carboxylate (HCCA) to trans-O-hydroxybenzylidenepyruvate (THBPA) in the naphthalene catabolic pathway

EC:  5.99.1.4
Gene Ontology:  GO:0018845|GO:1901170|GO:0043295
PubMed:  17508726

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 5-194 6.80e-91

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


:

Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 264.10  E-value: 6.80e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   5 IEFFFDFGSPTTYLAWTQLPRIAAAHGASIAWRPMLLGGVFKATGNHSPIEVP-AKGRYTLHDLARYAKRYGVPLAFNPA 83
Cdd:cd03022   1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRPpAKGRYRLRDLERWARRYGIPLRFPPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  84 FPINTLTLMRGAQGY-LGGEGFQPYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEA 162
Cdd:cd03022  81 FPPNTLRAMRAALAAqAEGDAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALRANTEEA 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 15595316 163 VRRGVFGAPSFFVGDQLFFGQDRLDFVAEVLA 194
Cdd:cd03022 161 IARGVFGVPTFVVDGEMFWGQDRLDMLEEALA 192
 
Name Accession Description Interval E-value
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 5-194 6.80e-91

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 264.10  E-value: 6.80e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   5 IEFFFDFGSPTTYLAWTQLPRIAAAHGASIAWRPMLLGGVFKATGNHSPIEVP-AKGRYTLHDLARYAKRYGVPLAFNPA 83
Cdd:cd03022   1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRPpAKGRYRLRDLERWARRYGIPLRFPPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  84 FPINTLTLMRGAQGY-LGGEGFQPYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEA 162
Cdd:cd03022  81 FPPNTLRAMRAALAAqAEGDAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALRANTEEA 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 15595316 163 VRRGVFGAPSFFVGDQLFFGQDRLDFVAEVLA 194
Cdd:cd03022 161 IARGVFGVPTFVVDGEMFWGQDRLDMLEEALA 192
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
 4-195 2.27e-87

2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 255.10  E-value: 2.27e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   4 QIEFFFDFGSPTTYLAWTQLPRIAAAHGASIAWRPMLLGGVFKATGNHSPIE-VPAKGRYTLHDLARYAKRYGVPLAFNP 82
Cdd:COG3917   1 TIDFYFDFSSPYAYLAATRLEALAARHGAEVRWRPVLLGAVFKATGGTPPAErIPAKGRYRLRDLARWARKLGLPFRFPP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  83 AFPINTLTLMRGAQGYLGGEGFQPYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEA 162
Cdd:COG3917  81 HFPVNPLLAARAALAAQDAGAAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAALLAAAQSPAVKARLRANTEEA 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 15595316 163 VRRGVFGAPSFFVGDQLFFGQDRLDFVAEVLAG 195
Cdd:COG3917 161 VARGVFGAPTFVVDGELFWGQDRLDFLEAALAG 193
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 4-194 1.41e-48

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 156.43  E-value: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316     4 QIEFFFDFGSPTTYLAWTQLPRIAAAHG-ASIAWRPMLLGGVfKATGNHSPIEVPAKGRYTLHDLARYAKRYGVPLAFNP 82
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGdVKVVYRPFPLAGA-KKIGNVGPSNLPVKLKYMMADLERWAALYGIPLRFPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316    83 AFPINTLTLMRGAQgYLGGEGFQP-YLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEE 161
Cdd:pfam01323  80 NFLGNSTRANRLAL-AAGAEGLAEkVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTAA 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 15595316   162 AVRRGVFGAPSFFVGDQLFFGQDRLDFVAEVLA 194
Cdd:pfam01323 159 AISLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
 
Name Accession Description Interval E-value
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 5-194 6.80e-91

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 264.10  E-value: 6.80e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   5 IEFFFDFGSPTTYLAWTQLPRIAAAHGASIAWRPMLLGGVFKATGNHSPIEVP-AKGRYTLHDLARYAKRYGVPLAFNPA 83
Cdd:cd03022   1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRPpAKGRYRLRDLERWARRYGIPLRFPPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  84 FPINTLTLMRGAQGY-LGGEGFQPYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEA 162
Cdd:cd03022  81 FPPNTLRAMRAALAAqAEGDAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALRANTEEA 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 15595316 163 VRRGVFGAPSFFVGDQLFFGQDRLDFVAEVLA 194
Cdd:cd03022 161 IARGVFGVPTFVVDGEMFWGQDRLDMLEEALA 192
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
 4-195 2.27e-87

2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 255.10  E-value: 2.27e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   4 QIEFFFDFGSPTTYLAWTQLPRIAAAHGASIAWRPMLLGGVFKATGNHSPIE-VPAKGRYTLHDLARYAKRYGVPLAFNP 82
Cdd:COG3917   1 TIDFYFDFSSPYAYLAATRLEALAARHGAEVRWRPVLLGAVFKATGGTPPAErIPAKGRYRLRDLARWARKLGLPFRFPP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  83 AFPINTLTLMRGAQGYLGGEGFQPYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEA 162
Cdd:COG3917  81 HFPVNPLLAARAALAAQDAGAAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAALLAAAQSPAVKARLRANTEEA 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 15595316 163 VRRGVFGAPSFFVGDQLFFGQDRLDFVAEVLAG 195
Cdd:COG3917 161 VARGVFGAPTFVVDGELFWGQDRLDFLEAALAG 193
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 4-194 1.41e-48

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 156.43  E-value: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316     4 QIEFFFDFGSPTTYLAWTQLPRIAAAHG-ASIAWRPMLLGGVfKATGNHSPIEVPAKGRYTLHDLARYAKRYGVPLAFNP 82
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGdVKVVYRPFPLAGA-KKIGNVGPSNLPVKLKYMMADLERWAALYGIPLRFPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316    83 AFPINTLTLMRGAQgYLGGEGFQP-YLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEE 161
Cdd:pfam01323  80 NFLGNSTRANRLAL-AAGAEGLAEkVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTAA 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 15595316   162 AVRRGVFGAPSFFVGDQLFFGQDRLDFVAEVLA 194
Cdd:pfam01323 159 AISLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
 3-194 1.02e-46

DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the GST family of enzymes which catalyzes the transfer of the thiol of GSH to electrophilic substrates. It is specifically located in the mitochondria and peroxisomes, unlike other members of the canonical GST family, which are mainly cytosolic. The biological substrates of GSTK are not yet known. It is presumed to have a protective role during respiration when large amounts of reactive oxygen species are generated. GSTK has the same general fold as DsbA, consisting of a thioredoxin domain interrupted by an alpha-helical domain and its biological unit is a homodimer. GSTK is closely related to the bacterial enzyme, 2-hydroxychromene-2-carboxylate (HCCA) isomerase. It shows little sequence similarity to the other members of the GST family.


Pssm-ID: 239319 [Multi-domain]  Cd Length: 209  Bit Score: 152.51  E-value: 1.02e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   3 KQIEFFFDFGSPTTYLAWTQLPRIAAAHGASIAWRPMLLGGVFKATGNHSPIEVPAKGRYTLHDLARYAKRYGVPLAFNP 82
Cdd:cd03021   1 PKIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIMLPNKAKYMAKDRKRSAEFFGVPIRQPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  83 AF---PINTLTLMRgaqgYLGG------EGFQPYLKAVFEALWVRQQNLGKPEVVAQVLAEAGF-------DPDEFLRLV 146
Cdd:cd03021  81 DFffmKKGTLTAQR----FLTAiseqhpESTLTALEALFREFWVRPWSLTEPITESQSISVAADklggsaeQAEKLLKAA 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15595316 147 GDEQVKEGLKATTEEAVRRGVFGAPSFFVGD-----QLFFGQDRLDFVAEVLA 194
Cdd:cd03021 157 STPEVKNRLKENTDEALKYGAFGLPWIVVTNdkgktEMFFGSDRFEQVADFLG 209
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 4-179 1.81e-23

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 92.25  E-value: 1.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   4 QIEFFFDFGSPTTYLAWTQLPRIAAAHG--ASIAWRPMLLGGVFKATGNHSPIEVPAKG-----RYTLHDLARYAKRYGV 76
Cdd:COG2761   3 KIDIFSDVVCPWCYIGKRRLEKALAEFGddVEIRWRPFELNPDMPPEGEDRREYLLAKGspeqaEQMRAHVEEAAAEEGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  77 PLAFNPAFPINTLTLMRGAQgYLGGEGFQ-PYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGL 155
Cdd:COG2761  83 PFDFDRIKPPNTFDAHRLLK-AAELQGKQdALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAAAAV 161

                       170       180
                ....*....|....*....|....
gi 15595316 156 KATTEEAVRRGVFGAPSFFVGDQL 179
Cdd:COG2761 162 RADEAEARELGVTGVPTFVFDGKY 185
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 5-178 1.77e-12

DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239322 [Multi-domain]  Cd Length: 201  Bit Score: 62.98  E-value: 1.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   5 IEFFFDFGSPTTYLAWTQLPRIAAAHGASIA----WRPMLLGGVFKATGnhspieVPAKGRYT------------LHDLA 68
Cdd:cd03024   1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDveieWRPFELNPDMPPEG------EDRREYLArkygstaeqaaaMRRVE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  69 RYAKRYGVPLAFNPAFPINTLTLMRGAQgYLGGEGFQ-PYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVG 147
Cdd:cd03024  75 AAAAAEGLEFDFDRVRPPNTFDAHRLIH-LAKEQGKQdALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLA 153

                       170       180       190
                ....*....|....*....|....*....|.
gi 15595316 148 DEQVKEGLKATTEEAVRRGVFGAPSFFVGDQ 178
Cdd:cd03024 154 SDEYADEVRADEARARQLGISGVPFFVFNGK 184
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 104-194 9.59e-10

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 54.62  E-value: 9.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316 104 FQPYLKAVFEAlwvrQQNLGkPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEAVRRGVFGAPSFFVGDQLFFGQ 183
Cdd:COG1651  64 FWAFHDALFAN----QPALT-DDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGA 138

                        90
                ....*....|.
gi 15595316 184 DRLDFVAEVLA 194
Cdd:COG1651 139 VPYEELEAALD 149
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
 25-180 4.87e-08

Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 51.02  E-value: 4.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  25 RIAAAHGASIAWRpMLLGGVFkATGNHSPIEvPAKGRYTLHDLARYAKRYGVPlaFNPA---------FPINTLTLMRG- 94
Cdd:COG3531  24 ALAEALGDRLDVE-LLSGGLF-PGSNRRPMD-PEMRAYIQPHWQRIAQLTGQP--FGEAyndllrdgtFVLDSEPACRAv 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  95 --AQGYLGGEGFqPYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEAVRRGVFGAPS 172
Cdd:COG3531  99 laARELAPEREL-AMLHAIQRAFYVEGRDISDPEVLAELAAELGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPT 177

                       170
                ....*....|
gi 15595316 173 FFV--GDQLF 180
Cdd:COG3531 178 LVLeqGGQLY 187
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 110-176 3.72e-04

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 39.58  E-value: 3.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595316 110 AVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEAVRRGVFGAPSFFVG 176
Cdd:cd03019  84 ALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVN 150
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 105-178 6.47e-04

DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239323 [Multi-domain]  Cd Length: 193  Bit Score: 38.84  E-value: 6.47e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595316 105 QPYLKAVFEALWVRQQNLGKPEVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEAVRRGVFGAPSFFVGDQ 178
Cdd:cd03025 105 LEMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAIQEDQKLARELGINGFPTLVLEDD 178
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 5-184 8.47e-04

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 37.39  E-value: 8.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316   5 IEFFFDFGSPTTYLAWTQLPRI--AAAHGASIAWRPMLLGGVFkatgnhspievpakgrytlhdlaryakrygvplafnp 82
Cdd:cd02972   1 IVEFFDPLCPYCYLFEPELEKLlyADDGGVRVVYRPFPLLGGM------------------------------------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595316  83 afPINTLTLMRGAqgylggegfqpylkavfeaLWVRQQNlgkpevvaqvlaeagfDPDEFLRLVGDEQvkeglkatteEA 162
Cdd:cd02972  44 --PPNSLAAARAA-------------------LAAAAQG----------------KFEALHEALADTA----------LA 76

                       170       180
                ....*....|....*....|..
gi 15595316 163 VRRGVFGAPSFFVGDQLFFGQD 184
Cdd:cd02972  77 RALGVTGTPTFVVNGEKYSGAG 98
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 126-182 1.98e-03

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 37.19  E-value: 1.98e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15595316 126 EVVAQVLAEAGFDPDEFLRLVGDEQVKEGLKATTEEAVRRGVFGAPSFFVGDQLFFG 182
Cdd:cd03023  86 ESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPG 142
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH