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Conserved domains on  [gi|654762029|ref|WP_028216855|]
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2-hydroxychromene-2-carboxylate isomerase [Paraburkholderia oxyphila]

Protein Classification

2-hydroxychromene-2-carboxylate isomerase( domain architecture ID 10790476)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
6-207 5.02e-78

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


:

Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 231.98  E-value: 5.02e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   6 VQFLFDFGSPNAYLSHKVIPAIEARQGVRFEYVPILLGGLFKLTGNRSPAEttaHIENKRKYMMLEMQRFVDKHGLAaYR 85
Cdd:COG3917    2 IDFYFDFSSPYAYLAATRLEALAARHGAEVRWRPVLLGAVFKATGGTPPAE---RIPAKGRYRLRDLARWARKLGLP-FR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  86 MNPHFPVNTLQLMRGAVAAQREGvdgLFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTLL 165
Cdd:COG3917   78 FPPHFPVNPLLAARAALAAQDAG---AAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAALLAAAQSPAVKARLR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 654762029 166 ANTQAAFERGAFGAPTFFVGEEMFFGKDRLRDVEEEIARAKA 207
Cdd:COG3917  155 ANTEEAVARGVFGAPTFVVDGELFWGQDRLDFLEAALAGGGA 196
 
Name Accession Description Interval E-value
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
6-207 5.02e-78

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


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 231.98  E-value: 5.02e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   6 VQFLFDFGSPNAYLSHKVIPAIEARQGVRFEYVPILLGGLFKLTGNRSPAEttaHIENKRKYMMLEMQRFVDKHGLAaYR 85
Cdd:COG3917    2 IDFYFDFSSPYAYLAATRLEALAARHGAEVRWRPVLLGAVFKATGGTPPAE---RIPAKGRYRLRDLARWARKLGLP-FR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  86 MNPHFPVNTLQLMRGAVAAQREGvdgLFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTLL 165
Cdd:COG3917   78 FPPHFPVNPLLAARAALAAQDAG---AAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAALLAAAQSPAVKARLR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 654762029 166 ANTQAAFERGAFGAPTFFVGEEMFFGKDRLRDVEEEIARAKA 207
Cdd:COG3917  155 ANTEEAVARGVFGAPTFVVDGELFWGQDRLDFLEAALAGGGA 196
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
6-203 4.01e-75

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: 224.43  E-value: 4.01e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   6 VQFLFDFGSPNAYLSHKVIPAIEARQGVRFEYVPILLGGLFKLTGNRSPAETTAhieNKRKYMMLEMQRFVDKHGLAaYR 85
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRPP---AKGRYRLRDLERWARRYGIP-LR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  86 MNPHFPVNTLQLMRGAVAAQREGVDglFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTLL 165
Cdd:cd03022   77 FPPRFPPNTLRAMRAALAAQAEGDA--AEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALR 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 654762029 166 ANTQAAFERGAFGAPTFFVGEEMFFGKDRLRDVEEEIA 203
Cdd:cd03022  155 ANTEEAIARGVFGVPTFVVDGEMFWGQDRLDMLEEALA 192
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
6-203 5.15e-34

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: 119.84  E-value: 5.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029    6 VQFLFDFGSPNAYLSHKVIPAIEAR-QGVRFEYVPILLGGLfKLTGNRSPAETTAhienKRKYMMLEMQRFVDKHGLAaY 84
Cdd:pfam01323   2 VDEFFDFLCPFCYLAKERLEKLAARyGDVKVVYRPFPLAGA-KKIGNVGPSNLPV----KLKYMMADLERWAALYGIP-L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   85 RMNPHFPVNTLQLMRGAVAAQREGvdgLFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTL 164
Cdd:pfam01323  76 RFPANFLGNSTRANRLALAAGAEG---LAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAV 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 654762029  165 LANTQAAFERGAFGAPTFFVGEEMFFGKDRLRDVEEEIA 203
Cdd:pfam01323 153 RENTAAAISLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
 
Name Accession Description Interval E-value
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
6-207 5.02e-78

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


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 231.98  E-value: 5.02e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   6 VQFLFDFGSPNAYLSHKVIPAIEARQGVRFEYVPILLGGLFKLTGNRSPAEttaHIENKRKYMMLEMQRFVDKHGLAaYR 85
Cdd:COG3917    2 IDFYFDFSSPYAYLAATRLEALAARHGAEVRWRPVLLGAVFKATGGTPPAE---RIPAKGRYRLRDLARWARKLGLP-FR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  86 MNPHFPVNTLQLMRGAVAAQREGvdgLFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTLL 165
Cdd:COG3917   78 FPPHFPVNPLLAARAALAAQDAG---AAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAALLAAAQSPAVKARLR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 654762029 166 ANTQAAFERGAFGAPTFFVGEEMFFGKDRLRDVEEEIARAKA 207
Cdd:COG3917  155 ANTEEAVARGVFGAPTFVVDGELFWGQDRLDFLEAALAGGGA 196
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
6-203 4.01e-75

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: 224.43  E-value: 4.01e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   6 VQFLFDFGSPNAYLSHKVIPAIEARQGVRFEYVPILLGGLFKLTGNRSPAETTAhieNKRKYMMLEMQRFVDKHGLAaYR 85
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRPP---AKGRYRLRDLERWARRYGIP-LR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  86 MNPHFPVNTLQLMRGAVAAQREGVDglFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTLL 165
Cdd:cd03022   77 FPPRFPPNTLRAMRAALAAQAEGDA--AEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALR 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 654762029 166 ANTQAAFERGAFGAPTFFVGEEMFFGKDRLRDVEEEIA 203
Cdd:cd03022  155 ANTEEAIARGVFGVPTFVVDGEMFWGQDRLDMLEEALA 192
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
6-203 5.15e-34

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: 119.84  E-value: 5.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029    6 VQFLFDFGSPNAYLSHKVIPAIEAR-QGVRFEYVPILLGGLfKLTGNRSPAETTAhienKRKYMMLEMQRFVDKHGLAaY 84
Cdd:pfam01323   2 VDEFFDFLCPFCYLAKERLEKLAARyGDVKVVYRPFPLAGA-KKIGNVGPSNLPV----KLKYMMADLERWAALYGIP-L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   85 RMNPHFPVNTLQLMRGAVAAQREGvdgLFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTL 164
Cdd:pfam01323  76 RFPANFLGNSTRANRLALAAGAEG---LAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAV 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 654762029  165 LANTQAAFERGAFGAPTFFVGEEMFFGKDRLRDVEEEIA 203
Cdd:pfam01323 153 RENTAAAISLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
5-195 7.39e-27

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: 101.66  E-value: 7.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   5 KVQFLFDFGSPNAYLSHKVIPAIEARQGVRFEYVPILLGGLFKLTGNRSPAEttahIENKRKYMMLEMQRfVDKHGLAAY 84
Cdd:cd03021    2 KIELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIM----LPNKAKYMAKDRKR-SAEFFGVPI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  85 RMNPHF---PVNTLQLMRGAVAAQREGVDGlFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGfDVARFEA-------- 153
Cdd:cd03021   77 RQPKDFffmKKGTLTAQRFLTAISEQHPES-TLTALEALFREFWVRPWSLTEPITESQSISVAA-DKLGGSAeqaekllk 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 654762029 154 ALGDADVKGTLLANTQAAFERGAFGAPTFFV----GE-EMFFGKDRL 195
Cdd:cd03021  155 AASTPEVKNRLKENTDEALKYGAFGLPWIVVtndkGKtEMFFGSDRF 201
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
3-186 3.06e-15

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: 71.07  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   3 TVKVQFLFDFGSPNAYLSHKVI-PAIEARQG-VRFEYVPI-LLGGLFKLTGNRSPAETTAHIENKRKYMMLEMQRFVDKH 79
Cdd:COG2761    1 PLKIDIFSDVVCPWCYIGKRRLeKALAEFGDdVEIRWRPFeLNPDMPPEGEDRREYLLAKGSPEQAEQMRAHVEEAAAEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  80 GLAaYRMNPHFPVNTLQLMRGAVAAQREGvdgLFERYVDRMFAHMWEDGLKLDDPQVLRATLEADGFDVARFEAALGDAD 159
Cdd:COG2761   81 GLP-FDFDRIKPPNTFDAHRLLKAAELQG---KQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDE 156
                        170       180
                 ....*....|....*....|....*..
gi 654762029 160 VKGTLLANTQAAFERGAFGAPTFFVGE 186
Cdd:COG2761  157 AAAAVRADEAEARELGVTGVPTFVFDG 183
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
89-206 7.19e-10

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 55.39  E-value: 7.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  89 HFPV---NTLQLMRGAVAAQREGVdglFERYVDRMFAHmwEDGLkldDPQVLRATLEADGFDVARFEAALGDADVKGTLL 165
Cdd:COG1651   40 PFPLlhpDSLRAARAALCAADQGK---FWAFHDALFAN--QPAL---TDDDLREIAKEAGLDAAKFDACLNSGAVAAKVE 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 654762029 166 ANTQAAFERGAFGAPTFFVGEEMFFGKDRLRDVEEEIARAK 206
Cdd:COG1651  112 ADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
54-185 1.23e-07

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: 49.89  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  54 PAETTAHIEN-KRKY--------MMLEMQRFVDKHGLAaYRMNPHFPVNTLQLMRGAVAAQREGvdgLFERYVDRMFAHM 124
Cdd:cd03024   46 PPEGEDRREYlARKYgstaeqaaAMRRVEAAAAAEGLE-FDFDRVRPPNTFDAHRLIHLAKEQG---KQDALVEALFRAY 121
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654762029 125 WEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTLLANTQAAFERGAFGAPTFFVG 185
Cdd:cd03024  122 FTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADEVRADEARARQLGISGVPFFVFN 182
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
99-198 4.46e-05

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: 42.20  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  99 RGAVAAQREGVDGlFERYVDRMFAHmwedGLKLDDPQVLRATLEAdGFDVARFEAALGDADVKGTLLANTQAAFERGAFG 178
Cdd:cd03023   56 RVALAVWKNGPGK-YLEFHNALMAT----RGRLNEESLLRIAKKA-GLDEAKLKKDMDDPEIEATIDKNRQLARALGITG 129
                         90       100
                 ....*....|....*....|...
gi 654762029 179 APTFFVGEEMFFG---KDRLRDV 198
Cdd:cd03023  130 TPAFIIGDTVIPGavpADTLKEA 152
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
23-187 1.27e-04

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 41.39  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  23 VIPAIEARQGVRFEyVPILLGGLFklTGNRSPAETTAhienKRKYMMLEMQRFVDKHGL---AAYR---MNPHFPVNTLQ 96
Cdd:COG3531   21 VIEALAEALGDRLD-VELLSGGLF--PGSNRRPMDPE----MRAYIQPHWQRIAQLTGQpfgEAYNdllRDGTFVLDSEP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  97 LMRGAVAAQREGVDGLFErYVDRM-FAHmWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKgtllANTQAAFER- 174
Cdd:COG3531   94 ACRAVLAARELAPERELA-MLHAIqRAF-YVEGRDISDPEVLAELAAELGLDAEAFAAALASEETR----QHIQQEFALa 167
                        170
                 ....*....|....*.
gi 654762029 175 ---GAFGAPTFFVGEE 187
Cdd:COG3531  168 rqlGVQGFPTLVLEQG 183
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
6-193 3.61e-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: 38.54  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029   6 VQFLFDFGSPNAYLSHKVIPAI--EARQGVRFEYVPILLgglfkltgnrspaettahienkrkymmlemqrfvdkhglaa 83
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLlyADDGGVRVVYRPFPL----------------------------------------- 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  84 yrmNPHFPVNTLQLMRGAVAAQREGvdgLFERYVDRmfahmwedglklddpqvlratleadgfdvarfeaalgdadvkgt 163
Cdd:cd02972   40 ---LGGMPPNSLAAARAALAAAAQG---KFEALHEA-------------------------------------------- 69
                        170       180       190
                 ....*....|....*....|....*....|
gi 654762029 164 lLANTQAAFERGAFGAPTFFVGEEMFFGKD 193
Cdd:cd02972   70 -LADTALARALGVTGTPTFVVNGEKYSGAG 98
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
26-184 1.57e-03

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: 38.07  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029  26 AIEARQGVRFEYVPillGGLfkLTGNRSPAETT----AHIENKRKYMMLEMQRFVDkhglaaYRMNPHFPVNTLQLMRGA 101
Cdd:cd03025   25 KEEYGGGIEVELHL---GGL--LPGNNARQITKqwriYVHWHKARIALTGQPFGED------YLELLLFDLDSAPASRAI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654762029 102 VAAQREGVDGLFErYVDRM-FAHmWEDGLKLDDPQVLRATLEADGFDVARFEAALGDADVKGTLLANTQAAFERGAFGAP 180
Cdd:cd03025   94 KAARLQGPERLLE-MLKAIqRAH-YVEGRDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAIQEDQKLARELGINGFP 171

                 ....
gi 654762029 181 TFFV 184
Cdd:cd03025  172 TLVL 175
 
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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