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Conserved domains on  [gi|654680519|ref|WP_028139343|]
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MULTISPECIES: 2-hydroxychromene-2-carboxylate isomerase [Bradyrhizobium]

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

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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 ...
 6-199 6.99e-78

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: 231.36  E-value: 6.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519   6 PQFLFDFGSPNAYLSHLAIPAIEQRIGVKFEYMPILLGGIFKSTNNKSPAETLagiKNKREFHQVETERFIKRFHVqPYV 85
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRP---PAKGRYRLRDLERWARRYGI-PLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  86 WNPHFPINTLNLMRTAIAAQLEGV-FEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKN 164
Cdd:cd03022   77 FPPRFPPNTLRAMRAALAAQAEGDaAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALRAN 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 654680519 165 TEDAVARGAFGSPTFFVGNEMFFGKEQLREVEEMV 199
Cdd:cd03022  157 TEEAIARGVFGVPTFVVDGEMFWGQDRLDMLEEAL 191
 
Name Accession Description Interval E-value
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 6-199 6.99e-78

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: 231.36  E-value: 6.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519   6 PQFLFDFGSPNAYLSHLAIPAIEQRIGVKFEYMPILLGGIFKSTNNKSPAETLagiKNKREFHQVETERFIKRFHVqPYV 85
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRP---PAKGRYRLRDLERWARRYGI-PLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  86 WNPHFPINTLNLMRTAIAAQLEGV-FEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKN 164
Cdd:cd03022   77 FPPRFPPNTLRAMRAALAAQAEGDaAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALRAN 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 654680519 165 TEDAVARGAFGSPTFFVGNEMFFGKEQLREVEEMV 199
Cdd:cd03022  157 TEEAIARGVFGVPTFVVDGEMFWGQDRLDMLEEAL 191
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
 5-201 1.61e-75

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


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 225.44  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519   5 TPQFLFDFGSPNAYLSHLAIPAIEQRIGVKFEYMPILLGGIFKSTNNKSPAETlagIKNKREFHQVETERFIKRFHVqPY 84
Cdd:COG3917    1 TIDFYFDFSSPYAYLAATRLEALAARHGAEVRWRPVLLGAVFKATGGTPPAER---IPAKGRYRLRDLARWARKLGL-PF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  85 VWNPHFPINTLNLMRTAIAAQLEGVFEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKN 164
Cdd:COG3917   77 RFPPHFPVNPLLAARAALAAQDAGAAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAALLAAAQSPAVKARLRAN 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 654680519 165 TEDAVARGAFGSPTFFVGNEMFFGKEQLREVEEMVLG 201
Cdd:COG3917  157 TEEAVARGVFGAPTFVVDGELFWGQDRLDFLEAALAG 193
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 8-188 3.59e-29

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: 107.13  E-value: 3.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519    8 FLFDFGSPNAYLSHLAIPAIEQRIG-VKFEYMPILLGGIfKSTNNKSPAETLAGIKnkrefHQVETERFIKRFHVQPYVW 86
Cdd:pfam01323   4 EFFDFLCPFCYLAKERLEKLAARYGdVKVVYRPFPLAGA-KKIGNVGPSNLPVKLK-----YMMADLERWAALYGIPLRF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519   87 NPHFPINTLNLMRTAIAAQLEGVFEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKNTE 166
Cdd:pfam01323  78 PANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTA 157

                         170       180
                  ....*....|....*....|..
gi 654680519  167 DAVARGAFGSPTFFVGNEMFFG 188
Cdd:pfam01323 158 AAISLGVFGVPTFVVGGKMVFG 179
 
Name Accession Description Interval E-value
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 6-199 6.99e-78

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: 231.36  E-value: 6.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519   6 PQFLFDFGSPNAYLSHLAIPAIEQRIGVKFEYMPILLGGIFKSTNNKSPAETLagiKNKREFHQVETERFIKRFHVqPYV 85
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNVPPANRP---PAKGRYRLRDLERWARRYGI-PLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  86 WNPHFPINTLNLMRTAIAAQLEGV-FEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKN 164
Cdd:cd03022   77 FPPRFPPNTLRAMRAALAAQAEGDaAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALRAN 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 654680519 165 TEDAVARGAFGSPTFFVGNEMFFGKEQLREVEEMV 199
Cdd:cd03022  157 TEEAIARGVFGVPTFVVDGEMFWGQDRLDMLEEAL 191
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
 5-201 1.61e-75

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


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 225.44  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519   5 TPQFLFDFGSPNAYLSHLAIPAIEQRIGVKFEYMPILLGGIFKSTNNKSPAETlagIKNKREFHQVETERFIKRFHVqPY 84
Cdd:COG3917    1 TIDFYFDFSSPYAYLAATRLEALAARHGAEVRWRPVLLGAVFKATGGTPPAER---IPAKGRYRLRDLARWARKLGL-PF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  85 VWNPHFPINTLNLMRTAIAAQLEGVFEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKN 164
Cdd:COG3917   77 RFPPHFPVNPLLAARAALAAQDAGAAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAALLAAAQSPAVKARLRAN 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 654680519 165 TEDAVARGAFGSPTFFVGNEMFFGKEQLREVEEMVLG 201
Cdd:COG3917  157 TEEAVARGVFGAPTFVVDGELFWGQDRLDFLEAALAG 193
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 8-188 3.59e-29

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: 107.13  E-value: 3.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519    8 FLFDFGSPNAYLSHLAIPAIEQRIG-VKFEYMPILLGGIfKSTNNKSPAETLAGIKnkrefHQVETERFIKRFHVQPYVW 86
Cdd:pfam01323   4 EFFDFLCPFCYLAKERLEKLAARYGdVKVVYRPFPLAGA-KKIGNVGPSNLPVKLK-----YMMADLERWAALYGIPLRF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519   87 NPHFPINTLNLMRTAIAAQLEGVFEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKNTE 166
Cdd:pfam01323  78 PANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTA 157

                         170       180
                  ....*....|....*....|..
gi 654680519  167 DAVARGAFGSPTFFVGNEMFFG 188
Cdd:pfam01323 158 AAISLGVFGVPTFVVGGKMVFG 179
DsbA_GSTK cd03021
DsbA family, Glutathione (GSH) S-transferase Kappa (GSTK) subfamily; GSTK is a member of the ...
 7-195 4.82e-28

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: 104.74  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519   7 QFLFDFGSPNAYLSHLAIPAIEQRIGVKFEYMPILLGGIFKSTNNKSPAEtlagIKNKREFHQVETERFIKRFHVqPYVW 86
Cdd:cd03021    4 ELYYDVVSPYSYLAFEVLCRYQTAWNVDITYVPVFLGGIMKDSGNKPPIM----LPNKAKYMAKDRKRSAEFFGV-PIRQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  87 NPHF---PINTLNLMR--TAIAAQLEGVFEKYVEAAFHHMWREPKKMDDPE-------IAVKALASSGLDAQKLFARSQE 154
Cdd:cd03021   79 PKDFffmKKGTLTAQRflTAISEQHPESTLTALEALFREFWVRPWSLTEPItesqsisVAADKLGGSAEQAEKLLKAAST 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 654680519 155 PEVKGRLIKNTEDAVARGAFGSPTFFVGN-----EMFFGKEQLREV 195
Cdd:cd03021  159 PEVKNRLKENTDEALKYGAFGLPWIVVTNdkgktEMFFGSDRFEQV 204
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 83-183 1.00e-10

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: 58.36  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  83 PYVWNPHFPINTLNLMRTAIAAQLEGVFEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLI 162
Cdd:COG2761   83 PFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAAAAVR 162

                         90       100
                 ....*....|....*....|.
gi 654680519 163 KNTEDAVARGAFGSPTFFVGN 183
Cdd:COG2761  163 ADEAEARELGVTGVPTFVFDG 183
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 89-195 5.98e-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: 5.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  89 HFPI---NTLNLMRTAIAAQLEGVFEKYVEAafhhMWREPKKMDDPEIAvKALASSGLDAQKLFARSQEPEVKGRLIKNT 165
Cdd:COG1651   40 PFPLlhpDSLRAARAALCAADQGKFWAFHDA----LFANQPALTDDDLR-EIAKEAGLDAAKFDACLNSGAVAAKVEADT 114

                         90       100       110
                 ....*....|....*....|....*....|...
gi 654680519 166 EDAVARGAFGSPTFFVGNEMFFG---KEQLREV 195
Cdd:COG1651  115 ALAQALGVTGTPTFVVNGKLVSGavpYEELEAA 147
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 90-195 8.13e-09

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: 52.21  E-value: 8.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  90 FPI---NTLNLMRTAIAAQLEGVfEKYVEaaFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKNTE 166
Cdd:cd03023   44 FPIlgeSSVLAARVALAVWKNGP-GKYLE--FHNALMATRGRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQ 120

                         90       100       110
                 ....*....|....*....|....*....|..
gi 654680519 167 DAVARGAFGSPTFFVGNEMFFG---KEQLREV 195
Cdd:cd03023  121 LARALGITGTPAFIIGDTVIPGavpADTLKEA 152
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 76-199 7.46e-06

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: 44.59  E-value: 7.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  76 IKRFHVqpyVWNPHFPINtlnLMRTAIAAQLEGVFEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEP 155
Cdd:cd03019   50 FEKVPV---VFGGGEGEP---LARAFYAAEALGLEDKLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSF 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 654680519 156 EVKGRLIKNTEDAVARGAFGSPTFFVG------NEMFFGKEQLREVEEMV 199
Cdd:cd03019  124 SVKALVAKAEKLAKKYKITGVPAFVVNgkyvvnPSAIGGDDTLQVLDELI 173
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 91-183 1.52e-03

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: 37.94  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654680519  91 PINTLNLMRTAIAAQLEGVFEKYVEAAFHHMWREPKKMDDPEIAVKALASSGLDAQKLFARSQEPEVKGRLIKNTEDAVA 170
Cdd:cd03024   91 PPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADEVRADEARARQ 170

                         90
                 ....*....|...
gi 654680519 171 RGAFGSPTFFVGN 183
Cdd:cd03024  171 LGISGVPFFVFNG 183
 
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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