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Conserved domains on  [gi|446574365|ref|WP_000651711|]
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MULTISPECIES: thioredoxin domain-containing protein [Leptospira]

Protein Classification

DsbA family protein( domain architecture ID 11447254)

DsbA family protein belongs to the thioredoxin superfamily of proteins containing a redox active CXXC motif, similar to DsbA that is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  11967064|9099998|10049365|15558583|12524212
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 195-346 3.32e-59

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


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 187.90  E-value: 3.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 195 KVTVIEFSDFECPFCKRSQSINSQLREKYKD-QIRWVFRDYPLsFHPNAMFAHIAANCSASQGKYWEFFKVLFDNSGNLP 273
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDgKVRVVYRPFPL-LHPDSLRAARAALCAADQGKFWAFHDALFANQPALT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446574365 274 KDRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFINGVMIEGAQPIEAFIKVIDQEL 346
Cdd:COG1651   80 DDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 195-346 3.32e-59

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 187.90  E-value: 3.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 195 KVTVIEFSDFECPFCKRSQSINSQLREKYKD-QIRWVFRDYPLsFHPNAMFAHIAANCSASQGKYWEFFKVLFDNSGNLP 273
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDgKVRVVYRPFPL-LHPDSLRAARAALCAADQGKFWAFHDALFANQPALT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446574365 274 KDRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFINGVMIEGAQPIEAFIKVIDQEL 346
Cdd:COG1651   80 DDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
Thioredoxin_4 pfam13462
Thioredoxin;
183-344 5.77e-33

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 120.14  E-value: 5.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365  183 AGNNPSIGPENAKVTVIEFSDFECPFCKRSQSINSQLREKYKD--QIRWVFRDYPLSFHPNAMFAHIAANCSASQG-KYW 259
Cdd:pfam13462   1 TPTDPVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEYIDtgKVRFIIRDFPLDGEGESLLAAMAARCAGDQSpEYF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365  260 EFFKVLFDNSGNLPKdRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFINGVMIEGAQPIEAFI 339
Cdd:pfam13462  81 LVIDKLLYSQQEEWA-QDLELAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKVDGPLTYEELK 159


                  ....*
gi 446574365  340 KVIDQ 344
Cdd:pfam13462 160 KLIDD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 190-343 5.37e-31

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: 114.61  E-value: 5.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 190 GPENAKVTVIEFSDFECPFCKRSQSINSQLREKYKDqIRWVFRDYPLsFHPNAMFAHIAANCS--ASQGKYWEFFKVLFD 267
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPD-VRVVFKEFPI-LGESSVLAARVALAVwkNGPGKYLEFHNALMA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446574365 268 NSGNLPKDRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFINGVMIEGAQPIEAFIKVID 343
Cdd:cd03023   79 TRGRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPGAVPADTLKEAID 154
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 195-346 3.32e-59

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 187.90  E-value: 3.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 195 KVTVIEFSDFECPFCKRSQSINSQLREKYKD-QIRWVFRDYPLsFHPNAMFAHIAANCSASQGKYWEFFKVLFDNSGNLP 273
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDgKVRVVYRPFPL-LHPDSLRAARAALCAADQGKFWAFHDALFANQPALT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446574365 274 KDRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFINGVMIEGAQPIEAFIKVIDQEL 346
Cdd:COG1651   80 DDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
Thioredoxin_4 pfam13462
Thioredoxin;
183-344 5.77e-33

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 120.14  E-value: 5.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365  183 AGNNPSIGPENAKVTVIEFSDFECPFCKRSQSINSQLREKYKD--QIRWVFRDYPLSFHPNAMFAHIAANCSASQG-KYW 259
Cdd:pfam13462   1 TPTDPVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEYIDtgKVRFIIRDFPLDGEGESLLAAMAARCAGDQSpEYF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365  260 EFFKVLFDNSGNLPKdRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFINGVMIEGAQPIEAFI 339
Cdd:pfam13462  81 LVIDKLLYSQQEEWA-QDLELAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKVDGPLTYEELK 159


                  ....*
gi 446574365  340 KVIDQ 344
Cdd:pfam13462 160 KLIDD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 190-343 5.37e-31

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: 114.61  E-value: 5.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 190 GPENAKVTVIEFSDFECPFCKRSQSINSQLREKYKDqIRWVFRDYPLsFHPNAMFAHIAANCS--ASQGKYWEFFKVLFD 267
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPD-VRVVFKEFPI-LGESSVLAARVALAVwkNGPGKYLEFHNALMA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446574365 268 NSGNLPKDRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFINGVMIEGAQPIEAFIKVID 343
Cdd:cd03023   79 TRGRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPGAVPADTLKEAID 154
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 195-347 5.81e-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: 94.57  E-value: 5.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 195 KVTVIEFSDFECPFC---KRSqsINsQLREKYKDQIRWVFR--------------------------------------- 232
Cdd:COG2761    1 PLKIDIFSDVVCPWCyigKRR--LE-KALAEFGDDVEIRWRpfelnpdmppegedrreyllakgspeqaeqmrahveeaa 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 233 -------DYPLSFHPNAMFAHIAANCSASQGKYWEF----FKVLFDNSGNLPKDRVL-DLARGLGLDMKVFSQCVNDSEV 300
Cdd:COG2761   78 aeeglpfDFDRIKPPNTFDAHRLLKAAELQGKQDALlealFEAYFTEGRDIGDREVLlDLAAEVGLDAEEFRADLESDEA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446574365 301 RKEVEADMAEGEKYGVSGTPAFFING-VMIEGAQPIEAFIKVIDQELK 347
Cdd:COG2761  158 AAAVRADEAEARELGVTGVPTFVFDGkYAVSGAQPYEVFEQALRQALA 205
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 198-333 2.62e-22

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: 89.77  E-value: 2.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 198 VIEFSDFECPFCKRSQSINSQLREKYKDQIRWVFRDYPL--SFHPNAMFAHIAANCSASQGKYWEFFKVLfdnsgnlpkd 275
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLlgGMPPNSLAAARAALAAAAQGKFEALHEAL---------- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446574365 276 rvldlarglgldmkvfsqcvndsevrkeveADMAEGEKYGVSGTPAFFINGVMIEGAQ 333
Cdd:cd02972   71 ------------------------------ADTALARALGVTGTPTFVVNGEKYSGAG 98
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 197-343 3.88e-19

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: 84.02  E-value: 3.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365  197 TVIEFSDFECPFCKRSQSINSQLREKYKD-QIRW----------------------------------VFRDYPLSFHPN 241
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDvKVVYrpfplagakkignvgpsnlpvklkymmadlerwaALYGIPLRFPAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365  242 AMFAHIAANCSA--------SQGKYWEFFKVLFDNSGNL-PKDRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGE 312
Cdd:pfam01323  81 FLGNSTRANRLAlaagaeglAEKVVRELFNALWGEGAAItDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTAAAI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 446574365  313 KYGVSGTPAFFINGVMIEGAQPIEAFIKVID 343
Cdd:pfam01323 161 SLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 233-343 4.96e-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: 64.14  E-value: 4.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 233 DYPLSFHPNAMFAHIAANCSASQGK----YWEFFKVLFDNSGNLPKDRVL-DLARGLGLDMKVFSQCVNDSEVRKEVEAD 307
Cdd:cd03024   85 DFDRVRPPNTFDAHRLIHLAKEQGKqdalVEALFRAYFTEGKDIGDRDVLvDLAEEAGLDAAEARAVLASDEYADEVRAD 164

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446574365 308 MAEGEKYGVSGTPAFFING-VMIEGAQPIEAFIKVID 343
Cdd:cd03024  165 EARARQLGISGVPFFVFNGkYAVSGAQPPEVFLQALR 201
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 190-339 5.70e-12

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 63.87  E-value: 5.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 190 GPENAKVTVIEFSDFECPFCKRsqsINSQLREKYKD-QIRWVFrdYPLSFHPNAMfaHIAAN--CSasqgkyweffkvlf 266
Cdd:cd03020   73 GKGNGKRVVYVFTDPDCPYCRK---LEKELKPNADGvTVRIFP--VPILGLPDST--AKAAAiwCA-------------- 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446574365 267 dnsgnlpKDRV--LDLARGLGLDMKVFSQCvnDSEVRKEVEAdmaeGEKYGVSGTPA-FFINGVMIEGAQP---IEAFI 339
Cdd:cd03020  132 -------KDRAkaWTDAMSGGKVPPPAASC--DNPVAANLAL----GRQLGVNGTPTiVLADGRVVPGAPPaaqLEALL 197
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 191-344 1.90e-09

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: 56.14  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 191 PENAKVTVIEFSDFECPFCKRSQSINSQLREKYKDQirWVFRDYPLSFHPN----AMFAHIAANcSASQGKYWE--FFKV 264
Cdd:cd03019   12 IPSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPKD--VKFEKVPVVFGGGegepLARAFYAAE-ALGLEDKLHaaLFEA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 265 LFD-NSGNLPKDRVLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFING---VMIEGAQPIeAFIK 340
Cdd:cd03019   89 IHEkRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGkyvVNPSAIGGD-DTLQ 167


                 ....
gi 446574365 341 VIDQ 344
Cdd:cd03019  168 VLDE 171
Thioredoxin_3 pfam13192
Thioredoxin domain;
288-340 1.36e-05

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 42.59  E-value: 1.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446574365  288 MKVFSQCVNDSEVRKEVE--ADMAEGEKYGVSGTPAFFING-VMIEGAQPIEAFIK 340
Cdd:pfam13192  12 EKAVKEAAAELGIDAEVEkvTDFPEIAKYGVMSTPALVINGkVVSSGKVPSEEEIR 67
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 224-328 2.55e-04

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: 41.46  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 224 KDQIRW-VFRDYPLSFHP-------NAM-FAHIAANCSASQGKYWEF-FKVLFDNSGNLPKDRVL-DLARGLGLDMKVFS 292
Cdd:cd03022   62 RDLERWaRRYGIPLRFPPrfppntlRAMrAALAAQAEGDAAEAFARAvFRALWGEGLDIADPAVLaAVAAAAGLDADELL 141

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446574365 293 QCVNDSEVRKEVEADMAEGEKYGVSGTPAFFINGVM 328
Cdd:cd03022  142 AAADDPAVKAALRANTEEAIARGVFGVPTFVVDGEM 177
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
304-343 5.22e-04

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 40.50  E-value: 5.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446574365 304 VEADMAEG-------EKYGVSGTPAFFINGVMI-EGAQPIEAFIKVID 343
Cdd:COG3634  152 ITHEMIDGaefpdeaEKYGVMSVPTVVLNGEVFfVGRMPEEEILEKLD 199
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 210-336 1.02e-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: 39.61  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574365 210 KRSQSINSQLREKYKDQIrwvFRDYPLS--FHPNAMFAHIAANCSASQ---GKYWEFFKVL----FDNSGNLPKDRVL-D 279
Cdd:cd03025   54 WRIYVHWHKARIALTGQP---FGEDYLEllLFDLDSAPASRAIKAARLqgpERLLEMLKAIqrahYVEGRDLADTEVLrE 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446574365 280 LARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFI-----NGVMIEGAQPIE 336
Cdd:cd03025  131 LAIELGLDVEEFLEDFQSDEAKQAIQEDQKLARELGINGFPTLVLeddngEGILLTGYYPYE 192
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
 277-324 1.18e-03

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 39.46  E-value: 1.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446574365 277 VLDLARGLGLDMKVFSQCVNDSEVRKEVEADMAEGEKYGVSGTPAFFI 324
Cdd:COG3531  133 LAELAAELGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPTLVL 180
 
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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