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Conserved domains on  [gi|446032292|ref|WP_000110147|]
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MULTISPECIES: glutathione S-transferase N-terminal domain-containing protein [Acinetobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sspA super family cl35840
stringent starvation protein A; Provisional
 11-207 1.29e-56

stringent starvation protein A; Provisional


The actual alignment was detected with superfamily member PRK09481:

Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 178.75  E-value: 1.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTDHED--EDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRYRQNKLYA 88
Cdd:PRK09481  11 MTLFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKDNlpQDLIDLNPYQSVPTLVDRELTLYESRIIMEYLDERFPHPPLMP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  89 DAPMARAEQRQYIWRLENDWFKLADHMLRHadtlNVEQKQKAQKELRDTLISLTPLFQHFPYFMSENFSILDCMLAPIFV 168
Cdd:PRK09481  91 VYPVARGESRLMMHRIEKDWYSLMNKIVNG----SASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVDCYLAPLLW 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446032292 169 RLNSMGIDLPKQQCRPIFLYCKRIFNRPSFVKSMTPQEK 207
Cdd:PRK09481 167 RLPVLGIELSGPGAKELKGYMTRVFERDSFLASLTEAER 205
 
Name Accession Description Interval E-value
sspA PRK09481
stringent starvation protein A; Provisional
 11-207 1.29e-56

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 178.75  E-value: 1.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTDHED--EDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRYRQNKLYA 88
Cdd:PRK09481  11 MTLFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKDNlpQDLIDLNPYQSVPTLVDRELTLYESRIIMEYLDERFPHPPLMP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  89 DAPMARAEQRQYIWRLENDWFKLADHMLRHadtlNVEQKQKAQKELRDTLISLTPLFQHFPYFMSENFSILDCMLAPIFV 168
Cdd:PRK09481  91 VYPVARGESRLMMHRIEKDWYSLMNKIVNG----SASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVDCYLAPLLW 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446032292 169 RLNSMGIDLPKQQCRPIFLYCKRIFNRPSFVKSMTPQEK 207
Cdd:PRK09481 167 RLPVLGIELSGPGAKELKGYMTRVFERDSFLASLTEAER 205
GST_C_SspA cd03186
C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase ...
 91-202 2.54e-44

C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase (GST) C-terminal domain family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 198295 [Multi-domain]  Cd Length: 108  Bit Score: 143.57  E-value: 2.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  91 PMARAEQRQYIWRLENDWFKLADHMLRHADTlnvEQKQKAQKELRDTLISLTPLFQHFPYFMSENFSILDCMLAPIFVRL 170
Cdd:cd03186    1 PVSRARSRLMMHRIEQDWYPLLDTILNGRDE---KEAEKARKELRESLTALAPVFAASPYFLSEEFSLVDCYLAPLLWRL 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446032292 171 NSMGIDLPKQQcRPIFLYCKRIFNRPSFVKSM 202
Cdd:cd03186   78 PALGIELPKQA-KAIKDYMERVFARDSFQASL 108
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
11-206 4.55e-35

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 123.08  E-value: 4.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTD-----HEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRYRQNK 85
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDlakgeQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  86 LYADAPMARAEQRQYIWRLENDWFK-LADHMLRHADTLNVEQKQKAQKELRDTLISLTPLFQHFPYFMSENFSILDCMLA 164
Cdd:COG0625   82 LLPADPAARARVRQWLAWADGDLHPaLRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446032292 165 PIFVRLNSMGIDLPKqqcRPIFL-YCKRIFNRPSFVKSMTPQE 206
Cdd:COG0625  162 PVLRRLDRLGLDLAD---YPNLAaWLARLAARPAFQRALAAAE 201
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 11-79 6.84e-12

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 58.86  E-value: 6.84e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446032292   11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTD-----HEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDD 79
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDfgagpEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 12-99 1.74e-05

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 43.85  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292   12 TLYSHaddFRS---HWIRFLLAEKQIKYQLIVTD-------HEDEDLAsLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRY 81
Cdd:TIGR01262   1 KLYSY---WRSscsYRVRIALALKGIDYEYVPVNllrdgeqRSPEFLA-LNPQGLVPTLDIDGEVLTQSLAIIEYLEETY 76

                          90
                  ....*....|....*...
gi 446032292   82 RQNKLYADAPMARAEQRQ 99
Cdd:TIGR01262  77 PDPPLLPADPIKRARVRA 94
 
Name Accession Description Interval E-value
sspA PRK09481
stringent starvation protein A; Provisional
 11-207 1.29e-56

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 178.75  E-value: 1.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTDHED--EDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRYRQNKLYA 88
Cdd:PRK09481  11 MTLFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKDNlpQDLIDLNPYQSVPTLVDRELTLYESRIIMEYLDERFPHPPLMP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  89 DAPMARAEQRQYIWRLENDWFKLADHMLRHadtlNVEQKQKAQKELRDTLISLTPLFQHFPYFMSENFSILDCMLAPIFV 168
Cdd:PRK09481  91 VYPVARGESRLMMHRIEKDWYSLMNKIVNG----SASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVDCYLAPLLW 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446032292 169 RLNSMGIDLPKQQCRPIFLYCKRIFNRPSFVKSMTPQEK 207
Cdd:PRK09481 167 RLPVLGIELSGPGAKELKGYMTRVFERDSFLASLTEAER 205
GST_C_SspA cd03186
C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase ...
 91-202 2.54e-44

C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase (GST) C-terminal domain family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 198295 [Multi-domain]  Cd Length: 108  Bit Score: 143.57  E-value: 2.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  91 PMARAEQRQYIWRLENDWFKLADHMLRHADTlnvEQKQKAQKELRDTLISLTPLFQHFPYFMSENFSILDCMLAPIFVRL 170
Cdd:cd03186    1 PVSRARSRLMMHRIEQDWYPLLDTILNGRDE---KEAEKARKELRESLTALAPVFAASPYFLSEEFSLVDCYLAPLLWRL 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446032292 171 NSMGIDLPKQQcRPIFLYCKRIFNRPSFVKSM 202
Cdd:cd03186   78 PALGIELPKQA-KAIKDYMERVFARDSFQASL 108
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
11-206 4.55e-35

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 123.08  E-value: 4.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTD-----HEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRYRQNK 85
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDlakgeQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  86 LYADAPMARAEQRQYIWRLENDWFK-LADHMLRHADTLNVEQKQKAQKELRDTLISLTPLFQHFPYFMSENFSILDCMLA 164
Cdd:COG0625   82 LLPADPAARARVRQWLAWADGDLHPaLRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446032292 165 PIFVRLNSMGIDLPKqqcRPIFL-YCKRIFNRPSFVKSMTPQE 206
Cdd:COG0625  162 PVLRRLDRLGLDLAD---YPNLAaWLARLAARPAFQRALAAAE 201
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 11-81 1.22e-33

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 115.50  E-value: 1.22e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446032292  11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTD--HEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRY 81
Cdd:cd03059    1 MTLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDpdNPPEDLAELNPYGTVPTLVDRDLVLYESRIIMEYLDERF 73
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 11-78 3.40e-12

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 59.51  E-value: 3.40e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446032292  11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTD---HEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLD 78
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDlgeGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 11-79 6.84e-12

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 58.86  E-value: 6.84e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446032292   11 ITLYSHADDFRSHWIRFLLAEKQIKYQLIVTD-----HEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDD 79
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDfgagpEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 11-81 1.89e-07

GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 47.11  E-value: 1.89e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446032292  11 ITLYsHADDFRSHWIRFLLAEKQIKYQLIVTDHEDEDLAS-----LNPYNQLPMLVEQNLKLFSAPIIAEYLDDRY 81
Cdd:cd03046    1 ITLY-HLPRSRSFRILWLLEELGLPYELVLYDRGPGEQAPpeylaINPLGKVPVLVDGDLVLTESAAIILYLAEKY 75
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 25-80 1.10e-06

GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.


Pssm-ID: 239351 [Multi-domain]  Cd Length: 76  Bit Score: 44.95  E-value: 1.10e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446032292  25 IRFLLAEKQIKYQLIVTD-----HEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDR 80
Cdd:cd03053   16 VLLCLEEKGVDYELVPVDltkgeHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAEK 76
PRK15113 PRK15113
glutathione transferase;
11-99 3.57e-06

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 46.11  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  11 ITLYSHADDFR----SHWIrfLLAEKQIKYQLIVTD-----HEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRY 81
Cdd:PRK15113   6 ITLYSDAHFFSpyvmSAFV--ALQEKGLPFELKTVDldageHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERF 83

                         90       100
                 ....*....|....*....|.
gi 446032292  82 RQ---NKLYADAPMARAEQRQ 99
Cdd:PRK15113  84 APpawERIYPADLQARARARQ 104
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 12-99 1.74e-05

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 43.85  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292   12 TLYSHaddFRS---HWIRFLLAEKQIKYQLIVTD-------HEDEDLAsLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRY 81
Cdd:TIGR01262   1 KLYSY---WRSscsYRVRIALALKGIDYEYVPVNllrdgeqRSPEFLA-LNPQGLVPTLDIDGEVLTQSLAIIEYLEETY 76

                          90
                  ....*....|....*...
gi 446032292   82 RQNKLYADAPMARAEQRQ 99
Cdd:TIGR01262  77 PDPPLLPADPIKRARVRA 94
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 22-80 7.87e-05

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 39.54  E-value: 7.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446032292   22 SHWIRFLLAEKQIKYQLIVTDHED----EDLASLNPYNQLPMLV-EQNLKLFSAPIIAEYLDDR 80
Cdd:pfam13409   5 SHRVRLALEEKGLPYEIELVDLDPkdkpPELLALNPLGTVPVLVlPDGTVLTDSLVILEYLEEL 68
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 25-139 7.93e-05

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 42.01  E-value: 7.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  25 IRFLLAEKQIKYQLIVTD--HEDEDLASLNPYNQLPMLV-EQNLKLFSAPIIAEYLDDRYRQNKLYADAPMARAEQRQyi 101
Cdd:PRK10357  15 ISILLLEKGITFEFVNELpyNADNGVAQYNPLGKVPALVtEEGECWFDSPIIAEYIELLNVAPAMLPRDPLAALRVRQ-- 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446032292 102 wrLEndwfKLADHMLRHADTLNVEQKQKAQKELRDTLI 139
Cdd:PRK10357  93 --LE----ALADGIMDAALVSVREQARPAAQQSEDELL 124
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 13-78 8.04e-05

GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 39.55  E-value: 8.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446032292  13 LYSHADDFrSHWIRFLLAEKQ--IKYQLIVTD--HEDEDLASLNPYNQLPMLV-EQNLKLFSAPIIAEYLD 78
Cdd:cd03049    4 LYSPTSPY-VRKVRVAAHETGlgDDVELVLVNpwSDDESLLAVNPLGKIPALVlDDGEALFDSRVICEYLD 73
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
25-85 9.79e-05

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 39.52  E-value: 9.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446032292   25 IRFLLAEKQIKYQ--LIVTDHEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLDDRYRQNK 85
Cdd:pfam13417  13 VRIALNEKGLPYEfvPIPPGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 11-78 2.18e-04

GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid.


Pssm-ID: 239340 [Multi-domain]  Cd Length: 73  Bit Score: 38.32  E-value: 2.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446032292  11 ITLYSHaddFRS---HWIRFLLAEKQIKYQ-----LIVTDHEDEDLASLNPYNQLPMLVEQNLKLFSAPIIAEYLD 78
Cdd:cd03042    1 MILYSY---FRSsasYRVRIALNLKGLDYEyvpvnLLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYLD 73
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 11-81 3.69e-03

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes.


Pssm-ID: 239346 [Multi-domain]  Cd Length: 81  Bit Score: 35.21  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  11 ITLYSHADDfRSHWIRFLLAEKQIKYQLIVTD-----HEDEDLASLNPYNQLPMLVEQN---LKLF-SAPIIaEYLDDRY 81
Cdd:cd03048    2 ITLYTHGTP-NGFKVSIMLEELGLPYEIHPVDiskgeQKKPEFLKINPNGRIPAIVDHNgtpLTVFeSGAIL-LYLAEKY 79
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 128-191 5.97e-03

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 34.22  E-value: 5.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446032292  128 QKAQKELRDTLISLTPLFQHFPYFMSENFSILDCMLAPIFVRLNSMGIDLP-KQQCRPIFLYCKR 191
Cdd:pfam13410   3 ERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDlREGYPRLRAWLER 67
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 25-78 8.18e-03

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 34.20  E-value: 8.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446032292  25 IRFLLAEKQIKYQLIVTD-----HEDEDLASLNPYNQLPMLV-EQNLKLFSAPIIAEYLD 78
Cdd:cd03051   15 VRIFLAEKGIDVPLVTVDlaageQRSPEFLAKNPAGTVPVLElDDGTVITESVAICRYLE 74
GST_C_3 cd03194
C-terminal, alpha helical domain of an unknown subfamily 3 of Glutathione S-transferases; ...
 151-198 9.68e-03

C-terminal, alpha helical domain of an unknown subfamily 3 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 3; composed of uncharacterized proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198303  Cd Length: 115  Bit Score: 34.84  E-value: 9.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446032292 151 FMSENFSILDCMLAPIFVRLNSMGIDLPkQQCRPiflYCKRIFNRPSF 198
Cdd:cd03194   66 FLFGEFSIADAFYAPVVTRFRTYGVPLS-PAARA---YVEALLALPAM 109
 
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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