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Conserved domains on  [gi|1071412039|ref|WP_069837544|]
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type 1 glutamine amidotransferase family protein [Bacillus subtilis]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 10123441)

type 1 glutamine amidotransferase (GATase1) family protein similar to Bacillus subtilis proteases YoaZ and YdeA

CATH:  3.40.50.880
EC:  3.2.-.-
Gene Ontology:  GO:0019172|GO:0008233
MEROPS:  C56
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-181 1.93e-83

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


:

Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 244.82  E-value: 1.93e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   6 VYLYVFHTMSDWEYGYLIAELNSGRYFKqdaaslkVVTVGANKEMITTLGGLSIKPDISLDECTLESQDLIILPGGNTWG 85
Cdd:cd03140     1 IAVFLTDEFADWEGAYLAALLNSYEGFE-------VRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  86 EDIHQPILKKVGDALKLGTTIAAICGATLGLANEGYLNSRKHTSNDLEYMKMVCPNYKGETLYEKEPAVSDKNLVTASGI 165
Cdd:cd03140    74 NPEAPDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEYYDEPQAVSDGNLITANGT 153

                         170
                  ....*....|....*.
gi 1071412039 166 APLEFAVEVLKKLDVF 181
Cdd:cd03140   154 APVEFAAEILRALDVF 169
 
Name Accession Description Interval E-value
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-181 1.93e-83

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 244.82  E-value: 1.93e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   6 VYLYVFHTMSDWEYGYLIAELNSGRYFKqdaaslkVVTVGANKEMITTLGGLSIKPDISLDECTLESQDLIILPGGNTWG 85
Cdd:cd03140     1 IAVFLTDEFADWEGAYLAALLNSYEGFE-------VRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  86 EDIHQPILKKVGDALKLGTTIAAICGATLGLANEGYLNSRKHTSNDLEYMKMVCPNYKGETLYEKEPAVSDKNLVTASGI 165
Cdd:cd03140    74 NPEAPDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEYYDEPQAVSDGNLITANGT 153

                         170
                  ....*....|....*.
gi 1071412039 166 APLEFAVEVLKKLDVF 181
Cdd:cd03140   154 APVEFAAEILRALDVF 169
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 4-177 4.57e-48

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 155.11  E-value: 4.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   4 RKVYLYVFHTMSDWEYGYLIAELNsgryfkqdAASLKVVTVGANKEMITTLGGLSIKPDISLDECTLESQDLIILPGGNT 83
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLR--------RAGIKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  84 WGEDIHQP--ILKKVGDALKLGTTIAAICGATLGLANEGYLNSRKHTSNDLEYMKMVCPNYKgetlYEKEPAVSDKNLVT 161
Cdd:pfam01965  73 GPERLRDNekLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGAT----YVDKPVVVDGNLVT 148

                         170
                  ....*....|....*..
gi 1071412039 162 ASG-IAPLEFAVEVLKK 177
Cdd:pfam01965 149 SRGpGDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 3-178 1.52e-29

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 107.50  E-value: 1.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   3 TRKVYLYVFHTMSDWEYGYLIAELNSGRYfkqdaaslKVVTVGANK-EMITTLGGLSIKPDISLDECTLESQDLIILPGG 81
Cdd:COG0693     2 MKKVLILLTDGFEDEELTVPYDALREAGA--------EVDVASPEGgPPVTSKHGITVTADKTLDDVDPDDYDALVLPGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  82 NTWGEDI--HQPILKKVGDALKLGTTIAAICGATLGLANEGYLNSRKHTS--NDLEYMKMvcpnyKGETlYEKEPAVSDK 157
Cdd:COG0693    74 HGAPDDLreDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSfpNIEDDLKN-----AGAT-YVDEEVVVDG 147

                         170       180
                  ....*....|....*....|..
gi 1071412039 158 NLVTASGIAPL-EFAVEVLKKL 178
Cdd:COG0693   148 NLITSRGPGDApAFARALLELL 169
ftrA PRK09393
transcriptional activator FtrA; Provisional
 43-128 4.36e-05

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 43.41  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  43 TVGANKEMITTLGGLSIKPDISLDecTLESQDLIILPGGNTWGEDIHQPILKKVGDALKLGTTIAAICGATLGLANEGYL 122
Cdd:PRK09393   48 VAAVEPGPLRAAGGITVVADGGLE--LLDRADTIVIPGWRGPDAPVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLL 125


                  ....*.
gi 1071412039 123 NSRKHT 128
Cdd:PRK09393  126 DGRRAT 131
 
Name Accession Description Interval E-value
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-181 1.93e-83

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 244.82  E-value: 1.93e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   6 VYLYVFHTMSDWEYGYLIAELNSGRYFKqdaaslkVVTVGANKEMITTLGGLSIKPDISLDECTLESQDLIILPGGNTWG 85
Cdd:cd03140     1 IAVFLTDEFADWEGAYLAALLNSYEGFE-------VRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  86 EDIHQPILKKVGDALKLGTTIAAICGATLGLANEGYLNSRKHTSNDLEYMKMVCPNYKGETLYEKEPAVSDKNLVTASGI 165
Cdd:cd03140    74 NPEAPDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEYYDEPQAVSDGNLITANGT 153

                         170
                  ....*....|....*.
gi 1071412039 166 APLEFAVEVLKKLDVF 181
Cdd:cd03140   154 APVEFAAEILRALDVF 169
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 4-177 4.57e-48

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 155.11  E-value: 4.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   4 RKVYLYVFHTMSDWEYGYLIAELNsgryfkqdAASLKVVTVGANKEMITTLGGLSIKPDISLDECTLESQDLIILPGGNT 83
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLR--------RAGIKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  84 WGEDIHQP--ILKKVGDALKLGTTIAAICGATLGLANEGYLNSRKHTSNDLEYMKMVCPNYKgetlYEKEPAVSDKNLVT 161
Cdd:pfam01965  73 GPERLRDNekLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGAT----YVDKPVVVDGNLVT 148

                         170
                  ....*....|....*..
gi 1071412039 162 ASG-IAPLEFAVEVLKK 177
Cdd:pfam01965 149 SRGpGDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 3-178 1.52e-29

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 107.50  E-value: 1.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   3 TRKVYLYVFHTMSDWEYGYLIAELNSGRYfkqdaaslKVVTVGANK-EMITTLGGLSIKPDISLDECTLESQDLIILPGG 81
Cdd:COG0693     2 MKKVLILLTDGFEDEELTVPYDALREAGA--------EVDVASPEGgPPVTSKHGITVTADKTLDDVDPDDYDALVLPGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  82 NTWGEDI--HQPILKKVGDALKLGTTIAAICGATLGLANEGYLNSRKHTS--NDLEYMKMvcpnyKGETlYEKEPAVSDK 157
Cdd:COG0693    74 HGAPDDLreDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSfpNIEDDLKN-----AGAT-YVDEEVVVDG 147

                         170       180
                  ....*....|....*....|..
gi 1071412039 158 NLVTASGIAPL-EFAVEVLKKL 178
Cdd:COG0693   148 NLITSRGPGDApAFARALLELL 169
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 37-178 8.61e-18

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 76.82  E-value: 8.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  37 ASLKVVTVG-ANKEMITTLGGLSIKPDISLDECTLESQDLIILPGGNTwGEDIH---QPILKKVGDALKLGTTIAAICGA 112
Cdd:cd03135    24 AGIEVTTASlEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLP-GAQNLadnEKLIKLLKEFNAKGKLIAAICAA 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1071412039 113 TLGLANEGYLNSRKHTSNDLEYMKMVCPNykgetlYEKEPAVSDKNLVTASGIA-PLEFAVEVLKKL 178
Cdd:cd03135   103 PAVLAKAGLLKGKKATCYPGFEDKLGGAN------YVDEPVVVDGNIITSRGPGtAFEFALKIVEAL 163
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 36-178 1.30e-12

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 63.33  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  36 AASLKVVTVGANKEMITTLGGLSIKPDISLDECTLEsqDLIILPGG-NTWGEDIHQPILKKVGDALKLGTTIAAICGATL 114
Cdd:cd03139    28 AAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDL--DVLLVPGGgGTRALVNDPALLDFIRRQAARAKYVTSVCTGAL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1071412039 115 GLANEGYLNSRKHTSN--DLEYMKMVCPNYKGETLYekepaVSDKNLVTASGI-APLEFAVEVLKKL 178
Cdd:cd03139   106 LLAAAGLLDGRRATTHwaAIDWLKEFGAIVVVDARW-----VVDGNIWTSGGVsAGIDMALALVARL 167
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 24-162 4.69e-10

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 56.01  E-value: 4.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  24 AELNSGRY-FKQDAASLKVVTVGANKEMITTLGGLSIKPDISLDECTLESQDLIILPGGntWGED---IHQPILKKVGDA 99
Cdd:cd03134    13 VELTYPLYrLREAGAEVVVAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGG--TNPDklrRDPDAVAFVRAF 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1071412039 100 LKLGTTIAAICGATLGLANEGYLNSRKHTS-----NDLEymkmvcpNYKGEtlYEKEPAVSDKNLVTA 162
Cdd:cd03134    91 AEAGKPVAAICHGPWVLISAGVVRGRKLTSypsikDDLI-------NAGAN--WVDEEVVVDGNLITS 149
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 41-126 6.67e-07

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 48.62  E-value: 6.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  41 VVTVGANKEMITTLGGLSIKPDISLDEctLESQDLIILPGGNTWGEDIHQPILKKVGDALKLGTTIAAICGATLGLANEG 120
Cdd:COG4977    37 WRLVSLDGGPVRSSSGLTVAPDHGLAD--LAAADTLIVPGGLDPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAG 114


                  ....*.
gi 1071412039 121 YLNSRK 126
Cdd:COG4977   115 LLDGRR 120
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 41-166 3.60e-06

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 45.57  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  41 VVTVGANKEMITTLGGLSIKPDISLDecTLESQDLIILPGGNT-WGEDIHQPILKKVGDALKLGTTIAAICGATLGLANE 119
Cdd:cd03137    35 LRVCSPEGGPVRSSSGLSLVADAGLD--ALAAADTVIVPGGPDvDGRPPPPALLAALRRAAARGARVASVCTGAFVLAEA 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1071412039 120 GYLNSRKHTS--NDLEYMKMVCPNYKGET--LYekepaVSDKNLVTASGIA 166
Cdd:cd03137   113 GLLDGRRATThwAYAEDLARRFPAVRVDPdvLY-----VDDGNVWTSAGVT 158
ftrA PRK09393
transcriptional activator FtrA; Provisional
 43-128 4.36e-05

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 43.41  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039  43 TVGANKEMITTLGGLSIKPDISLDecTLESQDLIILPGGNTWGEDIHQPILKKVGDALKLGTTIAAICGATLGLANEGYL 122
Cdd:PRK09393   48 VAAVEPGPLRAAGGITVVADGGLE--LLDRADTIVIPGWRGPDAPVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLL 125


                  ....*.
gi 1071412039 123 NSRKHT 128
Cdd:PRK09393  126 DGRRAT 131
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-116 5.50e-04

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 38.35  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   6 VYLYVFHTMSDWEYGYLIAELNsgryfkqdAASLKVVTVGANKEMITTlgglsikpDISLDECtlesqDLIILPGGNTWG 85
Cdd:cd01653     1 VAVLLFPGFEELELASPLDALR--------EAGAEVDVVSPDGGPVES--------DVDLDDY-----DGLILPGGPGTP 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1071412039  86 EDI--HQPILKKVGDALKLGTTIAAICGATLGL 116
Cdd:cd01653    60 DDLarDEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-116 3.25e-03

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 35.64  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071412039   6 VYLYVFHTMSDWEYGYLIAELNsgryfkqdAASLKVVTVGANKEMITTlgglsikpDISLDECtlesqDLIILPGGNTWG 85
Cdd:cd03128     1 VAVLLFGGSEELELASPLDALR--------EAGAEVDVVSPDGGPVES--------DVDLDDY-----DGLILPGGPGTP 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1071412039  86 EDIH--QPILKKVGDALKLGTTIAAICGATLGL 116
Cdd:cd03128    60 DDLAwdEALLALLREAAAAGKPVLGICLGAQLL 92
 
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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