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Conserved domains on  [gi|499321970|ref|WP_011012462|]
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MULTISPECIES: class II glutamine amidotransferase [Pyrococcus]

Protein Classification

class II glutamine amidotransferase domain-containing protein( domain architecture ID 1025)

class II glutamine amidotransferase domain-containing protein may hydrolyze ammonia from glutamine and transfer the amino group to the appropriate substrate

EC:  2.4.2.-
Gene Ontology:  GO:0016740|GO:0006541
PubMed:  9559052|8430515
SCOP:  3000131

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gn_AT_II super family cl00319
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 1-145 2.97e-43

Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.


The actual alignment was detected with superfamily member pfam13230:

Pssm-ID: 469719 [Multi-domain]  Cd Length: 272  Bit Score: 144.01  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970    1 MCELFDVNANKGVSVNFTWRGFV-RKGELNPH--GWGISWYltavnGKRAASLIKQPIPAYESMIALTLPRLNIRSQIII 77
Cdd:pfam13230   1 MCQLLGMNCNVPTDICFSFTGFArRGGLTDHHadGWGIAFY-----EGRGARVFKDPQPSADSPIAELVRRYPIRSRNVI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970   78 SHVRFAT-SEINYLDTHPFVRRIKsiGQYdeWIFAHNGVLNGVK-ELPKRFKPLGTTDSEAAFCYIMENL 145
Cdd:pfam13230  76 AHIRKATqGRVTLENTHPFMRELW--GRY--WIFAHNGDLKGYApKLSGRFQPVGSTDSELAFCWLLDRL 141
 
Name Accession Description Interval E-value
GATase_4 pfam13230
Glutamine amidotransferases class-II; This family captures members that are not found in ...
 1-145 2.97e-43

Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.


Pssm-ID: 433047 [Multi-domain]  Cd Length: 272  Bit Score: 144.01  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970    1 MCELFDVNANKGVSVNFTWRGFV-RKGELNPH--GWGISWYltavnGKRAASLIKQPIPAYESMIALTLPRLNIRSQIII 77
Cdd:pfam13230   1 MCQLLGMNCNVPTDICFSFTGFArRGGLTDHHadGWGIAFY-----EGRGARVFKDPQPSADSPIAELVRRYPIRSRNVI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970   78 SHVRFAT-SEINYLDTHPFVRRIKsiGQYdeWIFAHNGVLNGVK-ELPKRFKPLGTTDSEAAFCYIMENL 145
Cdd:pfam13230  76 AHIRKATqGRVTLENTHPFMRELW--GRY--WIFAHNGDLKGYApKLSGRFQPVGSTDSELAFCWLLDRL 141
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
2-146 2.99e-36

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 125.08  E-value: 2.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970   2 CELFDVNANKGVSVNF----TWRGFVR-----KGELNPHGWGISWYltavNGKRAASLIKQPIPAYESMIALTLPRlNIR 72
Cdd:COG0121    1 CRLLGYSGNVPTDLEFllldPEHSLVRqsgatREGPHADGWGIGWY----EGDGEPRLYRDPLPAWSDPNLRLLAR-PIK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970  73 SQIIISHVRFAT-SEINYLDTHPFVrriksigqYDEWIFAHNGVLNGVKELPKR----------FKPLGTTDSEAAFCYI 141
Cdd:COG0121   76 SRLVIAHVRKATvGPVSLENTHPFR--------GGRWLFAHNGQLDGFDRLRRRlaeelpdelyFQPVGTTDSELAFALL 147


                 ....*
gi 499321970 142 MENLE 146
Cdd:COG0121  148 LSRLR 152
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 1-147 7.25e-28

Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238889 [Multi-domain]  Cd Length: 257  Bit Score: 103.62  E-value: 7.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970   1 MCELFDVNANKGVS----VNFTWRGFVR-------KGELNPHGWGISWYltavNGKRAASLI-KQPIPAyESMIALtlPR 68
Cdd:cd01908    1 MCRLLGYSGAPIPLepllIRPSHSLLVQsggpremKGTVHADGWGIGWY----EGKGGRPFRyRSPLPA-WSDINL--ES 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970  69 LN--IRSQIIISHVRFATS-EINYLDTHPFvrriksigQYDEWIFAHNGVLNGVKELPKRF------KPLGTTDSEAAFC 139
Cdd:cd01908   74 LArpIKSPLVLAHVRAATVgPVSLENCHPF--------TRGRWLFAHNGQLDGFRLLRRRLlrllprLPVGTTDSELAFA 145


                 ....*...
gi 499321970 140 YIMENLEG 147
Cdd:cd01908  146 LLLSRLLE 153
 
Name Accession Description Interval E-value
GATase_4 pfam13230
Glutamine amidotransferases class-II; This family captures members that are not found in ...
 1-145 2.97e-43

Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.


Pssm-ID: 433047 [Multi-domain]  Cd Length: 272  Bit Score: 144.01  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970    1 MCELFDVNANKGVSVNFTWRGFV-RKGELNPH--GWGISWYltavnGKRAASLIKQPIPAYESMIALTLPRLNIRSQIII 77
Cdd:pfam13230   1 MCQLLGMNCNVPTDICFSFTGFArRGGLTDHHadGWGIAFY-----EGRGARVFKDPQPSADSPIAELVRRYPIRSRNVI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970   78 SHVRFAT-SEINYLDTHPFVRRIKsiGQYdeWIFAHNGVLNGVK-ELPKRFKPLGTTDSEAAFCYIMENL 145
Cdd:pfam13230  76 AHIRKATqGRVTLENTHPFMRELW--GRY--WIFAHNGDLKGYApKLSGRFQPVGSTDSELAFCWLLDRL 141
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
2-146 2.99e-36

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 125.08  E-value: 2.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970   2 CELFDVNANKGVSVNF----TWRGFVR-----KGELNPHGWGISWYltavNGKRAASLIKQPIPAYESMIALTLPRlNIR 72
Cdd:COG0121    1 CRLLGYSGNVPTDLEFllldPEHSLVRqsgatREGPHADGWGIGWY----EGDGEPRLYRDPLPAWSDPNLRLLAR-PIK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970  73 SQIIISHVRFAT-SEINYLDTHPFVrriksigqYDEWIFAHNGVLNGVKELPKR----------FKPLGTTDSEAAFCYI 141
Cdd:COG0121   76 SRLVIAHVRKATvGPVSLENTHPFR--------GGRWLFAHNGQLDGFDRLRRRlaeelpdelyFQPVGTTDSELAFALL 147


                 ....*
gi 499321970 142 MENLE 146
Cdd:COG0121  148 LSRLR 152
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 1-147 7.25e-28

Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238889 [Multi-domain]  Cd Length: 257  Bit Score: 103.62  E-value: 7.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970   1 MCELFDVNANKGVS----VNFTWRGFVR-------KGELNPHGWGISWYltavNGKRAASLI-KQPIPAyESMIALtlPR 68
Cdd:cd01908    1 MCRLLGYSGAPIPLepllIRPSHSLLVQsggpremKGTVHADGWGIGWY----EGKGGRPFRyRSPLPA-WSDINL--ES 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970  69 LN--IRSQIIISHVRFATS-EINYLDTHPFvrriksigQYDEWIFAHNGVLNGVKELPKRF------KPLGTTDSEAAFC 139
Cdd:cd01908   74 LArpIKSPLVLAHVRAATVgPVSLENCHPF--------TRGRWLFAHNGQLDGFRLLRRRLlrllprLPVGTTDSELAFA 145


                 ....*...
gi 499321970 140 YIMENLEG 147
Cdd:cd01908  146 LLLSRLLE 153
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 2-154 1.22e-16

Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.


Pssm-ID: 238212 [Multi-domain]  Cd Length: 220  Bit Score: 73.64  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970   2 CELFDVNANKGVSVNFTW---RGFVRKGELNPHGWGISWYltavngkRAASLIKQPIPAYESMIALTLPRLNIRSQIIIS 78
Cdd:cd00352    1 CGIFGIVGADGAASLLLLlllRGLAALEHRGPDGAGIAVY-------DGDGLFVEKRAGPVSDVALDLLDEPLKSGVALG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321970  79 HVRFAT----SEINyldTHPFVRriksigQYDEWIFAHNGVLNGVKELPKRFKPLG-----TTDSEAAFCYIMENLEGIG 149
Cdd:cd00352   74 HVRLATnglpSEAN---AQPFRS------EDGRIALVHNGEIYNYRELREELEARGyrfegESDSEVILHLLERLGREGG 144


                 ....*
gi 499321970 150 TMRAL 154
Cdd:cd00352  145 LFEAV 149
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 68-135 7.83e-03

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.


Pssm-ID: 433279 [Multi-domain]  Cd Length: 130  Bit Score: 34.59  E-value: 7.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499321970   68 RLNIRSQIIISHVRFATSEINYLDTHPFVRRiksigqYDEWIFAHNG-VLNGVK---ELP-KRFKPLGTTDSE 135
Cdd:pfam13522   5 GIWVEGGVALGHVRLAIVDLPDAGNQPMLSR------DGRLVLVHNGeIYNYGElreELAdLGHAFRSRSDTE 71
 
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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