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Conserved domains on  [gi|79313243|ref|NP_001030701|]
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aluminum induced protein with YGL and LRDR motifs [Arabidopsis thaliana]

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 ...
 2-200 1.09e-115

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 pfam12481:

Pssm-ID: 469719 [Multi-domain]  Cd Length: 228  Bit Score: 328.56  E-value: 1.09e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243     2 LAIFQKAFAHPPEELNSPAS-HFSGKTPKLPGETLSDFLSHHQNnAFSMNFGDSAVLAYARQETS-LRQRLFCGLDGIYC 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHPN-AVSVNLGDSGFLAYSHHKQNpLLPRLFAVVDDIFC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243    80 MFLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLY 159
Cdd:pfam12481  80 LFQGHLENLASLKQQYGLS-KGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 79313243   160 WGISGDGSVVMSDDIQIIKQGCAKSFAPFPNGkpklKFFIS 200
Cdd:pfam12481 159 WGIDADGSLVFSDDIEIVKKGCGKSFAPFPKG----CFFTS 195
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
 2-200 1.09e-115

Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.


Pssm-ID: 403619 [Multi-domain]  Cd Length: 228  Bit Score: 328.56  E-value: 1.09e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243     2 LAIFQKAFAHPPEELNSPAS-HFSGKTPKLPGETLSDFLSHHQNnAFSMNFGDSAVLAYARQETS-LRQRLFCGLDGIYC 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHPN-AVSVNLGDSGFLAYSHHKQNpLLPRLFAVVDDIFC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243    80 MFLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLY 159
Cdd:pfam12481  80 LFQGHLENLASLKQQYGLS-KGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 79313243   160 WGISGDGSVVMSDDIQIIKQGCAKSFAPFPNGkpklKFFIS 200
Cdd:pfam12481 159 WGIDADGSLVFSDDIEIVKKGCGKSFAPFPKG----CFFTS 195
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 2-191 5.44e-98

This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of 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 Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.


Pssm-ID: 238891 [Multi-domain]  Cd Length: 224  Bit Score: 283.82  E-value: 5.44e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243   2 LAIFQKAFAHPPEELNSPASHfsgKTPKLPGETLSDFLSHHQNNAFSMnFGDSAVLAY-ARQETSLRQRLFCGLDGIYCM 80
Cdd:cd01910   1 LAVFSKAVAKPPEELVSAGSR---TPAKTAEELLKRFLSANPSAVFVH-LGAAGFLAYsHHNQSPLHPRLFAVKDDIFCL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243  81 FLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLYW 160
Cdd:cd01910  77 FQGHLDNLGSLKQQYGLS-KTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYW 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 79313243 161 GISGDGSVVMSDDIQIIKQGCAKSFAPFPNG 191
Cdd:cd01910 156 GIAADGSVVFSDDVELVKASCGKSFAPFPKG 186
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 130-191 1.69e-06

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 47.79  E-value: 1.69e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79313243  130 LEGSFAFVVYDTQTSSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCAKsFAPFPNG 191
Cdd:PTZ00077 125 LDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVE-VKQFPPG 185
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
 2-200 1.09e-115

Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.


Pssm-ID: 403619 [Multi-domain]  Cd Length: 228  Bit Score: 328.56  E-value: 1.09e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243     2 LAIFQKAFAHPPEELNSPAS-HFSGKTPKLPGETLSDFLSHHQNnAFSMNFGDSAVLAYARQETS-LRQRLFCGLDGIYC 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHPN-AVSVNLGDSGFLAYSHHKQNpLLPRLFAVVDDIFC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243    80 MFLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLY 159
Cdd:pfam12481  80 LFQGHLENLASLKQQYGLS-KGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 79313243   160 WGISGDGSVVMSDDIQIIKQGCAKSFAPFPNGkpklKFFIS 200
Cdd:pfam12481 159 WGIDADGSLVFSDDIEIVKKGCGKSFAPFPKG----CFFTS 195
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 2-191 5.44e-98

This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of 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 Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.


Pssm-ID: 238891 [Multi-domain]  Cd Length: 224  Bit Score: 283.82  E-value: 5.44e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243   2 LAIFQKAFAHPPEELNSPASHfsgKTPKLPGETLSDFLSHHQNNAFSMnFGDSAVLAY-ARQETSLRQRLFCGLDGIYCM 80
Cdd:cd01910   1 LAVFSKAVAKPPEELVSAGSR---TPAKTAEELLKRFLSANPSAVFVH-LGAAGFLAYsHHNQSPLHPRLFAVKDDIFCL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243  81 FLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLYW 160
Cdd:cd01910  77 FQGHLDNLGSLKQQYGLS-KTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYW 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 79313243 161 GISGDGSVVMSDDIQIIKQGCAKSFAPFPNG 191
Cdd:cd01910 156 GIAADGSVVFSDDVELVKASCGKSFAPFPKG 186
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 70-191 5.15e-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: 73.25  E-value: 5.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313243  70 LFCGLDGIYCMFLGRLNNLCTLNRQYGLSGKNsNEAMFVIEAYRTLRDRGPY------PADQVLRGLEGSFAFVVYDTQT 143
Cdd:cd00352  91 FRSEDGRIALVHNGEIYNYRELREELEARGYR-FEGESDSEVILHLLERLGRegglfeAVEDALKRLDGPFAFALWDGKP 169

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 79313243 144 SSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCAKSFAPFPNG 191
Cdd:cd00352 170 DRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPFKGVRRLPPG 217
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 130-191 1.69e-06

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 47.79  E-value: 1.69e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79313243  130 LEGSFAFVVYDTQTSSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCAKsFAPFPNG 191
Cdd:PTZ00077 125 LDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVE-VKQFPPG 185
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 130-191 9.45e-06

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 45.53  E-value: 9.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79313243  130 LEGSFAFVVYDTQTSSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCAKsFAPFPNG 191
Cdd:PLN02549 117 LDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALCDDCER-FEEFPPG 177
asnB PRK09431
asparagine synthetase B; Provisional
 130-191 8.56e-04

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 39.51  E-value: 8.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79313243  130 LEGSFAFVVYDTQTSSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCaKSFAPFPNG 191
Cdd:PRK09431 118 LDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALVPVC-KTIKEFPPG 178
 
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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