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Conserved domains on  [gi|15219153|ref|NP_177988|]
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gamma-glutamyl hydrolase 3 [Arabidopsis thaliana]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 60-339 1.84e-133

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.


The actual alignment was detected with superfamily member cd01747:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 273  Bit Score: 381.28  E-value: 1.84e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153  60 IGILTHPGegrwdarlHSLKNYAYATniSYIAASYVKLAETGGARVIPLIYNEPEEILFQKLELVNGVIFTGGWA--KTG 137
Cdd:cd01747   1 IGILTQPV--------DGAGSNKTGH--SYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVdiDTS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153 138 LYYDVVEKIFNKVMEKNDAGEHFPVYAMCLGFEILSMIISQNRDILERFNSVNYASSLQFfKNVNIEATVFQRFPPELLK 217
Cdd:cd01747  71 GYARTAKIIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNF-TEDALQSRLFKRFPPDLLK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153 218 KLSADCLVMQNHYFGISPDNFQGNPYLSSFFNIVTTSADKDSKTFVSTIRSKRYPVTAFQWHPEKNAFEWGSSE-IPHSE 296
Cdd:cd01747 150 SLATEPLTMNNHRYGISPENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSsIPHSE 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15219153 297 DAIQVTQHAANYLVSEARKSMNRPSSEKVLSN-LIYNYKPTYSG 339
Cdd:cd01747 230 EAIRLTQYFANFFVNEARKSNNRFESAEEETKhLIYNYKPTYTG 273
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 60-339 1.84e-133

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 381.28  E-value: 1.84e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153  60 IGILTHPGegrwdarlHSLKNYAYATniSYIAASYVKLAETGGARVIPLIYNEPEEILFQKLELVNGVIFTGGWA--KTG 137
Cdd:cd01747   1 IGILTQPV--------DGAGSNKTGH--SYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVdiDTS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153 138 LYYDVVEKIFNKVMEKNDAGEHFPVYAMCLGFEILSMIISQNRDILERFNSVNYASSLQFfKNVNIEATVFQRFPPELLK 217
Cdd:cd01747  71 GYARTAKIIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNF-TEDALQSRLFKRFPPDLLK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153 218 KLSADCLVMQNHYFGISPDNFQGNPYLSSFFNIVTTSADKDSKTFVSTIRSKRYPVTAFQWHPEKNAFEWGSSE-IPHSE 296
Cdd:cd01747 150 SLATEPLTMNNHRYGISPENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSsIPHSE 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15219153 297 DAIQVTQHAANYLVSEARKSMNRPSSEKVLSN-LIYNYKPTYSG 339
Cdd:cd01747 230 EAIRLTQYFANFFVNEARKSNNRFESAEEETKhLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 58-172 9.30e-10

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 58.04  E-value: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153    58 PVIGILthpgegrwdARLHSLKNYAYATNI-SYIAASYVKLAETGGARVIPLIYNEPEEILFQKLELVNGVIFTGG---- 132
Cdd:pfam07722   1 PVIGIT---------ANEESLGGHVFHGAGeSYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGpnvd 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 15219153   133 ----WA----KTGlYYDVVEKIFNKVMEKNDAGEHFPVYAMCLGFEIL 172
Cdd:pfam07722  72 phfyGEepseSGG-PYDPARDAYELALIRAALARGKPILGICRGFQLL 118
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 60-339 1.84e-133

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 381.28  E-value: 1.84e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153  60 IGILTHPGegrwdarlHSLKNYAYATniSYIAASYVKLAETGGARVIPLIYNEPEEILFQKLELVNGVIFTGGWA--KTG 137
Cdd:cd01747   1 IGILTQPV--------DGAGSNKTGH--SYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVdiDTS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153 138 LYYDVVEKIFNKVMEKNDAGEHFPVYAMCLGFEILSMIISQNRDILERFNSVNYASSLQFfKNVNIEATVFQRFPPELLK 217
Cdd:cd01747  71 GYARTAKIIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNF-TEDALQSRLFKRFPPDLLK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153 218 KLSADCLVMQNHYFGISPDNFQGNPYLSSFFNIVTTSADKDSKTFVSTIRSKRYPVTAFQWHPEKNAFEWGSSE-IPHSE 296
Cdd:cd01747 150 SLATEPLTMNNHRYGISPENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSsIPHSE 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15219153 297 DAIQVTQHAANYLVSEARKSMNRPSSEKVLSN-LIYNYKPTYSG 339
Cdd:cd01747 230 EAIRLTQYFANFFVNEARKSNNRFESAEEETKhLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 58-172 9.30e-10

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 58.04  E-value: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153    58 PVIGILthpgegrwdARLHSLKNYAYATNI-SYIAASYVKLAETGGARVIPLIYNEPEEILFQKLELVNGVIFTGG---- 132
Cdd:pfam07722   1 PVIGIT---------ANEESLGGHVFHGAGeSYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGpnvd 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 15219153   133 ----WA----KTGlYYDVVEKIFNKVMEKNDAGEHFPVYAMCLGFEIL 172
Cdd:pfam07722  72 phfyGEepseSGG-PYDPARDAYELALIRAALARGKPILGICRGFQLL 118
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 83-132 9.01e-03

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: 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. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 36.78  E-value: 9.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15219153  83 YATNISYIAASYVKLAETGGARVIPLIYNEPEEILFQKLELVNGVIFTGG 132
Cdd:cd01745  13 GYERRDYLNQYYVDAVRKAGGLPVLLPPVDDEEDLEQYLELLDGLLLTGG 62
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 91-172 9.57e-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: 35.25  E-value: 9.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219153  91 AASYVKLAETGGARVIPLIYNEPEEILFQKLELVNGVIFTGGWAkTGLYYDVVEKIFNKVMEKNDAGehFPVYAMCLGFE 170
Cdd:cd03128  14 LASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPG-TPDDLAWDEALLALLREAAAAG--KPVLGICLGAQ 90


                ..
gi 15219153 171 IL 172
Cdd:cd03128  91 LL 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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