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Conserved domains on  [gi|1002266221|ref|XP_015637440|]
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gamma-glutamyl hydrolase 2 [Oryza sativa Japonica Group]

Protein Classification

GATase1_Glutamyl_Hydrolase domain-containing protein( domain architecture ID 10109835)

GATase1_Glutamyl_Hydrolase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 52-324 7.57e-148

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: 417.11  E-value: 7.57e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221  52 IGIVSHPGDGAGgrvSNGTAASYIAASYVKFVESAGARVVPLIYNEPEERLLEKLSLVNGVLFTGGSV--KSGPYFETIK 129
Cdd:cd01747     1 IGILTQPVDGAG---SNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVdiDTSGYARTAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221 130 KVFQYVLDKNDAGIPFPLFAQCLGFELVSMIVSKDNNILESFSATNQASTLQFPNYSsLEGSVFERFDPDLIKKLSTSCL 209
Cdd:cd01747    78 IIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDA-LQSRLFKRFPPDLLKSLATEPL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221 210 VMQNHKYGISPKTLRENVALSSFFKILTTSPDENGEVYVSTVQANKYPITCTQWHPEKAIFEFGKQ-MIPHSEEAVQVTQ 288
Cdd:cd01747   157 TMNNHRYGISPENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSsSIPHSEEAIRLTQ 236

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1002266221 289 NFANYFISQARKSQNRPPADKVLDN-LIYNYSPTFIG 324
Cdd:cd01747   237 YFANFFVNEARKSNNRFESAEEETKhLIYNYKPTYTG 273
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 52-324 7.57e-148

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: 417.11  E-value: 7.57e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221  52 IGIVSHPGDGAGgrvSNGTAASYIAASYVKFVESAGARVVPLIYNEPEERLLEKLSLVNGVLFTGGSV--KSGPYFETIK 129
Cdd:cd01747     1 IGILTQPVDGAG---SNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVdiDTSGYARTAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221 130 KVFQYVLDKNDAGIPFPLFAQCLGFELVSMIVSKDNNILESFSATNQASTLQFPNYSsLEGSVFERFDPDLIKKLSTSCL 209
Cdd:cd01747    78 IIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDA-LQSRLFKRFPPDLLKSLATEPL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221 210 VMQNHKYGISPKTLRENVALSSFFKILTTSPDENGEVYVSTVQANKYPITCTQWHPEKAIFEFGKQ-MIPHSEEAVQVTQ 288
Cdd:cd01747   157 TMNNHRYGISPENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSsSIPHSEEAIRLTQ 236

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1002266221 289 NFANYFISQARKSQNRPPADKVLDN-LIYNYSPTFIG 324
Cdd:cd01747   237 YFANFFVNEARKSNNRFESAEEETKhLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 50-157 2.21e-13

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: 68.44  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221  50 PVIGIVSHPgDGAGGRVSNGTAASYIAASYVKFVESAGARVVPLIYNEPEERLLEKLSLVNGVLFTGG------------ 117
Cdd:pfam07722   1 PVIGITANE-ESLGGHVFHGAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGpnvdphfygeep 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002266221 118 SVKSGPYF----ETIKKVFQYVLDKNdagipFPLFAQCLGFELV 157
Cdd:pfam07722  80 SESGGPYDpardAYELALIRAALARG-----KPILGICRGFQLL 118
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 52-324 7.57e-148

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: 417.11  E-value: 7.57e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221  52 IGIVSHPGDGAGgrvSNGTAASYIAASYVKFVESAGARVVPLIYNEPEERLLEKLSLVNGVLFTGGSV--KSGPYFETIK 129
Cdd:cd01747     1 IGILTQPVDGAG---SNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVdiDTSGYARTAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221 130 KVFQYVLDKNDAGIPFPLFAQCLGFELVSMIVSKDNNILESFSATNQASTLQFPNYSsLEGSVFERFDPDLIKKLSTSCL 209
Cdd:cd01747    78 IIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDA-LQSRLFKRFPPDLLKSLATEPL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221 210 VMQNHKYGISPKTLRENVALSSFFKILTTSPDENGEVYVSTVQANKYPITCTQWHPEKAIFEFGKQ-MIPHSEEAVQVTQ 288
Cdd:cd01747   157 TMNNHRYGISPENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSsSIPHSEEAIRLTQ 236

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1002266221 289 NFANYFISQARKSQNRPPADKVLDN-LIYNYSPTFIG 324
Cdd:cd01747   237 YFANFFVNEARKSNNRFESAEEETKhLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 50-157 2.21e-13

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: 68.44  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221  50 PVIGIVSHPgDGAGGRVSNGTAASYIAASYVKFVESAGARVVPLIYNEPEERLLEKLSLVNGVLFTGG------------ 117
Cdd:pfam07722   1 PVIGITANE-ESLGGHVFHGAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGpnvdphfygeep 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002266221 118 SVKSGPYF----ETIKKVFQYVLDKNdagipFPLFAQCLGFELV 157
Cdd:pfam07722  80 SESGGPYDpardAYELALIRAALARG-----KPILGICRGFQLL 118
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 52-126 8.75e-06

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: 45.64  E-value: 8.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002266221  52 IGIVSHPGDGAGGrvsnGTAASYIAASYVKFVESAGARVVPLIYNEPEERLLEKLSLVNGVLFTGG-SVKSGPYFE 126
Cdd:cd01745     1 IGITARLREEEGG----YERRDYLNQYYVDAVRKAGGLPVLLPPVDDEEDLEQYLELLDGLLLTGGgDVDPPLYGE 72
GATase pfam00117
Glutamine amidotransferase class-I;
90-277 4.58e-05

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 43.38  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221  90 VVPliYNEPEERLLEKLslVNGVLFTGG--SVKSGPY-FETIKKVFqyvldknDAGIPFplFAQCLGFELvsmivskdnn 166
Cdd:pfam00117  26 VVP--NDTPAEEILEEN--PDGIILSGGpgSPGAAGGaIEAIREAR-------ELKIPI--LGICLGHQL---------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221 167 ILESFSAT--------NQASTLQFPNYSSlegSVFERFDPDLIkklstsclVMQNHKYGISPKTLRENvalssfFKILTT 238
Cdd:pfam00117  83 LALAFGGKvvkakkfgHHGKNSPVGDDGC---GLFYGLPNVFI--------VRRYHSYAVDPDTLPDG------LEVTAT 145

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002266221 239 SpdENGEVYVStVQANKYPITCTQWHPEKAIFEFGKQMI 277
Cdd:pfam00117 146 S--ENDGTIMG-IRHKKLPIFGVQFHPESILTPHGPEIL 181
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 66-156 7.84e-04

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: 37.95  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221  66 VSNGTAASYIAASYVKFVESAGARVVPLIYNEPEERLLEKLSLVNGVLFTGGSVkSGPYFETIKKVFQYVLDKNDAGIpf 145
Cdd:cd03128     4 LLFGGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPG-TPDDLAWDEALLALLREAAAAGK-- 80

                          90
                  ....*....|.
gi 1002266221 146 PLFAQCLGFEL 156
Cdd:cd03128    81 PVLGICLGAQL 91
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 66-156 9.69e-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: 9.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266221  66 VSNGTAASYIAASYVKFVESAGARVVPLIYNEPEERLLEKLSLVNGVLFTGGSVkSGPYFETIKKVFQYVLDKNDAGIpf 145
Cdd:cd01653     4 LLFPGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPG-TPDDLARDEALLALLREAAAAGK-- 80

                          90
                  ....*....|.
gi 1002266221 146 PLFAQCLGFEL 156
Cdd:cd01653    81 PILGICLGAQL 91
 
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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