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Conserved domains on  [gi|24665099|ref|NP_730119|]
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lethal (3) 72Dp [Drosophila melanogaster]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 10109835)

type 1 glutamine amidotransferase (GATase1) family 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 ...
 28-303 2.54e-151

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: 427.51  E-value: 2.54e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  28 IGVLTQEVYVDGlisrHFDNKTSYIAASYVKYLEGAGARVVPIWIGRNRSYYDDLMRKINGVLLPGGATWFNqSNGYADA 107
Cdd:cd01747   1 IGILTQPVDGAG----SNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDID-TSGYART 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 108 GEHLIHLAIELNDQGVFMPVWGTCLGMELLVYKLANETEHRINCEATGMAVPMEFKEDYKKSRLFASITDDVVDTMVKEN 187
Cdd:cd01747  76 AKIIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDALQSRLFKRFPPDLLKSLATEP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 188 VTYHWHQFCYT-EKDFERDLLNETWRVMSLNHDWNGVEFISTVEHIKYPFYGVQFHPEKPLYEFTKTS-IPHTAAAVLSG 265
Cdd:cd01747 156 LTMNNHRYGISpENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSsIPHSEEAIRLT 235

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 24665099 266 QFFADFFVSEARESNQSFSNATEQARTLIYNYKPEYTS 303
Cdd:cd01747 236 QYFANFFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 28-303 2.54e-151

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: 427.51  E-value: 2.54e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  28 IGVLTQEVYVDGlisrHFDNKTSYIAASYVKYLEGAGARVVPIWIGRNRSYYDDLMRKINGVLLPGGATWFNqSNGYADA 107
Cdd:cd01747   1 IGILTQPVDGAG----SNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDID-TSGYART 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 108 GEHLIHLAIELNDQGVFMPVWGTCLGMELLVYKLANETEHRINCEATGMAVPMEFKEDYKKSRLFASITDDVVDTMVKEN 187
Cdd:cd01747  76 AKIIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDALQSRLFKRFPPDLLKSLATEP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 188 VTYHWHQFCYT-EKDFERDLLNETWRVMSLNHDWNGVEFISTVEHIKYPFYGVQFHPEKPLYEFTKTS-IPHTAAAVLSG 265
Cdd:cd01747 156 LTMNNHRYGISpENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSsIPHSEEAIRLT 235

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 24665099 266 QFFADFFVSEARESNQSFSNATEQARTLIYNYKPEYTS 303
Cdd:cd01747 236 QYFANFFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 26-244 2.75e-30

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: 115.43  E-value: 2.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099    26 PIIGVLTQEVYVDGLiSRHfDNKTSYIAASYVKYLEGAGARVVPIWIGRNRSYYDDLMRKINGVLLPGGAT------WFN 99
Cdd:pfam07722   1 PVIGITANEESLGGH-VFH-GAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGPNvdphfyGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099   100 --QSNGYADAGEH-----LIHLAIELNdqgvfMPVWGTCLGMELL-----------VYKLANETEHRINC----EATGMA 157
Cdd:pfam07722  79 psESGGPYDPARDayelaLIRAALARG-----KPILGICRGFQLLnvalggtlyqdIQEQPGFTDHREHCqvapYAPSHA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099   158 VPMEfkedykKSRLFASITDdvvDTMVKENvTYHwHQFCytekdferDLLNETWRVMSLNhDWNGVEFISTVEHiKYPFY 237
Cdd:pfam07722 154 VNVE------PGSLLASLLG---SEEFRVN-SLH-HQAI--------DRLAPGLRVEAVA-PDGTIEAIESPNA-KGFAL 212


                  ....*..
gi 24665099   238 GVQFHPE 244
Cdd:pfam07722 213 GVQWHPE 219
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 60-245 1.06e-05

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 45.80  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  60 LEGAGARVVpiwIGRNRsyydDLMRKINGVLLPG-GAtwfnqsngYADAGEHL--------IHLAIELNdqgvfMPVWGT 130
Cdd:COG0118  20 LERLGAEVV---VTSDP----DEIRAADRLVLPGvGA--------FGDAMENLrergldeaIREAVAGG-----KPVLGI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 131 CLGMELLvyklANETE---------------HRIncEATGMAVP-M-----EFKEDykkSRLFASITDDvvdtmvkENVt 189
Cdd:COG0118  80 CLGMQLL----FERSEengdteglglipgevVRF--PASDLKVPhMgwntvEIAKD---HPLFAGIPDG-------EYF- 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24665099 190 YHWHQFcYTEKDFERDLLNETwrvmslNHdwnGVEFISTVEhiKYPFYGVQFHPEK 245
Cdd:COG0118 143 YFVHSY-YVPPDDPEDVVATT------DY---GVPFTAAVE--RGNVFGTQFHPEK 186
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 89-245 2.33e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 38.69  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099   89 VLLPG-GAtwFNQ------SNGYADAGEHLIhlaielnDQGVfmPVWGTCLGMELLvyklANETEH-RINC--------- 151
Cdd:PRK13181  41 VILPGvGA--FGQamrslrESGLDEALKEHV-------EKKQ--PVLGICLGMQLL----FESSEEgNVKGlglipgdvk 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  152 --EATGMAVP-MEFKE--DYKKSRLFASITDdvvdtmvkENVTYHWHQFcYTEKDFERDLLNETWRvmslnhdwnGVEFI 226
Cdd:PRK13181 106 rfRSEPLKVPqMGWNSvkPLKESPLFKGIEE--------GSYFYFVHSY-YVPCEDPEDVLATTEY---------GVPFC 167

                        170
                 ....*....|....*....
gi 24665099  227 STVEhiKYPFYGVQFHPEK 245
Cdd:PRK13181 168 SAVA--KDNIYAVQFHPEK 184
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 28-303 2.54e-151

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: 427.51  E-value: 2.54e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  28 IGVLTQEVYVDGlisrHFDNKTSYIAASYVKYLEGAGARVVPIWIGRNRSYYDDLMRKINGVLLPGGATWFNqSNGYADA 107
Cdd:cd01747   1 IGILTQPVDGAG----SNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDID-TSGYART 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 108 GEHLIHLAIELNDQGVFMPVWGTCLGMELLVYKLANETEHRINCEATGMAVPMEFKEDYKKSRLFASITDDVVDTMVKEN 187
Cdd:cd01747  76 AKIIYNLALERNDAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDALQSRLFKRFPPDLLKSLATEP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 188 VTYHWHQFCYT-EKDFERDLLNETWRVMSLNHDWNGVEFISTVEHIKYPFYGVQFHPEKPLYEFTKTS-IPHTAAAVLSG 265
Cdd:cd01747 156 LTMNNHRYGISpENFTENGLLSDFFNVLTTNDDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSsIPHSEEAIRLT 235

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 24665099 266 QFFADFFVSEARESNQSFSNATEQARTLIYNYKPEYTS 303
Cdd:cd01747 236 QYFANFFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 26-244 2.75e-30

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: 115.43  E-value: 2.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099    26 PIIGVLTQEVYVDGLiSRHfDNKTSYIAASYVKYLEGAGARVVPIWIGRNRSYYDDLMRKINGVLLPGGAT------WFN 99
Cdd:pfam07722   1 PVIGITANEESLGGH-VFH-GAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGPNvdphfyGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099   100 --QSNGYADAGEH-----LIHLAIELNdqgvfMPVWGTCLGMELL-----------VYKLANETEHRINC----EATGMA 157
Cdd:pfam07722  79 psESGGPYDPARDayelaLIRAALARG-----KPILGICRGFQLLnvalggtlyqdIQEQPGFTDHREHCqvapYAPSHA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099   158 VPMEfkedykKSRLFASITDdvvDTMVKENvTYHwHQFCytekdferDLLNETWRVMSLNhDWNGVEFISTVEHiKYPFY 237
Cdd:pfam07722 154 VNVE------PGSLLASLLG---SEEFRVN-SLH-HQAI--------DRLAPGLRVEAVA-PDGTIEAIESPNA-KGFAL 212


                  ....*..
gi 24665099   238 GVQFHPE 244
Cdd:pfam07722 213 GVQWHPE 219
GATase pfam00117
Glutamine amidotransferase class-I;
85-245 3.33e-09

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 55.71  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099    85 KINGVLLPGGAtwfnqsnGYADAGEHLIHLAIELNDQGVfmPVWGTCLGMELLVYKLANETehrinceatgmaVPMEFKE 164
Cdd:pfam00117  40 NPDGIILSGGP-------GSPGAAGGAIEAIREARELKI--PILGICLGHQLLALAFGGKV------------VKAKKFG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099   165 D-YKKSRLFASITDDVVDTmVKENVTYHWHQFCytekdFERDLLNETWRVMSLNHDWNGVEFIstvEHIKYPFYGVQFHP 243
Cdd:pfam00117  99 HhGKNSPVGDDGCGLFYGL-PNVFIVRRYHSYA-----VDPDTLPDGLEVTATSENDGTIMGI---RHKKLPIFGVQFHP 169


                  ..
gi 24665099   244 EK 245
Cdd:pfam00117 170 ES 171
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 45-139 5.34e-08

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: 50.67  E-value: 5.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  45 FDNKTSYIAASYVKYLEGAGARVVPIWIGRNRSYYDDLMRKINGVLLPGGAtwfnQSNGYADAGEHLIHLAIELNDQGVf 124
Cdd:cd01653   6 FPGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGP----GTPDDLARDEALLALLREAAAAGK- 80

                        90
                ....*....|....*
gi 24665099 125 mPVWGTCLGMELLVY 139
Cdd:cd01653  81 -PILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 45-137 1.78e-07

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: 48.74  E-value: 1.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  45 FDNKTSYIAASYVKYLEGAGARVVPIWIGRNRSYYDDLMRKINGVLLPGGATWFNqsngYADAGEHLIHLAIELNDQGVf 124
Cdd:cd03128   6 FGGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPD----DLAWDEALLALLREAAAAGK- 80

                        90
                ....*....|...
gi 24665099 125 mPVWGTCLGMELL 137
Cdd:cd03128  81 -PVLGICLGAQLL 92
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 28-137 9.23e-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: 9.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  28 IGVLTQEVYVDGLISRHfdnktSYIAASYVKYLEGAGARVVPIWIGRNRSYYDDLMRKINGVLLPGGATwFNQSNGYA-- 105
Cdd:cd01745   1 IGITARLREEEGGYERR-----DYLNQYYVDAVRKAGGLPVLLPPVDDEEDLEQYLELLDGLLLTGGGD-VDPPLYGEep 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 24665099 106 -----------DAGE-HLIHLAIELNdqgvfMPVWGTCLGMELL 137
Cdd:cd01745  75 hpelgpidperDAFElALLRAALERG-----KPILGICRGMQLL 113
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 60-245 1.06e-05

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 45.80  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  60 LEGAGARVVpiwIGRNRsyydDLMRKINGVLLPG-GAtwfnqsngYADAGEHL--------IHLAIELNdqgvfMPVWGT 130
Cdd:COG0118  20 LERLGAEVV---VTSDP----DEIRAADRLVLPGvGA--------FGDAMENLrergldeaIREAVAGG-----KPVLGI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 131 CLGMELLvyklANETE---------------HRIncEATGMAVP-M-----EFKEDykkSRLFASITDDvvdtmvkENVt 189
Cdd:COG0118  80 CLGMQLL----FERSEengdteglglipgevVRF--PASDLKVPhMgwntvEIAKD---HPLFAGIPDG-------EYF- 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24665099 190 YHWHQFcYTEKDFERDLLNETwrvmslNHdwnGVEFISTVEhiKYPFYGVQFHPEK 245
Cdd:COG0118 143 YFVHSY-YVPPDDPEDVVATT------DY---GVPFTAAVE--RGNVFGTQFHPEK 186
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 46-244 1.04e-04

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 42.52  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  46 DNKTSYiaaSY--VKYLEGAGARVVPIwigRNRSYYDDLMRKIN--GVLL-PG-GATwfnqsngyADAGEHLIhlAIELN 119
Cdd:cd01743   5 DNYDSF---TYnlVQYLRELGAEVVVV---RNDEITLEELELLNpdAIVIsPGpGHP--------EDAGISLE--IIRAL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 120 DQGVfmPVWGTCLGMELLVY------KLANETEHrinceatGMAVPMEFKedykKSRLFASITDDVvdtmvkeNVT-YH- 191
Cdd:cd01743  69 AGKV--PILGVCLGHQAIAEafggkvVRAPEPMH-------GKTSEIHHD----GSGLFKGLPQPF-------TVGrYHs 128

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 24665099 192 WHqfcytekdFERDLLNETWRVMSLNHDwnGVefISTVEHIKYPFYGVQFHPE 244
Cdd:cd01743 129 LV--------VDPDPLPDLLEVTASTED--GV--IMALRHRDLPIYGVQFHPE 169
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 39-244 1.93e-04

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 42.54  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  39 GLISRHFDNKTSYIaaSYVKYLEGAGA----RVVPIWI---GRNRSYYDDLMRKINGVLLPGGAtwfnqsnGYADAgEHL 111
Cdd:cd01746   4 ALVGKYVELPDAYL--SVLEALKHAGIalgvKLEIKWIdseDLEEENAEEALKGADGILVPGGF-------GIRGV-EGK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099 112 IhLAIE---LNDqgvfMPVWGTCLGMELLV---------YKLANETEHRINCEATGMAVPMEFKEDYKK---SRLFASIT 176
Cdd:cd01746  74 I-LAIKyarENN----IPFLGICLGMQLAViefarnvlgLPDANSTEFDPDTPHPVVDLMPEQKGVKDLggtMRLGAYPV 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24665099 177 DDVVDTMVKE----NVTY--HWHQFcytE--KDFERDLLNETWRVMSLNHDWNGVEfisTVEHIKYPFY-GVQFHPE 244
Cdd:cd01746 149 ILKPGTLAHKyygkDEVEerHRHRY---EvnPEYVDELEEAGLRFSGTDPDGGLVE---IVELPDHPFFvGTQFHPE 219
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 229-244 8.28e-04

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 40.02  E-value: 8.28e-04
                        10
                ....*....|....*.
gi 24665099 229 VEHIKYPFYGVQFHPE 244
Cdd:COG0512 154 IRHRELPIEGVQFHPE 169
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 89-245 2.33e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 38.69  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099   89 VLLPG-GAtwFNQ------SNGYADAGEHLIhlaielnDQGVfmPVWGTCLGMELLvyklANETEH-RINC--------- 151
Cdd:PRK13181  41 VILPGvGA--FGQamrslrESGLDEALKEHV-------EKKQ--PVLGICLGMQLL----FESSEEgNVKGlglipgdvk 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099  152 --EATGMAVP-MEFKE--DYKKSRLFASITDdvvdtmvkENVTYHWHQFcYTEKDFERDLLNETWRvmslnhdwnGVEFI 226
Cdd:PRK13181 106 rfRSEPLKVPqMGWNSvkPLKESPLFKGIEE--------GSYFYFVHSY-YVPCEDPEDVLATTEY---------GVPFC 167

                        170
                 ....*....|....*....
gi 24665099  227 STVEhiKYPFYGVQFHPEK 245
Cdd:PRK13181 168 SAVA--KDNIYAVQFHPEK 184
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 215-244 2.44e-03

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 38.63  E-value: 2.44e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 24665099 215 SLNHDWNgVEFIS----TVE---HIKYPFYGVQFHPE 244
Cdd:cd01744 127 SLPGGLE-VTHVNlndgTVEgirHKDLPVFSVQFHPE 162
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
60-151 9.58e-03

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 36.68  E-value: 9.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665099   60 LEGAGARVVPIwigRNRsyyDDLmRKINGVLLPGG--ATwfnqsngyadagehLIHLaieLNDQGVF----------MPV 127
Cdd:PRK13525  20 LEALGAEAVEV---RRP---EDL-DEIDGLILPGGesTT--------------MGKL---LRDFGLLeplrefiasgLPV 75

                         90       100
                 ....*....|....*....|....
gi 24665099  128 WGTCLGMELLVYKLANETEHRINC 151
Cdd:PRK13525  76 FGTCAGMILLAKEIEGYEQEHLGL 99
 
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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