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Conserved domains on  [gi|556300243|ref|WP_023292584|]
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MULTISPECIES: gamma-glutamyl-gamma-aminobutyrate hydrolase [Enterobacter]

Protein Classification

gamma-glutamyl-gamma-aminobutyrate hydrolase( domain architecture ID 11485326)

gamma-glutamyl-gamma-aminobutyrate hydrolase catalyzes the hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate, an important step in putrescine degradation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 1-254 0e+00

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


:

Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 517.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   1 MENIMNKPVIGVVMCRNRLKGHETQTLQEKYLNAIINAGGLPIALPHALAEPELLTALLPTLDGIYLPGSPSNVQPHLYG 80
Cdd:PRK11366   1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  81 ENGDEPDADPGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFEQNDLLEHREDPELPVELQYAPSHEVQ 160
Cdd:PRK11366  81 ENGDEPDADPGRDLLSMALINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 161 VQEGGLLSQLIPGCNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFALGVQWHPEWNSSEYALSRMLFEGF 240
Cdd:PRK11366 161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240

                        250
                 ....*....|....
gi 556300243 241 ITACQSHIAEKQRL 254
Cdd:PRK11366 241 ITACQHHIAEKQRL 254
 
Name Accession Description Interval E-value
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 1-254 0e+00

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 517.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   1 MENIMNKPVIGVVMCRNRLKGHETQTLQEKYLNAIINAGGLPIALPHALAEPELLTALLPTLDGIYLPGSPSNVQPHLYG 80
Cdd:PRK11366   1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  81 ENGDEPDADPGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFEQNDLLEHREDPELPVELQYAPSHEVQ 160
Cdd:PRK11366  81 ENGDEPDADPGRDLLSMALINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 161 VQEGGLLSQLIPGCNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFALGVQWHPEWNSSEYALSRMLFEGF 240
Cdd:PRK11366 161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240

                        250
                 ....*....|....
gi 556300243 241 ITACQSHIAEKQRL 254
Cdd:PRK11366 241 ITACQHHIAEKQRL 254
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 12-247 9.28e-97

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 282.83  E-value: 9.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  12 VVMCRNRLKGHETQTLQEKYLNAIINAGGLPIALPHaLAEPELLTALLPTLDGIYLPGSPsNVQPHLYGENGDEP--DAD 89
Cdd:COG2071    1 ITADLRTAGGYPAHYLPEDYVRAVRAAGGLPVLLPP-VGDEEDLDELLDRLDGLVLTGGA-DVDPALYGEEPHPElgPID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  90 PGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFEQND-LLEHREDpelpvELQYAPSHEVQVQEGGLLS 168
Cdd:COG2071   79 PERDAFELALIRAALERGKPVLGICRGMQLLNVALGGTLYQDLPDQVPgALDHRQP-----APRYAPRHTVEIEPGSRLA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556300243 169 QLIpGCNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFALGVQWHPEWNSSEYALSRMLFEGFITACQSH 247
Cdd:COG2071  154 RIL-GEEEIRVNSLHHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWLAASDPLSRRLFEAFVEAARAR 231
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 8-224 2.80e-91

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: 268.36  E-value: 2.80e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243    8 PVIGVVMCRNRLKGHETQTLQEKYLNA-----IINAGGLPIALPhALAEPELLTALLPTLDGIYLPGSPsNVQPHLYGEN 82
Cdd:pfam07722   1 PVIGITANEESLGGHVFHGAGESYLAAgyveaVEGAGGLPVLLP-ILGDPEDAAAILDRLDGLLLTGGP-NVDPHFYGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   83 GDE--PDADPGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFEQNDLLEHREDpelPVELQYAPSHEVQ 160
Cdd:pfam07722  79 PSEsgGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREH---CQVAPYAPSHAVN 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556300243  161 VQEGGLLSQlIPGCNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHP-FALGVQWHPE 224
Cdd:pfam07722 156 VEPGSLLAS-LLGSEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKgFALGVQWHPE 219
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 10-241 3.24e-67

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: 206.27  E-value: 3.24e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  10 IGVVMCRNRLKGH--ETQTLQEKYLNAIINAGGLPIALPHALAEpELLTALLPTLDGIYLPGSPSNVQPHLYGENGDEPD 87
Cdd:cd01745    1 IGITARLREEEGGyeRRDYLNQYYVDAVRKAGGLPVLLPPVDDE-EDLEQYLELLDGLLLTGGGDVDPPLYGEEPHPELG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  88 A-DPGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLfeqndllehredpelpvelqyapshevqvqeggl 166
Cdd:cd01745   80 PiDPERDAFELALLRAALERGKPILGICRGMQLLNVALGGTLYQDI---------------------------------- 125

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556300243 167 lsqlipgcntfWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFALGVQWHPEWNSSEYALSRMLFEGFI 241
Cdd:cd01745  126 -----------RVNSLHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLADTDPDSLKLFEAFV 189
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 64-241 6.11e-10

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 56.94  E-value: 6.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   64 GIYLPGSPSNVqphlYGENGDEPDAdpgrdllsmaliaAALERRIPIFAICRGLQELVVATGGTLYRRlfeqndllEHRE 143
Cdd:TIGR00888  44 GIILSGGPSSV----YAENAPRADE-------------KIFELGVPVLGICYGMQLMAKQLGGEVGRA--------EKRE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  144 dpelpvelqYAPShEVQVQEGGLLSQLIPGCNTFWVNslHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFAlGVQWHP 223
Cdd:TIGR00888  99 ---------YGKA-ELEILDEDDLFRGLPDESTVWMS--HGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIY-GVQFHP 165

                         170
                  ....*....|....*...
gi 556300243  224 EWNSSEYALSrmLFEGFI 241
Cdd:TIGR00888 166 EVTHTEYGNE--LLENFV 181
 
Name Accession Description Interval E-value
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 1-254 0e+00

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 517.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   1 MENIMNKPVIGVVMCRNRLKGHETQTLQEKYLNAIINAGGLPIALPHALAEPELLTALLPTLDGIYLPGSPSNVQPHLYG 80
Cdd:PRK11366   1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  81 ENGDEPDADPGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFEQNDLLEHREDPELPVELQYAPSHEVQ 160
Cdd:PRK11366  81 ENGDEPDADPGRDLLSMALINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 161 VQEGGLLSQLIPGCNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFALGVQWHPEWNSSEYALSRMLFEGF 240
Cdd:PRK11366 161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240

                        250
                 ....*....|....
gi 556300243 241 ITACQSHIAEKQRL 254
Cdd:PRK11366 241 ITACQHHIAEKQRL 254
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 12-247 9.28e-97

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 282.83  E-value: 9.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  12 VVMCRNRLKGHETQTLQEKYLNAIINAGGLPIALPHaLAEPELLTALLPTLDGIYLPGSPsNVQPHLYGENGDEP--DAD 89
Cdd:COG2071    1 ITADLRTAGGYPAHYLPEDYVRAVRAAGGLPVLLPP-VGDEEDLDELLDRLDGLVLTGGA-DVDPALYGEEPHPElgPID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  90 PGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFEQND-LLEHREDpelpvELQYAPSHEVQVQEGGLLS 168
Cdd:COG2071   79 PERDAFELALIRAALERGKPVLGICRGMQLLNVALGGTLYQDLPDQVPgALDHRQP-----APRYAPRHTVEIEPGSRLA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556300243 169 QLIpGCNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFALGVQWHPEWNSSEYALSRMLFEGFITACQSH 247
Cdd:COG2071  154 RIL-GEEEIRVNSLHHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWLAASDPLSRRLFEAFVEAARAR 231
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 8-224 2.80e-91

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: 268.36  E-value: 2.80e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243    8 PVIGVVMCRNRLKGHETQTLQEKYLNA-----IINAGGLPIALPhALAEPELLTALLPTLDGIYLPGSPsNVQPHLYGEN 82
Cdd:pfam07722   1 PVIGITANEESLGGHVFHGAGESYLAAgyveaVEGAGGLPVLLP-ILGDPEDAAAILDRLDGLLLTGGP-NVDPHFYGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   83 GDE--PDADPGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFEQNDLLEHREDpelPVELQYAPSHEVQ 160
Cdd:pfam07722  79 PSEsgGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREH---CQVAPYAPSHAVN 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556300243  161 VQEGGLLSQlIPGCNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHP-FALGVQWHPE 224
Cdd:pfam07722 156 VEPGSLLAS-LLGSEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKgFALGVQWHPE 219
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 10-241 3.24e-67

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: 206.27  E-value: 3.24e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  10 IGVVMCRNRLKGH--ETQTLQEKYLNAIINAGGLPIALPHALAEpELLTALLPTLDGIYLPGSPSNVQPHLYGENGDEPD 87
Cdd:cd01745    1 IGITARLREEEGGyeRRDYLNQYYVDAVRKAGGLPVLLPPVDDE-EDLEQYLELLDGLLLTGGGDVDPPLYGEEPHPELG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  88 A-DPGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLfeqndllehredpelpvelqyapshevqvqeggl 166
Cdd:cd01745   80 PiDPERDAFELALLRAALERGKPILGICRGMQLLNVALGGTLYQDI---------------------------------- 125

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556300243 167 lsqlipgcntfWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFALGVQWHPEWNSSEYALSRMLFEGFI 241
Cdd:cd01745  126 -----------RVNSLHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLADTDPDSLKLFEAFV 189
PRK13566 PRK13566
anthranilate synthase component I;
90-224 1.86e-12

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 66.48  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  90 PGR--DLLSMALIAAALERRIPIFAICRGLQELVVATGGTLyrrlfeqnDLLEHredpelpvelqyaPSH----EVQVQE 163
Cdd:PRK13566 579 PGRpsDFDCKATIDAALARNLPIFGVCLGLQAIVEAFGGEL--------GQLAY-------------PMHgkpsRIRVRG 637

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556300243 164 GGLLSQLIPgcNTFWV---NSLHGQgARTLGPRLRVEARSTDGLVEAVSVHDHPFAlGVQWHPE 224
Cdd:PRK13566 638 PGRLFSGLP--EEFTVgryHSLFAD-PETLPDELLVTAETEDGVIMAIEHKTLPVA-AVQFHPE 697
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 64-241 6.11e-10

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 56.94  E-value: 6.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   64 GIYLPGSPSNVqphlYGENGDEPDAdpgrdllsmaliaAALERRIPIFAICRGLQELVVATGGTLYRRlfeqndllEHRE 143
Cdd:TIGR00888  44 GIILSGGPSSV----YAENAPRADE-------------KIFELGVPVLGICYGMQLMAKQLGGEVGRA--------EKRE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  144 dpelpvelqYAPShEVQVQEGGLLSQLIPGCNTFWVNslHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFAlGVQWHP 223
Cdd:TIGR00888  99 ---------YGKA-ELEILDEDDLFRGLPDESTVWMS--HGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIY-GVQFHP 165

                         170
                  ....*....|....*...
gi 556300243  224 EWNSSEYALSrmLFEGFI 241
Cdd:TIGR00888 166 EVTHTEYGNE--LLENFV 181
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 97-224 1.04e-09

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: 56.39  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  97 MALIAAALERRIPIFAICRGLQELVVATGGTLYRrlfeqndllehredpelpvelqyAP------SHEVQVQEGGLLSQL 170
Cdd:cd01743   61 SLEIIRALAGKVPILGVCLGHQAIAEAFGGKVVR-----------------------APepmhgkTSEIHHDGSGLFKGL 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556300243 171 IpgcNTFWV---NSLHGQgARTLGPRLRVEARSTDGLVEAVSVHDHPFAlGVQWHPE 224
Cdd:cd01743  118 P---QPFTVgryHSLVVD-PDPLPDLLEVTASTEDGVIMALRHRDLPIY-GVQFHPE 169
GATase pfam00117
Glutamine amidotransferase class-I;
63-241 1.04e-09

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 56.48  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   63 DGIYLPGSPsnvqphlygengdepdADPGRDLLSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFE----QNDL 138
Cdd:pfam00117  42 DGIILSGGP----------------GSPGAAGGAIEAIREARELKIPILGICLGHQLLALAFGGKVVKAKKFghhgKNSP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  139 LEHREDPE---LPVELQYAPSHEVQVQEGGLLSQLIPgcnTFWvnslhgqgartlgprlrveaRSTDGLVEAVSVHDHPF 215
Cdd:pfam00117 106 VGDDGCGLfygLPNVFIVRRYHSYAVDPDTLPDGLEV---TAT--------------------SENDGTIMGIRHKKLPI 162

                         170       180
                  ....*....|....*....|....*.
gi 556300243  216 aLGVQWHPEWNSSEYAlSRMLFEGFI 241
Cdd:pfam00117 163 -FGVQFHPESILTPHG-PEILFNFFI 186
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 95-224 3.04e-09

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: 55.04  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  95 LSMALIAAaLERRIPIFAICRGLQELVVATGGTLYRrlfeqndllehredpeLPVelqyaPSH----EVQVQEGGLLSQL 170
Cdd:COG0512   60 ISLEVIRA-FAGKIPILGVCLGHQAIGEAFGGKVVR----------------APE-----PMHgktsPITHDGSGLFAGL 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556300243 171 iPgcNTFWV---NSLHGQGArTLGPRLRVEARSTDGLVEAVSVHDHPFAlGVQWHPE 224
Cdd:COG0512  118 -P--NPFTAtryHSLVVDRE-TLPDELEVTAWTEDGEIMGIRHRELPIE-GVQFHPE 169
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-241 6.16e-09

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: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 54.17  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  63 DGIYLPGSPSNVqphlygENGDEPDAdpgRDLLsmALIAAALERRIPIFAICRGLQELVVATGGTLYRRlfeqndllehr 142
Cdd:cd01741   48 DGLVILGGPMSV------DEDDYPWL---KKLK--ELIRQALAAGKPVLGICLGHQLLARALGGKVGRN----------- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 143 edpELPVELQYapsHEVQVQEGGLLSQLIPGC-NTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHpfALGVQW 221
Cdd:cd01741  106 ---PKGWEIGW---FPVTLTEAGKADPLFAGLpDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFRYGDR--ALGLQF 177

                        170       180
                 ....*....|....*....|
gi 556300243 222 HPEwnsseyalsRMLFEGFI 241
Cdd:cd01741  178 HPE---------ERLLRNFL 188
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 63-224 1.04e-08

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 54.18  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  63 DGIYLPGSPSNVqphlYGENGDEPDAdpgrdllsMALIAAALERRIPIFAICRGLQELVVATGGTLYRRlfeqndllEHR 142
Cdd:COG0518   50 DGLILSGGPMSV----YDEDPWLEDE--------PALIREAFELGKPVLGICYGAQLLAHALGGKVEPG--------PGR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 143 EdpelpvelqYAPsHEVQVQEGGLLSQLIPgcNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHpfALGVQWH 222
Cdd:COG0518  110 E---------IGW-APVELTEADPLFAGLP--DEFTVWMSHGDTVTELPEGAEVLASSDNCPNQAFRYGRR--VYGVQFH 175


                 ..
gi 556300243 223 PE 224
Cdd:COG0518  176 PE 177
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 97-241 1.74e-08

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: 53.33  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  97 MALIAAALERRIPIFAICRGLQELVVAtggtlYRRL---FEQNDLLEHREDPELPVELQYAPSHEVqVQEGG-------- 165
Cdd:cd01746   74 ILAIKYARENNIPFLGICLGMQLAVIE-----FARNvlgLPDANSTEFDPDTPHPVVDLMPEQKGV-KDLGGtmrlgayp 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 166 ------LLSQLIPGCNTFW-------------VNSLHGQGartlgprLRVEARSTDG-LVEAVSVHDHPFALGVQWHPEW 225
Cdd:cd01746  148 vilkpgTLAHKYYGKDEVEerhrhryevnpeyVDELEEAG-------LRFSGTDPDGgLVEIVELPDHPFFVGTQFHPEF 220

                        170
                 ....*....|....*.
gi 556300243 226 NSSEYALSRmLFEGFI 241
Cdd:cd01746  221 KSRPLKPHP-LFVGFV 235
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 63-230 4.86e-08

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 51.38  E-value: 4.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  63 DGIYLPGSPSNVqphlYGEngDEPDADPGrdllsmaliaaALERRIPIFAICRGLQELVVATGGTLYRRlfeqndllEHR 142
Cdd:cd01742   43 KGIILSGGPSSV----YEE--DAPRVDPE-----------IFELGVPVLGICYGMQLIAKALGGKVERG--------DKR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 143 EdpelpvelqYAPShEVQVQEGGLLSQLIPGCNTFWVNslHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFAlGVQWH 222
Cdd:cd01742   98 E---------YGKA-EIEIDDSSPLFEGLPDEQTVWMS--HGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIY-GVQFH 164


                 ....*...
gi 556300243 223 PEWNSSEY 230
Cdd:cd01742  165 PEVTHTEK 172
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 10-126 6.34e-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: 49.90  E-value: 6.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  10 IGVVMCrnrlkgHETQTLQEKYLNAIINAGGLPIALPHALAEPELLTALLPTLDGIYLPGSPSNVQphlygengdepdaD 89
Cdd:cd01653    1 VAVLLF------PGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPD-------------D 61

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 556300243  90 PGRDLLSMALIAAALERRIPIFAICRGLQELVVATGG 126
Cdd:cd01653   62 LARDEALLALLREAAAAGKPILGICLGAQLLVLGVQF 98
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 57-243 7.20e-08

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 52.72  E-value: 7.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243   57 ALLPTLDGIYLPGSpsnvqphlYGENGDEpdadpGRdllsMALIAAALERRIPIFAICRGLQELVVAtggtlYRRL---F 133
Cdd:TIGR00337 339 EFLKGLDGILVPGG--------FGERGVE-----GK----ILAIKYARENNIPFLGICLGMQLAVIE-----FARNvagL 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  134 EQNDLLEHREDPELPVeLQYAPSHEVQVQEGGLL------SQLIPGCNTFwvnSLHGQgaRTLGPR-------------- 193
Cdd:TIGR00337 397 EGANSTEFDPDTKYPV-VDLLPEQKDISDLGGTMrlglypCILKPGTLAF---KLYGK--EEVYERhrhryevnneyreq 470

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 556300243  194 -----LRVEARSTDG-LVEAVSVHDHPFALGVQWHPEWNSSEYALSRmLFEGFITA 243
Cdd:TIGR00337 471 ienkgLIVSGTSPDGrLVEIIELPDHPFFVACQFHPEFTSRPNDPHP-LFLGFVKA 525
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 194-252 5.96e-07

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 50.01  E-value: 5.96e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556300243 194 LRVEARSTDG-LVEAVSVHDHPFALGVQWHPEWNsseyalSRM-----LFEGFITACQSHIAEKQ 252
Cdd:COG0504  477 LVFSGTSPDGrLVEIVELPDHPWFVGVQFHPEFK------SRPnrphpLFRGFVKAALEYKKKKK 535
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 63-224 1.60e-06

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: 47.11  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  63 DGIYL---PGSPSNVQPhlygengdepdadpgrdllSMALIAAALERRIPIFAICRGLQELVVATGGTLYRRLFeqndll 139
Cdd:cd01744   41 DGIFLsngPGDPALLDE-------------------AIKTVRKLLGKKIPIFGICLGHQLLALALGAKTYKMKF------ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 140 EHRedpelpvelqyAPSHEVQVQEGGLL---SQlipgcNtfwvnslHGQG--ARTLGPRLRVEARS-TDGLVEAVSVHDH 213
Cdd:cd01744   96 GHR-----------GSNHPVKDLITGRVyitSQ-----N-------HGYAvdPDSLPGGLEVTHVNlNDGTVEGIRHKDL 152

                        170
                 ....*....|.
gi 556300243 214 PFaLGVQWHPE 224
Cdd:cd01744  153 PV-FSVQFHPE 162
pyrG PRK05380
CTP synthetase; Validated
 194-251 2.08e-06

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 48.09  E-value: 2.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556300243 194 LRVEARSTDG-LVEAVSVHDHPFALGVQWHPEWNsseyalSRM-----LFEGFITACQSHIAEK 251
Cdd:PRK05380 476 LVFSGTSPDGrLVEIVELPDHPWFVGVQFHPEFK------SRPrrphpLFAGFVKAALENKKRK 533
guaA PRK00074
GMP synthase; Reviewed
 45-224 4.51e-06

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 47.35  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  45 LPHALAEPELLtALLPTldGIYLPGSPSNVqphlYGENGdePDADPgrdllsmaliaAALERRIPIFAICRGLQELVVAT 124
Cdd:PRK00074  33 VPYDISAEEIR-AFNPK--GIILSGGPASV----YEEGA--PRADP-----------EIFELGVPVLGICYGMQLMAHQL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 125 GGTLYRRlfeqndllEHREdpelpvelqYAPShEVQVQEGGLLSQLIPGCNTFWVNslHGQGARTLGPRLRVEARSTDGL 204
Cdd:PRK00074  93 GGKVERA--------GKRE---------YGRA-ELEVDNDSPLFKGLPEEQDVWMS--HGDKVTELPEGFKVIASTENCP 152

                        170       180
                 ....*....|....*....|
gi 556300243 205 VEAVSVHDHPFAlGVQWHPE 224
Cdd:PRK00074 153 IAAIANEERKFY-GVQFHPE 171
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 10-120 1.36e-05

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: 42.57  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  10 IGVVMCrnrlkgHETQTLQEKYLNAIINAGGLPIALPHALAEPELLTALLPTLDGIYLPGSPSNVQphlygengdepdaD 89
Cdd:cd03128    1 VAVLLF------GGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPD-------------D 61

                         90       100       110
                 ....*....|....*....|....*....|.
gi 556300243  90 PGRDLLSMALIAAALERRIPIFAICRGLQEL 120
Cdd:cd03128   62 LAWDEALLALLREAAAAGKPVLGICLGAQLL 92
PLN02347 PLN02347
GMP synthetase
 48-238 2.62e-05

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 45.06  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  48 ALAEPELLTALLPTLdgIYLPGSPSNVqphlYGENGdePDADPGrdllsmaLIAAALERRIPIFAICRGLQELVVATGGT 127
Cdd:PLN02347  42 GTASLDRIASLNPRV--VILSGGPHSV----HVEGA--PTVPEG-------FFDYCRERGVPVLGICYGMQLIVQKLGGE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 128 LyrrlfeqnDLLEHREDPELPVELqyapshevqVQEGGLLSQLiPGCNTFWVNSLHGQGARTLGPRLRVEARSTDGLVEA 207
Cdd:PLN02347 107 V--------KPGEKQEYGRMEIRV---------VCGSQLFGDL-PSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVA 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 556300243 208 VSVHDHPFaLGVQWHPEWNSSEYA---LSRMLFE 238
Cdd:PLN02347 169 IENRERRI-YGLQYHPEVTHSPKGmetLRHFLFD 201
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 33-224 8.01e-05

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 42.62  E-value: 8.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  33 NAIINAGGLPialPHALAEPELLTALLPTLD-----GIYLPGSPSNVQphlygengDEPDADPG------RDLlsMALIA 101
Cdd:PRK07567  21 AAFLRYTGLD---PAELRRIRLDREPLPDLDlddysGVIVGGSPFNVS--------DPAESKSPwqrrveAEL--SGLLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 102 AALERRIPIFAICRGLQELVVATGGTLYRRlfeqndlleHREDpelpvelqyAPSHEVQVQEGGLLSQLIPGC-NTFWVN 180
Cdd:PRK07567  88 EVVARDFPFLGACYGVGTLGHHQGGVVDRT---------YGEP---------VGAVTVSLTDAGRADPLLAGLpDTFTAF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 556300243 181 SLHGQGARTLGPRLRVEARSTDGLVEAVSVHDHPFAlgVQWHPE 224
Cdd:PRK07567 150 VGHKEAVSALPPGAVLLATSPTCPVQMFRVGENVYA--TQFHPE 191
PRK00758 PRK00758
GMP synthase subunit A; Validated
 108-247 9.57e-05

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 42.15  E-value: 9.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 108 IPIFAICRGLQELVVATGGTLYR-----------RLFEQNDLLEHredpeLPVELQYAPSHEVQVQEggllsqlipgcnt 176
Cdd:PRK00758  68 VPILGICLGHQLIAKAFGGEVGRgeygeyalvevEILDEDDILKG-----LPPEIRVWASHADEVKE------------- 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556300243 177 fwvnslhgqgartLGPRLRVEARSTDGLVEAVSVHDHPFaLGVQWHPEWNSSEYAlsRMLFEGFITACQSH 247
Cdd:PRK00758 130 -------------LPDGFEILARSDICEVEAMKHKEKPI-YGVQFHPEVAHTEYG--EEIFKNFLEICGKY 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
95-224 1.31e-04

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 42.78  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  95 LSMALIAAaLERRIPIFAICRGLQELVVATGGTLYRRLF-----------EQNDLLEHREDPELPVelQYapsHEVQVQE 163
Cdd:PRK14607  62 ISVEVIRH-FSGKVPILGVCLGHQAIGYAFGGKIVHAKRilhgktspidhNGKGLFRGIPNPTVAT--RY---HSLVVEE 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556300243 164 GGLlsqliPGCntfwvnslhgqgartlgprLRVEARSTDGLVEAVSVHDHPFaLGVQWHPE 224
Cdd:PRK14607 136 ASL-----PEC-------------------LEVTAKSDDGEIMGIRHKEHPI-FGVQFHPE 171
PLN02335 PLN02335
anthranilate synthase
 108-224 6.05e-04

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 40.17  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243 108 IPIFAICRGLQELVVATGGTLYRrlfeqndllehreDPELPVELQYAPSHEVQVQEGGLLSQLipgCNTFWVNSLHG--- 184
Cdd:PLN02335  92 VPLFGVCMGLQCIGEAFGGKIVR-------------SPFGVMHGKSSPVHYDEKGEEGLFSGL---PNPFTAGRYHSlvi 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556300243 185 QGARTLGPRLRVEARSTDGLVEAVSVHDHPFALGVQWHPE 224
Cdd:PLN02335 156 EKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQGVQFHPE 195
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 50-136 3.64e-03

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 37.95  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556300243  50 AEPELLTALLPtlDGIYL---PGSPSNVQPHLygengdepdaDPGRDLLSmaliaaalerRIPIFAICRGLQELVVATGG 126
Cdd:PRK12838 199 TSLEEIKNLNP--DGIVLsngPGDPKELQPYL----------PEIKKLIS----------SYPILGICLGHQLIALALGA 256

                         90
                 ....*....|
gi 556300243 127 TLYRRLFEQN 136
Cdd:PRK12838 257 DTEKLPFGHR 266
PLN02327 PLN02327
CTP synthase
 205-250 4.48e-03

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 38.08  E-value: 4.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 556300243 205 VEAVSVHDHPFALGVQWHPEWNSSEYALSRmLFEGFITACQSHIAE 250
Cdd:PLN02327 508 MEIVELPSHPFFVGVQFHPEFKSRPGKPSP-LFLGLIAAASGQLDA 552
 
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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