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Conserved domains on  [gi|90111245|ref|NP_415814|]
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gamma-glutamyl-gamma-aminobutyrate hydrolase [Escherichia coli str. K-12 substr. MG1655]

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: 525.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80
Cdd:PRK11366   1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   81 ENGDEPDADPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160
Cdd:PRK11366  81 ENGDEPDADPGRDLLSMALINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240
Cdd:PRK11366 161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240

                        250
                 ....*....|....
gi 90111245  241 ITACQHHIAEKQRL 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: 525.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80
Cdd:PRK11366   1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   81 ENGDEPDADPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160
Cdd:PRK11366  81 ENGDEPDADPGRDLLSMALINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240
Cdd:PRK11366 161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240

                        250
                 ....*....|....
gi 90111245  241 ITACQHHIAEKQRL 254
Cdd:PRK11366 241 ITACQHHIAEKQRL 254
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 12-247 1.70e-95

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: 279.36  E-value: 1.70e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  12 VVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHaLAEPSLLEQLLPKLDGIYLPGSPsNVQPHLYGENGDEP--DAD 89
Cdd:COG2071   1 ITADLRTAGGYPAHYLPEDYVRAVRAAGGLPVLLPP-VGDEEDLDELLDRLDGLVLTGGA-DVDPALYGEEPHPElgPID 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  90 PGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQ-PELLEHREDpelpvEQQYAPSHEVQVEEGGLLS 168
Cdd:COG2071  79 PERDAFELALIRAALERGKPVLGICRGMQLLNVALGGTLYQDLPDQvPGALDHRQP-----APRYAPRHTVEIEPGSRLA 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111245 169 ALLPEcSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGFITACQHH 247
Cdd:COG2071 154 RILGE-EEIRVNSLHHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWLAASDPLSRRLFEAFVEAARAR 231
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 8-224 8.20e-93

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: 272.21  E-value: 8.20e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245     8 PVIGVVMCRNRLKGHATQTLQEKYLNA-----IIHAGGLPIALPhALAEPSLLEQLLPKLDGIYLPGSPsNVQPHLYGEN 82
Cdd:pfam07722   1 PVIGITANEESLGGHVFHGAGESYLAAgyveaVEGAGGLPVLLP-ILGDPEDAAAILDRLDGLLLTGGP-NVDPHFYGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    83 GDE--PDADPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDpelPVEQQYAPSHEVQ 160
Cdd:pfam07722  79 PSEsgGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREH---CQVAPYAPSHAVN 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111245   161 VEEGGLLSALLPeCSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHP-FALGVQWHPE 224
Cdd:pfam07722 156 VEPGSLLASLLG-SEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKgFALGVQWHPE 219
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 10-241 1.53e-68

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: 209.35  E-value: 1.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  10 IGVVMCRNRLKGHAT--QTLQEKYLNAIIHAGGLPIALPHALAEpSLLEQLLPKLDGIYLPGSPSNVQPHLYGENGDEPD 87
Cdd:cd01745   1 IGITARLREEEGGYErrDYLNQYYVDAVRKAGGLPVLLPPVDDE-EDLEQYLELLDGLLLTGGGDVDPPLYGEEPHPELG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  88 A-DPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLceqpellehredpelpveqqyapshevqveeggl 166
Cdd:cd01745  80 PiDPERDAFELALLRAALERGKPILGICRGMQLLNVALGGTLYQDI---------------------------------- 125

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111245 167 lsallpecsnfWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGFI 241
Cdd:cd01745 126 -----------RVNSLHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLADTDPDSLKLFEAFV 189
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 55-241 8.15e-11

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: 59.64  E-value: 8.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    55 LEQL---LPKldGIYLPGSPSNVqphlYGENGDEPDAdpgrdllsmaiinAALERRIPIFAICRGLQELVVATGGSLHRK 131
Cdd:TIGR00888  34 LEEIrekNPK--GIILSGGPSSV----YAENAPRADE-------------KIFELGVPVLGICYGMQLMAKQLGGEVGRA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   132 lceqpellEHREdpelpveqqYAPShEVQVEEGGLLSALLPECSNFWVNslHGQGAKVVSPRLRVEARSPDGLVEAVSVI 211
Cdd:TIGR00888  95 --------EKRE---------YGKA-ELEILDEDDLFRGLPDESTVWMS--HGDKVKELPEGFKVLATSDNCPVAAMAHE 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 90111245   212 NHPFAlGVQWHPEWNSSEYALSriLFEGFI 241
Cdd:TIGR00888 155 EKPIY-GVQFHPEVTHTEYGNE--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: 525.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80
Cdd:PRK11366   1 MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   81 ENGDEPDADPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160
Cdd:PRK11366  81 ENGDEPDADPGRDLLSMALINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240
Cdd:PRK11366 161 VEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGF 240

                        250
                 ....*....|....
gi 90111245  241 ITACQHHIAEKQRL 254
Cdd:PRK11366 241 ITACQHHIAEKQRL 254
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 12-247 1.70e-95

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: 279.36  E-value: 1.70e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  12 VVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHaLAEPSLLEQLLPKLDGIYLPGSPsNVQPHLYGENGDEP--DAD 89
Cdd:COG2071   1 ITADLRTAGGYPAHYLPEDYVRAVRAAGGLPVLLPP-VGDEEDLDELLDRLDGLVLTGGA-DVDPALYGEEPHPElgPID 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  90 PGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQ-PELLEHREDpelpvEQQYAPSHEVQVEEGGLLS 168
Cdd:COG2071  79 PERDAFELALIRAALERGKPVLGICRGMQLLNVALGGTLYQDLPDQvPGALDHRQP-----APRYAPRHTVEIEPGSRLA 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111245 169 ALLPEcSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGFITACQHH 247
Cdd:COG2071 154 RILGE-EEIRVNSLHHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWLAASDPLSRRLFEAFVEAARAR 231
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 8-224 8.20e-93

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: 272.21  E-value: 8.20e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245     8 PVIGVVMCRNRLKGHATQTLQEKYLNA-----IIHAGGLPIALPhALAEPSLLEQLLPKLDGIYLPGSPsNVQPHLYGEN 82
Cdd:pfam07722   1 PVIGITANEESLGGHVFHGAGESYLAAgyveaVEGAGGLPVLLP-ILGDPEDAAAILDRLDGLLLTGGP-NVDPHFYGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    83 GDE--PDADPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDpelPVEQQYAPSHEVQ 160
Cdd:pfam07722  79 PSEsgGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREH---CQVAPYAPSHAVN 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111245   161 VEEGGLLSALLPeCSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHP-FALGVQWHPE 224
Cdd:pfam07722 156 VEPGSLLASLLG-SEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKgFALGVQWHPE 219
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 10-241 1.53e-68

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: 209.35  E-value: 1.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  10 IGVVMCRNRLKGHAT--QTLQEKYLNAIIHAGGLPIALPHALAEpSLLEQLLPKLDGIYLPGSPSNVQPHLYGENGDEPD 87
Cdd:cd01745   1 IGITARLREEEGGYErrDYLNQYYVDAVRKAGGLPVLLPPVDDE-EDLEQYLELLDGLLLTGGGDVDPPLYGEEPHPELG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  88 A-DPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLceqpellehredpelpveqqyapshevqveeggl 166
Cdd:cd01745  80 PiDPERDAFELALLRAALERGKPILGICRGMQLLNVALGGTLYQDI---------------------------------- 125

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111245 167 lsallpecsnfWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGFI 241
Cdd:cd01745 126 -----------RVNSLHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLADTDPDSLKLFEAFV 189
PRK13566 PRK13566
anthranilate synthase component I;
90-224 1.87e-11

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 63.40  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   90 PGR--DLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRklceqpellehredpeLPVEQQYAPShEVQVEEGGLL 167
Cdd:PRK13566 579 PGRpsDFDCKATIDAALARNLPIFGVCLGLQAIVEAFGGELGQ----------------LAYPMHGKPS-RIRVRGPGRL 641

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  168 SALLPECsnFWV---NSLHGQGAKVVSPrLRVEARSPDGLVEAVSVINHPFAlGVQWHPE 224
Cdd:PRK13566 642 FSGLPEE--FTVgryHSLFADPETLPDE-LLVTAETEDGVIMAIEHKTLPVA-AVQFHPE 697
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 55-241 8.15e-11

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: 59.64  E-value: 8.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    55 LEQL---LPKldGIYLPGSPSNVqphlYGENGDEPDAdpgrdllsmaiinAALERRIPIFAICRGLQELVVATGGSLHRK 131
Cdd:TIGR00888  34 LEEIrekNPK--GIILSGGPSSV----YAENAPRADE-------------KIFELGVPVLGICYGMQLMAKQLGGEVGRA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   132 lceqpellEHREdpelpveqqYAPShEVQVEEGGLLSALLPECSNFWVNslHGQGAKVVSPRLRVEARSPDGLVEAVSVI 211
Cdd:TIGR00888  95 --------EKRE---------YGKA-ELEILDEDDLFRGLPDESTVWMS--HGDKVKELPEGFKVLATSDNCPVAAMAHE 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 90111245   212 NHPFAlGVQWHPEWNSSEYALSriLFEGFI 241
Cdd:TIGR00888 155 EKPIY-GVQFHPEVTHTEYGNE--LLENFV 181
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 27-243 9.60e-10

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: 58.49  E-value: 9.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    27 LQEKYLN---AIIHAGG-----LPIALPHAL-AEPSLLEqLLPKLDGIYLPGSpsnvqphlYGENGDEpdadpgrdllsm 97
Cdd:TIGR00337 301 LKDAYLSvieALKHAGAkldtkVNIKWIDSEdLEEEGVE-FLKGLDGILVPGG--------FGERGVE------------ 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    98 AIINA---ALERRIPIFAICRGLQELVVatggSLHRKLCEQPEL--LEHREDPELPV-----EQQYAP---------SHE 158
Cdd:TIGR00337 360 GKILAikyARENNIPFLGICLGMQLAVI----EFARNVAGLEGAnsTEFDPDTKYPVvdllpEQKDISdlggtmrlgLYP 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   159 VQVEEGGLLSALLP------------ECSNFWVNSLHGQGakvvsprLRVEARSPDG-LVEAVSVINHPFALGVQWHPEW 225
Cdd:TIGR00337 436 CILKPGTLAFKLYGkeevyerhrhryEVNNEYREQIENKG-------LIVSGTSPDGrLVEIIELPDHPFFVACQFHPEF 508

                         250
                  ....*....|....*...
gi 90111245   226 NSSEYALSRiLFEGFITA 243
Cdd:TIGR00337 509 TSRPNDPHP-LFLGFVKA 525
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 32-241 6.69e-09

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: 54.87  E-value: 6.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  32 LNAIIHAGglpIALPHALA---------EPSLLEQLLPKLDGIYLPGSpsnvqphlYGENGDEpdadpGRdllsMAIINA 102
Cdd:cd01746  20 LEALKHAG---IALGVKLEikwidsedlEEENAEEALKGADGILVPGG--------FGIRGVE-----GK----ILAIKY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245 103 ALERRIPIFAICRGLQELVVAtggsLHRKLCEQPE--LLEHREDPELPV----EQQYAPSH----------EVQVEEGGL 166
Cdd:cd01746  80 ARENNIPFLGICLGMQLAVIE----FARNVLGLPDanSTEFDPDTPHPVvdlmPEQKGVKDlggtmrlgayPVILKPGTL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245 167 LSALLP------------ECSNFWVNSLHGQGakvvsprLRVEARSPDG-LVEAVSVINHPFALGVQWHPEWNSSEYALS 233
Cdd:cd01746 156 AHKYYGkdeveerhrhryEVNPEYVDELEEAG-------LRFSGTDPDGgLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                ....*...
gi 90111245 234 RiLFEGFI 241
Cdd:cd01746 229 P-LFVGFV 235
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 53-241 8.32e-09

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: 53.69  E-value: 8.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  53 SLLEQLLPKLDGIYLPGSPSNVqphlYGEngDEPDADPGrdllsmaiinaALERRIPIFAICRGLQELVVATGGSLHRKl 132
Cdd:cd01742  33 PLEEIKLKNPKGIILSGGPSSV----YEE--DAPRVDPE-----------IFELGVPVLGICYGMQLIAKALGGKVERG- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245 133 ceqpellEHREdpelpveqqYAPShEVQVEEGGLLSALLPECSNFWVNslHGQGAKVVSPRLRVEARSPDGLVEAVSVIN 212
Cdd:cd01742  95 -------DKRE---------YGKA-EIEIDDSSPLFEGLPDEQTVWMS--HGDEVVKLPEGFKVIASSDNCPVAAIANEE 155

                       170       180
                ....*....|....*....|....*....
gi 90111245 213 HPFAlGVQWHPEWNSSEYAlsRILFEGFI 241
Cdd:cd01742 156 KKIY-GVQFHPEVTHTEKG--KEILKNFL 181
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 194-252 5.08e-08

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: 53.09  E-value: 5.08e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111245 194 LRVEARSPDG-LVEAVSVINHPFALGVQWHPEWNsseyalSRI-----LFEGFITACQHHIAEKQ 252
Cdd:COG0504 477 LVFSGTSPDGrLVEIVELPDHPWFVGVQFHPEFK------SRPnrphpLFRGFVKAALEYKKKKK 535
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 51-224 6.20e-08

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: 51.38  E-value: 6.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  51 EPSLLEQLLPKLDGIYL---PGSPSNVQphlygengdepdadpgrdlLSMAIINAaLERRIPIFAICRGLQELVVATGGs 127
Cdd:cd01743  32 EITLEELELLNPDAIVIspgPGHPEDAG-------------------ISLEIIRA-LAGKVPILGVCLGHQAIAEAFGG- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245 128 lhrklceqpellehredpelPVEQQYAPSHEVQVEE---GGLLSALLPecSNFWV---NSLHGQGAKVVSPrLRVEARSP 201
Cdd:cd01743  91 --------------------KVVRAPEPMHGKTSEIhhdGSGLFKGLP--QPFTVgryHSLVVDPDPLPDL-LEVTASTE 147

                       170       180
                ....*....|....*....|...
gi 90111245 202 DGLVEAVSVINHPFAlGVQWHPE 224
Cdd:cd01743 148 DGVIMALRHRDLPIY-GVQFHPE 169
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 10-126 1.46e-07

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: 48.75  E-value: 1.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  10 IGVVMCrnrlkgHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQphlygengdepdaD 89
Cdd:cd01653   1 VAVLLF------PGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPD-------------D 61

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 90111245  90 PGRDLLSMAIINAALERRIPIFAICRGLQELVVATGG 126
Cdd:cd01653  62 LARDEALLALLREAAAAGKPILGICLGAQLLVLGVQF 98
GATase pfam00117
Glutamine amidotransferase class-I;
53-241 1.55e-07

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 50.31  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245    53 SLLEQLLPKLDGIYLPGSPsnvqphlygengdepdADPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKL 132
Cdd:pfam00117  32 PAEEILEENPDGIILSGGP----------------GSPGAAGGAIEAIREARELKIPILGICLGHQLLALAFGGKVVKAK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   133 CEqpellEHRedpelpveqqyAPSHEVQVEEGGLLSAlLPECSNFWVNslHGQGA--KVVSPRLRVEARSPDG-LVEAVS 209
Cdd:pfam00117  96 KF-----GHH-----------GKNSPVGDDGCGLFYG-LPNVFIVRRY--HSYAVdpDTLPDGLEVTATSENDgTIMGIR 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 90111245   210 VINHPFaLGVQWHPEWNSSEYAlSRILFEGFI 241
Cdd:pfam00117 157 HKKLPI-FGVQFHPESILTPHG-PEILFNFFI 186
pyrG PRK05380
CTP synthetase; Validated
 194-251 1.62e-07

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 51.56  E-value: 1.62e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111245  194 LRVEARSPDG-LVEAVSVINHPFALGVQWHPEWNsseyalSRI-----LFEGFITACQHHIAEK 251
Cdd:PRK05380 476 LVFSGTSPDGrLVEIVELPDHPWFVGVQFHPEFK------SRPrrphpLFAGFVKAALENKKRK 533
guaA PRK00074
GMP synthase; Reviewed
 55-224 2.08e-07

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 51.20  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   55 LEQLLPKldGIYLPGSPSNVqphlYGENGdePDADPgrdllsmAIINAAlerrIPIFAICRGLQELVVATGGSLHRKlce 134
Cdd:PRK00074  42 IRAFNPK--GIILSGGPASV----YEEGA--PRADP-------EIFELG----VPVLGICYGMQLMAHQLGGKVERA--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  135 qpellEHREdpelpveqqYAPShEVQVEEGGLLSALLPECSNFWVNslHG-------QGAKVVsprlrveARSPDGLVEA 207
Cdd:PRK00074 100 -----GKRE---------YGRA-ELEVDNDSPLFKGLPEEQDVWMS--HGdkvtelpEGFKVI-------ASTENCPIAA 155

                        170
                 ....*....|....*..
gi 90111245  208 VSVINHPFAlGVQWHPE 224
Cdd:PRK00074 156 IANEERKFY-GVQFHPE 171
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 95-224 2.75e-07

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: 49.27  E-value: 2.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  95 LSMAIInAALERRIPIFAICRGLQELVVATGGSLHRklceqpellehredpeLPVeqqyaPSH----EVQVEEGGLLSAL 170
Cdd:COG0512  60 ISLEVI-RAFAGKIPILGVCLGHQAIGEAFGGKVVR----------------APE-----PMHgktsPITHDGSGLFAGL 117

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111245 171 lPecSNFWV---NSLHGQGAKVvSPRLRVEARSPDGLVEAVSVINHPFAlGVQWHPE 224
Cdd:COG0512 118 -P--NPFTAtryHSLVVDRETL-PDELEVTAWTEDGEIMGIRHRELPIE-GVQFHPE 169
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 63-224 1.02e-06

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: 48.40  E-value: 1.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  63 DGIYLPGSPSNVqphlYGENGDEPDAdpgrdllsMAIINAALERRIPIFAICRGLQELVVATGGSLHR-----------K 131
Cdd:COG0518  50 DGLILSGGPMSV----YDEDPWLEDE--------PALIREAFELGKPVLGICYGAQLLAHALGGKVEPgpgreigwapvE 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245 132 LCEQPELLEHREDpELPVEQqyapSHEVQVEEggllsalLPEcsnfwvnslhgqGAKVVsprlrveARSPDGLVEAVSVI 211
Cdd:COG0518 118 LTEADPLFAGLPD-EFTVWM----SHGDTVTE-------LPE------------GAEVL-------ASSDNCPNQAFRYG 166

                       170
                ....*....|...
gi 90111245 212 NHpfALGVQWHPE 224
Cdd:COG0518 167 RR--VYGVQFHPE 177
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-225 1.84e-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: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 46.85  E-value: 1.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  63 DGIYLPGSPSNVqphlygENGDEPDADPGRDLlsmaiINAALERRIPIFAICRGLQELVVATGGSLHRklceqpelleHR 142
Cdd:cd01741  48 DGLVILGGPMSV------DEDDYPWLKKLKEL-----IRQALAAGKPVLGICLGHQLLARALGGKVGR----------NP 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245 143 EDPELPVeqqyapsHEVQVEEGGLLSALLPECSN-FWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVinHPFALGVQW 221
Cdd:cd01741 107 KGWEIGW-------FPVTLTEAGKADPLFAGLPDeFPVFHWHGDTVVELPPGAVLLASSEACPNQAFRY--GDRALGLQF 177


                ....
gi 90111245 222 HPEW 225
Cdd:cd01741 178 HPEE 181
PRK00758 PRK00758
GMP synthase subunit A; Validated
 108-245 1.87e-06

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 46.77  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  108 IPIFAICRGLQELVVATGGSLHRKlcEQPEllehredpelpveqqYApSHEVQV-EEGGLLSALLPEcSNFWVNslHGQG 186
Cdd:PRK00758  68 VPILGICLGHQLIAKAFGGEVGRG--EYGE---------------YA-LVEVEIlDEDDILKGLPPE-IRVWAS--HADE 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111245  187 AKVVSPRLRVEARSPDGLVEAVSVINHPFaLGVQWHPEWNSSEYAlsRILFEGFITACQ 245
Cdd:PRK00758 127 VKELPDGFEILARSDICEVEAMKHKEKPI-YGVQFHPEVAHTEYG--EEIFKNFLEICG 182
PLN02347 PLN02347
GMP synthetase
 105-238 2.23e-05

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 45.06  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  105 ERRIPIFAICRGLQELVVATGGSLHrklceqpellehredpelPVEQQYAPSHEVQVEEGGLLSALLPECSNFWVNSLHG 184
Cdd:PLN02347  84 ERGVPVLGICYGMQLIVQKLGGEVK------------------PGEKQEYGRMEIRVVCGSQLFGDLPSGETQTVWMSHG 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111245  185 QGAKVVSPRLRVEARSPDGLVEAVSVINHPFaLGVQWHPEWNSSEYA---LSRILFE 238
Cdd:PLN02347 146 DEAVKLPEGFEVVAKSVQGAVVAIENRERRI-YGLQYHPEVTHSPKGmetLRHFLFD 201
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 10-120 3.52e-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: 41.42  E-value: 3.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  10 IGVVMCrnrlkgHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQphlygengdepdaD 89
Cdd:cd03128   1 VAVLLF------GGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPD-------------D 61

                        90       100       110
                ....*....|....*....|....*....|.
gi 90111245  90 PGRDLLSMAIINAALERRIPIFAICRGLQEL 120
Cdd:cd03128  62 LAWDEALLALLREAAAAGKPVLGICLGAQLL 92
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
95-224 4.04e-04

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 41.24  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245   95 LSMAIInAALERRIPIFAICRGLQELVVATGGS-------LHRKLceqpELLEH------REDPELPVEQQYapsHEVQV 161
Cdd:PRK14607  62 ISVEVI-RHFSGKVPILGVCLGHQAIGYAFGGKivhakriLHGKT----SPIDHngkglfRGIPNPTVATRY---HSLVV 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111245  162 EEGGllsalLPECsnfwvnslhgqgakvvsprLRVEARSPDGLVEAVSVINHPFaLGVQWHPE 224
Cdd:PRK14607 134 EEAS-----LPEC-------------------LEVTAKSDDGEIMGIRHKEHPI-FGVQFHPE 171
PLN02335 PLN02335
anthranilate synthase
 108-224 1.05e-03

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 39.40  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111245  108 IPIFAICRGLQELVVATGGSLHRKlceqpellehredPELPVEQQYAPSHEVQVEEGGLLSALLPECSNFWVNSLHGQGA 187
Cdd:PLN02335  92 VPLFGVCMGLQCIGEAFGGKIVRS-------------PFGVMHGKSSPVHYDEKGEEGLFSGLPNPFTAGRYHSLVIEKD 158

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 90111245  188 KVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPE 224
Cdd:PLN02335 159 TFPSDELEVTAWTEDGLIMAARHRKYKHIQGVQFHPE 195
PLN02327 PLN02327
CTP synthase
 205-244 8.52e-03

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 37.31  E-value: 8.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 90111245  205 VEAVSVINHPFALGVQWHPEWNSSEYALSRiLFEGFITAC 244
Cdd:PLN02327 508 MEIVELPSHPFFVGVQFHPEFKSRPGKPSP-LFLGLIAAA 546
 
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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