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Conserved domains on  [gi|429241401|ref|NP_596851|]
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class I glutamine amidotransferase family protein [Schizosaccharomyces pombe]

Protein Classification

gamma-glutamyl-gamma-aminobutyrate hydrolase family protein( domain architecture ID 11449689)

gamma-glutamyl-gamma-aminobutyrate hydrolase family protein may catalyze the hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate, an important step in putrescine degradation

CATH:  3.40.50.880
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0016811
MEROPS:  C26
PubMed:  11517925|15590624

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 17-223 2.56e-79

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: 238.53  E-value: 2.56e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  17 QPYVEAIIKAGGCPIVIYPGLQRNSIPP---NIDGIILAGGESVHPNRYGEDFDPnAPKSVDVIRDSTEWGMIDFALKKK 93
Cdd:COG2071   18 EDYVRAVRAAGGLPVLLPPVGDEEDLDElldRLDGLVLTGGADVDPALYGEEPHP-ELGPIDPERDAFELALIRAALERG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  94 IPILGICRGCQVLNVYFGGSLYQNVSS-CGFRDIHRPSKPRHYLAHKVMAKPG-KLKNILGSNVIDVNSIHDQGIKTLGM 171
Cdd:COG2071   97 KPVLGICRGMQLLNVALGGTLYQDLPDqVPGALDHRQPAPRYAPRHTVEIEPGsRLARILGEEEIRVNSLHHQAVKRLGP 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 429241401 172 GLQSTVISDDGLCEGIESKD-GLIIGVQWHPEAIIDKQPHSLKLFQYFINRSK 223
Cdd:COG2071  177 GLRVSARAPDGVIEAIESPGaPFVLGVQWHPEWLAASDPLSRRLFEAFVEAAR 229
 
Name Accession Description Interval E-value
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 17-223 2.56e-79

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: 238.53  E-value: 2.56e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  17 QPYVEAIIKAGGCPIVIYPGLQRNSIPP---NIDGIILAGGESVHPNRYGEDFDPnAPKSVDVIRDSTEWGMIDFALKKK 93
Cdd:COG2071   18 EDYVRAVRAAGGLPVLLPPVGDEEDLDElldRLDGLVLTGGADVDPALYGEEPHP-ELGPIDPERDAFELALIRAALERG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  94 IPILGICRGCQVLNVYFGGSLYQNVSS-CGFRDIHRPSKPRHYLAHKVMAKPG-KLKNILGSNVIDVNSIHDQGIKTLGM 171
Cdd:COG2071   97 KPVLGICRGMQLLNVALGGTLYQDLPDqVPGALDHRQPAPRYAPRHTVEIEPGsRLARILGEEEIRVNSLHHQAVKRLGP 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 429241401 172 GLQSTVISDDGLCEGIESKD-GLIIGVQWHPEAIIDKQPHSLKLFQYFINRSK 223
Cdd:COG2071  177 GLRVSARAPDGVIEAIESPGaPFVLGVQWHPEWLAASDPLSRRLFEAFVEAAR 229
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 17-219 1.23e-57

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: 181.62  E-value: 1.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  17 QPYVEAIIKAGGCPIVIYPGL---QRNSIPPNIDGIILAGGESVHPNRYGEDFDPNaPKSVDVIRDSTEWGMIDFALKKK 93
Cdd:cd01745   22 QYYVDAVRKAGGLPVLLPPVDdeeDLEQYLELLDGLLLTGGGDVDPPLYGEEPHPE-LGPIDPERDAFELALLRAALERG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  94 IPILGICRGCQVLNVYFGGSLYQNvsscgfrdihrpskprhylahkvmakpgklknilgsnvIDVNSIHDQGIKTLGMGL 173
Cdd:cd01745  101 KPILGICRGMQLLNVALGGTLYQD--------------------------------------IRVNSLHHQAIKRLADGL 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 429241401 174 QSTVISDDGLCEGIESKD-GLIIGVQWHPEAIIDKQPHSLKLFQYFI 219
Cdd:cd01745  143 RVEARAPDGVIEAIESPDrPFVLGVQWHPEWLADTDPDSLKLFEAFV 189
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 4-202 3.60e-53

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: 171.29  E-value: 3.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401    4 PIIALS-------------VGFSNNSQPYVEAIIKAGGCPIVIYPGLQRNSIP---PNIDGIILAGGESVHPNRYGEDFD 67
Cdd:pfam07722   1 PVIGITaneeslgghvfhgAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAailDRLDGLLLTGGPNVDPHFYGEEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   68 PnAPKSVDVIRDSTEWGMIDFALKKKIPILGICRGCQVLNVYFGGSLYQNVSSCGFRDIHR--PSKPRHYLAHKVMAKPG 145
Cdd:pfam07722  81 E-SGGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHRehCQVAPYAPSHAVNVEPG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  146 -KLKNILGSNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESK--DGLIIGVQWHPE 202
Cdd:pfam07722 160 sLLASLLGSEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIEAIESPnaKGFALGVQWHPE 219
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 17-228 6.99e-34

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 122.70  E-value: 6.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  17 QPYVEAIIKAGGCPIVIYPGLQR----NSIPPNIDGIILAGGES-VHPNRYGEDFD-PNApksvDVIRDSTEWGMIDFAL 90
Cdd:PRK11366  29 EKYLNAIIHAGGLPIALPHALAEpsllEQLLPKLDGIYLPGSPSnVQPHLYGENGDePDA----DPGRDLLSMALINAAL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  91 KKKIPILGICRGCQVLNVYFGGSLYQNVssCGFRDI--HR-----PSKPRHYLAHKVMAKPGKL--KNILGSNVIDVNSI 161
Cdd:PRK11366 105 ERRIPIFAICRGLQELVVATGGSLHRKL--CEQPELleHRedpelPVEQQYAPSHEVQVEEGGLlsALLPECSNFWVNSL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429241401 162 HDQGIKTLGMGLQSTVISDDGLCEGIESKD-GLIIGVQWHPEAIIDKQPHSLKLFQYFINRSKWHMKQ 228
Cdd:PRK11366 183 HGQGAKVVSPRLRVEARSPDGLVEAVSVINhPFALGVQWHPEWNSSEYALSRILFEGFITACQHHIAE 250
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 48-202 1.31e-06

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: 47.31  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   48 GIILAGG-ESVhpnrYGEdfdpNAPKSVDVIRDStewgmidfalkkKIPILGICRGCQVLNVYFGGslyqnvsscgfrDI 126
Cdd:TIGR00888  44 GIILSGGpSSV----YAE----NAPRADEKIFEL------------GVPVLGICYGMQLMAKQLGG------------EV 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429241401  127 HRPSKPRHYLAHKVMAKPGKLKNILGsNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESKDGLIIGVQWHPE 202
Cdd:TIGR00888  92 GRAEKREYGKAELEILDEDDLFRGLP-DESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYGVQFHPE 166
 
Name Accession Description Interval E-value
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 17-223 2.56e-79

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: 238.53  E-value: 2.56e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  17 QPYVEAIIKAGGCPIVIYPGLQRNSIPP---NIDGIILAGGESVHPNRYGEDFDPnAPKSVDVIRDSTEWGMIDFALKKK 93
Cdd:COG2071   18 EDYVRAVRAAGGLPVLLPPVGDEEDLDElldRLDGLVLTGGADVDPALYGEEPHP-ELGPIDPERDAFELALIRAALERG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  94 IPILGICRGCQVLNVYFGGSLYQNVSS-CGFRDIHRPSKPRHYLAHKVMAKPG-KLKNILGSNVIDVNSIHDQGIKTLGM 171
Cdd:COG2071   97 KPVLGICRGMQLLNVALGGTLYQDLPDqVPGALDHRQPAPRYAPRHTVEIEPGsRLARILGEEEIRVNSLHHQAVKRLGP 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 429241401 172 GLQSTVISDDGLCEGIESKD-GLIIGVQWHPEAIIDKQPHSLKLFQYFINRSK 223
Cdd:COG2071  177 GLRVSARAPDGVIEAIESPGaPFVLGVQWHPEWLAASDPLSRRLFEAFVEAAR 229
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 17-219 1.23e-57

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: 181.62  E-value: 1.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  17 QPYVEAIIKAGGCPIVIYPGL---QRNSIPPNIDGIILAGGESVHPNRYGEDFDPNaPKSVDVIRDSTEWGMIDFALKKK 93
Cdd:cd01745   22 QYYVDAVRKAGGLPVLLPPVDdeeDLEQYLELLDGLLLTGGGDVDPPLYGEEPHPE-LGPIDPERDAFELALLRAALERG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  94 IPILGICRGCQVLNVYFGGSLYQNvsscgfrdihrpskprhylahkvmakpgklknilgsnvIDVNSIHDQGIKTLGMGL 173
Cdd:cd01745  101 KPILGICRGMQLLNVALGGTLYQD--------------------------------------IRVNSLHHQAIKRLADGL 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 429241401 174 QSTVISDDGLCEGIESKD-GLIIGVQWHPEAIIDKQPHSLKLFQYFI 219
Cdd:cd01745  143 RVEARAPDGVIEAIESPDrPFVLGVQWHPEWLADTDPDSLKLFEAFV 189
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 4-202 3.60e-53

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: 171.29  E-value: 3.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401    4 PIIALS-------------VGFSNNSQPYVEAIIKAGGCPIVIYPGLQRNSIP---PNIDGIILAGGESVHPNRYGEDFD 67
Cdd:pfam07722   1 PVIGITaneeslgghvfhgAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAailDRLDGLLLTGGPNVDPHFYGEEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   68 PnAPKSVDVIRDSTEWGMIDFALKKKIPILGICRGCQVLNVYFGGSLYQNVSSCGFRDIHR--PSKPRHYLAHKVMAKPG 145
Cdd:pfam07722  81 E-SGGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTDHRehCQVAPYAPSHAVNVEPG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  146 -KLKNILGSNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESK--DGLIIGVQWHPE 202
Cdd:pfam07722 160 sLLASLLGSEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIEAIESPnaKGFALGVQWHPE 219
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 17-228 6.99e-34

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 122.70  E-value: 6.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  17 QPYVEAIIKAGGCPIVIYPGLQR----NSIPPNIDGIILAGGES-VHPNRYGEDFD-PNApksvDVIRDSTEWGMIDFAL 90
Cdd:PRK11366  29 EKYLNAIIHAGGLPIALPHALAEpsllEQLLPKLDGIYLPGSPSnVQPHLYGENGDePDA----DPGRDLLSMALINAAL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  91 KKKIPILGICRGCQVLNVYFGGSLYQNVssCGFRDI--HR-----PSKPRHYLAHKVMAKPGKL--KNILGSNVIDVNSI 161
Cdd:PRK11366 105 ERRIPIFAICRGLQELVVATGGSLHRKL--CEQPELleHRedpelPVEQQYAPSHEVQVEEGGLlsALLPECSNFWVNSL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429241401 162 HDQGIKTLGMGLQSTVISDDGLCEGIESKD-GLIIGVQWHPEAIIDKQPHSLKLFQYFINRSKWHMKQ 228
Cdd:PRK11366 183 HGQGAKVVSPRLRVEARSPDGLVEAVSVINhPFALGVQWHPEWNSSEYALSRILFEGFITACQHHIAE 250
GATase pfam00117
Glutamine amidotransferase class-I;
19-204 8.78e-12

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 62.26  E-value: 8.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   19 YVEAIIKAG---GCPIVIYPglqrNSIPP------NIDGIILAGGesvhpnrygedfdPNAPKSVDVIRDstewgMIDFA 89
Cdd:pfam00117   9 FTYNLARALrelGVEVTVVP----NDTPAeeileeNPDGIILSGG-------------PGSPGAAGGAIE-----AIREA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   90 LKKKIPILGICRGCQVLNVYFGGSLYqnvsscgfrdiHRPSKPRHYLAHKVMAKPGKLKNILGSNVI---------DVNS 160
Cdd:pfam00117  67 RELKIPILGICLGHQLLALAFGGKVV-----------KAKKFGHHGKNSPVGDDGCGLFYGLPNVFIvrryhsyavDPDT 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 429241401  161 IHDqGIKTLGmglqstVISDDGLCEGIESKDGLIIGVQWHPEAI 204
Cdd:pfam00117 136 LPD-GLEVTA------TSENDGTIMGIRHKKLPIFGVQFHPESI 172
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 45-203 5.40e-11

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: 59.82  E-value: 5.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  45 NIDGIILAGGESvhpnrygedfDPN-APKSVDVIRDstewgmidfALKKKIPILGICRGCQVLNVYFGGSLYQnvsscgf 123
Cdd:cd01744   39 DPDGIFLSNGPG----------DPAlLDEAIKTVRK---------LLGKKIPIFGICLGHQLLALALGAKTYK------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 124 rdihrpSKPRHYlahkvmakpgklknilGSN--VIDVNS----I----HDQGI--KTLGMGLQSTVIS-DDGLCEGIESK 190
Cdd:cd01744   93 ------MKFGHR----------------GSNhpVKDLITgrvyItsqnHGYAVdpDSLPGGLEVTHVNlNDGTVEGIRHK 150

                        170
                 ....*....|...
gi 429241401 191 DGLIIGVQWHPEA 203
Cdd:cd01744  151 DLPVFSVQFHPEA 163
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 45-219 6.10e-11

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: 59.47  E-value: 6.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  45 NIDGIILAGG-ESVHpnrygedfDPNAPKSVDVIrdstewgmidfaLKKKIPILGICRGCQVLNVYFGGSlyqnvsscgf 123
Cdd:cd01742   41 NPKGIILSGGpSSVY--------EEDAPRVDPEI------------FELGVPVLGICYGMQLIAKALGGK---------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 124 rdIHRPSKPRHYLAHKVMAKPGKL-KNIlgSNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESKDGLIIGVQWHPE 202
Cdd:cd01742   91 --VERGDKREYGKAEIEIDDSSPLfEGL--PDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPE 166

                        170
                 ....*....|....*..
gi 429241401 203 aiIDKQPHSLKLFQYFI 219
Cdd:cd01742  167 --VTHTEKGKEILKNFL 181
PRK13566 PRK13566
anthranilate synthase component I;
86-204 9.41e-11

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 61.47  E-value: 9.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  86 IDFALKKKIPILGICRGCQVLNVYFGGSLYQnvsscgfrdihrpskprhyLAHKVMAKPGKLKNILGSNVID-------- 157
Cdd:PRK13566 591 IDAALARNLPIFGVCLGLQAIVEAFGGELGQ-------------------LAYPMHGKPSRIRVRGPGRLFSglpeeftv 651

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 429241401 158 --VNSIHDQgIKTLGMGLQSTVISDDGLCEGIESKDGLIIGVQWHPEAI 204
Cdd:PRK13566 652 grYHSLFAD-PETLPDELLVTAETEDGVIMAIEHKTLPVAAVQFHPESI 699
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 45-223 9.94e-11

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: 59.28  E-value: 9.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  45 NIDGIILAGGESvHPNrygedfdpNAPKSVDVIRdstewgmidfALKKKIPILGICRGCQVLNVYFGGSlyqnvsscgfr 124
Cdd:COG0512   42 APDGIVLSPGPG-TPE--------EAGISLEVIR----------AFAGKIPILGVCLGHQAIGEAFGGK----------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 125 dIHRPSKPRHylahkvmakpGKLKNIlgsnvidvnSIHDQGI--------------------KTLGMGLQSTVISDDGLC 184
Cdd:COG0512   92 -VVRAPEPMH----------GKTSPI---------THDGSGLfaglpnpftatryhslvvdrETLPDELEVTAWTEDGEI 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 429241401 185 EGIESKDGLIIGVQWHPEAIIdkQPHSLKLFQYFINRSK 223
Cdd:COG0512  152 MGIRHRELPIEGVQFHPESIL--TEHGHQLLANFLELAG 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 20-219 2.20e-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: 55.23  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  20 VEAIIKAGGCPIVIypglqRNSIPP-------NIDGIILAGGESvHPNrygedfdpNAPKSVDVIRdstewgmidfALKK 92
Cdd:cd01743   15 VQYLRELGAEVVVV-----RNDEITleelellNPDAIVISPGPG-HPE--------DAGISLEIIR----------ALAG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  93 KIPILGICRGCQVLNVYFGGslyqnvsscgfrDIHRPSKPRHylaHKVMA----KPGKLKNIlgSNVIDV---NSIHDQg 165
Cdd:cd01743   71 KVPILGVCLGHQAIAEAFGG------------KVVRAPEPMH---GKTSEihhdGSGLFKGL--PQPFTVgryHSLVVD- 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 429241401 166 IKTLGMGLQSTVISDDGLCEGIESKDGLIIGVQWHPEAIIdkQPHSLKLFQYFI 219
Cdd:cd01743  133 PDPLPDLLEVTASTEDGVIMALRHRDLPIYGVQFHPESIL--TEYGLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
68-220 2.21e-09

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 57.42  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  68 PNAPK----SVDVIRdstewgmidfALKKKIPILGICRGCQVLNVYFGGSLYQNVSSCG-------------FRDIHRPS 130
Cdd:PRK14607  54 PGRPEeagiSVEVIR----------HFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHgktspidhngkglFRGIPNPT 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 131 KPRHYlaHkvmakpgklknilgSNVIDVNSIHDQgiktlgmgLQSTVISDDGLCEGIESKDGLIIGVQWHPEAIIDKqpH 210
Cdd:PRK14607 124 VATRY--H--------------SLVVEEASLPEC--------LEVTAKSDDGEIMGIRHKEHPIFGVQFHPESILTE--E 177

                        170
                 ....*....|
gi 429241401 211 SLKLFQYFIN 220
Cdd:PRK14607 178 GKRILKNFLN 187
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 28-223 5.87e-09

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 54.37  E-value: 5.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  28 GCPIVIYpglqRNSIPP-------NIDGIILAGGesvhpnrygedfdPNAPK----SVDVIRdstewgmidfALKKKIPI 96
Cdd:PRK05670  23 GAEVVVY----RNDEITleeiealNPDAIVLSPG-------------PGTPAeagiSLELIR----------EFAGKVPI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  97 LGICRGCQVLNVYFGGslyqnvsscgfrDIHRPSKPRHylahkvmakpGKLKNILGSN-------------------VID 157
Cdd:PRK05670  76 LGVCLGHQAIGEAFGG------------KVVRAKEIMH----------GKTSPIEHDGsgifaglpnpftvtryhslVVD 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429241401 158 VNSIHDqgiktlgmGLQSTVISDDGLCEGIESKDGLIIGVQWHPEAIIdkQPHSLKLFQYFINRSK 223
Cdd:PRK05670 134 RESLPD--------CLEVTAWTDDGEIMGVRHKELPIYGVQFHPESIL--TEHGHKLLENFLELAR 189
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 3-230 8.79e-09

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 55.19  E-value: 8.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   3 CPIIALSVGFSNNSQPYveaiIKAGGCPIVIYPGL----QRNSIPPniDGIILAGGesvhpnrygedfdPNAPKSV-DVI 77
Cdd:CHL00197 193 LKIIVIDFGVKYNILRR----LKSFGCSITVVPATspyqDILSYQP--DGILLSNG-------------PGDPSAIhYGI 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  78 RDSTEWgmidfaLKKKIPILGICRGCQVLNVYFGGSLYQnvSSCGFRDIHRPSKPRhylahkvmakpgKLKNILGSN--- 154
Cdd:CHL00197 254 KTVKKL------LKYNIPIFGICMGHQILSLALEAKTFK--LKFGHRGLNHPSGLN------------QQVEITSQNhgf 313

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429241401 155 VIDVNSIHDQGIKTLGMGLqstvisDDGLCEGIESKDGLIIGVQWHPEAiiDKQPH-SLKLFQYFINRSKWHMKQSN 230
Cdd:CHL00197 314 AVNLESLAKNKFYITHFNL------NDGTVAGISHSPKPYFSVQYHPEA--SPGPHdADYLFEYFIEIIKHSKSSKN 382
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 43-203 1.92e-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: 53.41  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  43 PPNIDGIILAGG-ESVHpnrygeDFDPNAPKSVDVIRDstewgmidfALKKKIPILGICRGCQVLNVYFGGSLYQNVSSC 121
Cdd:COG0518   46 LEDPDGLILSGGpMSVY------DEDPWLEDEPALIRE---------AFELGKPVLGICYGAQLLAHALGGKVEPGPGRE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 122 -GFRDIHrpskprhylahkVMAKPGKLKNIlgSNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESKDgLIIGVQWH 200
Cdd:COG0518  111 iGWAPVE------------LTEADPLFAGL--PDEFTVWMSHGDTVTELPEGAEVLASSDNCPNQAFRYGR-RVYGVQFH 175


                 ...
gi 429241401 201 PEA 203
Cdd:COG0518  176 PEV 178
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 45-220 1.00e-07

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 51.95  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  45 NIDGIILAGGesvhPnryGedfDPNA-PKSVDVIRDstewgmidfALKKKIPILGICRGCQVLNVYFGGSLYqnvsscgf 123
Cdd:COG0505  217 NPDGVFLSNG----P---G---DPAAlDYAIETIRE---------LLGKGIPIFGICLGHQLLALALGAKTY-------- 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 124 rdihrpskprhylahkvmakpgKLKNi-lGSN--VIDVNS----I----HDQGI--KTL-GMGLQSTVIS-DDGLCEGIE 188
Cdd:COG0505  270 ----------------------KLKFghrGANhpVKDLETgrveItsqnHGFAVdeDSLpATDLEVTHVNlNDGTVEGLR 327

                        170       180       190
                 ....*....|....*....|....*....|...
gi 429241401 189 SKDGLIIGVQWHPEAiidkqPH-SLKLFQYFIN 220
Cdd:COG0505  328 HKDLPAFSVQYHPEAsp--gPHdSAYLFDRFIE 358
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-112 2.19e-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: 48.36  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   5 IIALSVGFSNNSQPYVEAIIKAGGCPIVIYPG---LQRNSIPPNIDGIILAGGESVHPNRYgedfdpNAPKSVDVIRDst 81
Cdd:cd01653    3 VLLFPGFEELELASPLDALREAGAEVDVVSPDggpVESDVDLDDYDGLILPGGPGTPDDLA------RDEALLALLRE-- 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 429241401  82 ewgmidfALKKKIPILGICRGCQVLNVYFGG 112
Cdd:cd01653   75 -------AAAAGKPILGICLGAQLLVLGVQF 98
guaA PRK00074
GMP synthase; Reviewed
 45-202 9.05e-07

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 49.28  E-value: 9.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  45 NIDGIILAGG-ESVHpnrygedfDPNAPKSVDVIrdstewgmidFALKkkIPILGICRGCQVLNVYFGGSLyqnvsscgf 123
Cdd:PRK00074  46 NPKGIILSGGpASVY--------EEGAPRADPEI----------FELG--VPVLGICYGMQLMAHQLGGKV--------- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 124 rdihRPSKPRHY-LAH-KVMAKPGKLKNIlgSNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESKDGLIIGVQWHP 201
Cdd:PRK00074  97 ----ERAGKREYgRAElEVDNDSPLFKGL--PEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEERKFYGVQFHP 170


                 .
gi 429241401 202 E 202
Cdd:PRK00074 171 E 171
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
45-220 1.08e-06

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 48.92  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  45 NIDGIILAGGesvhPnryGedfDPNAPKS-VDVIRDstewgmidfALKKKIPILGICRGCQVLNVYFGGSLYqnvsscgf 123
Cdd:PRK12564 218 NPDGVFLSNG----P---G---DPAALDYaIEMIRE---------LLEKKIPIFGICLGHQLLALALGAKTY-------- 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 124 rdihrpskprhylahkvmakpgKLK------NI----LGSNVIDVNSiHDQG----IKTLGMGLQSTVIS-DDGLCEGIE 188
Cdd:PRK12564 271 ----------------------KMKfghrgaNHpvkdLETGKVEITS-QNHGfavdEDSLPANLEVTHVNlNDGTVEGLR 327

                        170       180       190
                 ....*....|....*....|....*....|...
gi 429241401 189 SKDGLIIGVQWHPEAiidkqPH-SLKLFQYFIN 220
Cdd:PRK12564 328 HKDLPAFSVQYHPEAsp--gPHdSAYLFDEFVE 358
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 48-202 1.31e-06

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: 47.31  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   48 GIILAGG-ESVhpnrYGEdfdpNAPKSVDVIRDStewgmidfalkkKIPILGICRGCQVLNVYFGGslyqnvsscgfrDI 126
Cdd:TIGR00888  44 GIILSGGpSSV----YAE----NAPRADEKIFEL------------GVPVLGICYGMQLMAKQLGG------------EV 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429241401  127 HRPSKPRHYLAHKVMAKPGKLKNILGsNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESKDGLIIGVQWHPE 202
Cdd:TIGR00888  92 GRAEKREYGKAELEILDEDDLFRGLP-DESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYGVQFHPE 166
PLN02347 PLN02347
GMP synthetase
 49-219 1.91e-06

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 48.53  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  49 IILAGG-ESVHpnrygedfDPNAPKSVDvirdstewGMIDFALKKKIPILGICRGCQVLNVYFGGSLyqnvsscgfrdih 127
Cdd:PLN02347  57 VILSGGpHSVH--------VEGAPTVPE--------GFFDYCRERGVPVLGICYGMQLIVQKLGGEV------------- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 128 RPSKPRHY--LAHKVMAKPGKLKNILGSNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESKDGLIIGVQWHPEaiI 205
Cdd:PLN02347 108 KPGEKQEYgrMEIRVVCGSQLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPE--V 185

                        170
                 ....*....|....
gi 429241401 206 DKQPHSLKLFQYFI 219
Cdd:PLN02347 186 THSPKGMETLRHFL 199
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 45-205 2.03e-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: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  45 NIDGIILAGGE-SVHPNRYgedfdPNAPKSVDVIRDstewgmidfALKKKIPILGICRGCQVLNVYFGGSLYQNVS--SC 121
Cdd:cd01741   46 DYDGLVILGGPmSVDEDDY-----PWLKKLKELIRQ---------ALAAGKPVLGICLGHQLLARALGGKVGRNPKgwEI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 122 GFRDIHRPSKPRHYLAHKVMAKPgklknilgsnvIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIeSKDGLIIGVQWHP 201
Cdd:cd01741  112 GWFPVTLTEAGKADPLFAGLPDE-----------FPVFHWHGDTVVELPPGAVLLASSEACPNQAF-RYGDRALGLQFHP 179


                 ....
gi 429241401 202 EAII 205
Cdd:cd01741  180 EERL 183
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-106 5.54e-06

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: 43.73  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   5 IIALSVGFSNNSQPYVEAIIKAGGCPIVIYPGLQRNSI---PPNIDGIILAGGESVHPNRYgedfdpNAPKSVDVIRDst 81
Cdd:cd03128    3 VLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVESdvdLDDYDGLILPGGPGTPDDLA------WDEALLALLRE-- 74

                         90       100
                 ....*....|....*....|....*
gi 429241401  82 ewgmidfALKKKIPILGICRGCQVL 106
Cdd:cd03128   75 -------AAAAGKPVLGICLGAQLL 92
PRK00758 PRK00758
GMP synthase subunit A; Validated
 40-202 8.53e-06

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 44.84  E-value: 8.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  40 NSIPP-----NIDGIILAGGESVHpnRYGedfdpNAPksvdvirdstewgmiDFALKKKIPILGICRGCQVLNVYFGGSl 114
Cdd:PRK00758  31 NTTPVeeikaFEDGLILSGGPDIE--RAG-----NCP---------------EYLKELDVPILGICLGHQLIAKAFGGE- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 115 yqnvsscgfrdIHRPSKPRHYLAH-KVMAKPGKLKNIlgSNVIDVNSIHDQGIKTLGMGLQSTVISDdgLC--EGIESKD 191
Cdd:PRK00758  88 -----------VGRGEYGEYALVEvEILDEDDILKGL--PPEIRVWASHADEVKELPDGFEILARSD--ICevEAMKHKE 152

                        170
                 ....*....|.
gi 429241401 192 GLIIGVQWHPE 202
Cdd:PRK00758 153 KPIYGVQFHPE 163
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
47-221 1.52e-05

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 44.52  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  47 DGIILAGGESVHPNRYGEDFDPNAPK----SVDVIRDstewgmidFAlkKKIPILGICRGCQVLNVYFGGSLYQNVsscg 122
Cdd:PRK08007  32 DALTLADIDALKPQKIVISPGPCTPDeagiSLDVIRH--------YA--GRLPILGVCLGHQAMAQAFGGKVVRAA---- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 123 fRDIHRPSKPrhyLAHKvmaKPGKLKNIlgSNVIDVNSIHDQGIK--TLGMGLQSTVISDDGLCEGIESKDGLIIGVQWH 200
Cdd:PRK08007  98 -KVMHGKTSP---ITHN---GEGVFRGL--ANPLTVTRYHSLVVEpdSLPACFEVTAWSETREIMGIRHRQWDLEGVQFH 168

                        170       180
                 ....*....|....*....|.
gi 429241401 201 PEAIIDKQPHslKLFQYFINR 221
Cdd:PRK08007 169 PESILSEQGH--QLLANFLHR 187
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 93-205 1.00e-04

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 42.14  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  93 KIPILGICRGCQVLNVYFGGSlyqnVSSCGfrDIHRPSKP--------RHYLAH--KVMAKPGKlKNILGSNViDVNSIH 162
Cdd:PRK05637  73 QIPLLGICLGFQALLEHHGGK----VEPCG--PVHGTTDNmiltdagvQSPVFAglATDVEPDH-PEIPGRKV-PIARYH 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 429241401 163 DQGIKTLGMGLQSTVISDDGLCEGI---ESKDGLIIGVQWHPEAII 205
Cdd:PRK05637 145 SLGCVVAPDGMESLGTCSSEIGPVImaaETTDGKAIGLQFHPESVL 190
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 93-221 3.09e-04

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 40.54  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401   93 KIPILGICRGCQVLNVYFGGSLYQ----------NVSSCG---FRDIHRPSKPRHYlaHKVMAKPGKLKNILgsnviDVN 159
Cdd:TIGR00566  72 KLPILGVCLGHQAMGQAFGGDVVRantvmhgktsEIEHNGagiFRGLFNPLTATRY--HSLVVEPETLPTCF-----PVT 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429241401  160 SIHDQGIKTLgmglqstvisddglceGIESKDGLIIGVQWHPEAIIDKQPHslKLFQYFINR 221
Cdd:TIGR00566 145 AWEEENIEIM----------------AIRHRDLPLEGVQFHPESILSEQGH--QLLANFLHR 188
trpG CHL00101
anthranilate synthase component 2
 45-222 3.76e-04

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 40.48  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  45 NIDGIILAGGESvHPNRYGedfdpnapKSVDVIRdstewgmidfALKKKIPILGICRGCQVLNVYFGGSlyqnvsscgfr 124
Cdd:CHL00101  43 NIRHIIISPGPG-HPRDSG--------ISLDVIS----------SYAPYIPILGVCLGHQSIGYLFGGK----------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 125 dIHRPSKPRHYLAHKVMAKPGKL-KNILG--------SNVIDVNSIHDQgiktlgmgLQSTVISDDGLCEGIESKD-GLI 194
Cdd:CHL00101  93 -IIKAPKPMHGKTSKIYHNHDDLfQGLPNpftatryhSLIIDPLNLPSP--------LEITAWTEDGLIMACRHKKyKML 163

                        170       180
                 ....*....|....*....|....*...
gi 429241401 195 IGVQWHPEAIIDKqpHSLKLFQYFINRS 222
Cdd:CHL00101 164 RGIQFHPESLLTT--HGQQILRNFLSLS 189
PLN02335 PLN02335
anthranilate synthase
 94-205 2.53e-03

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 38.24  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  94 IPILGICRGCQVLNVYFGGSLYQnvSSCGFrdIHRPSKPRHYLAHKVMAKPGKLKNILG-----SNVIDVNSI-HDQgik 167
Cdd:PLN02335  92 VPLFGVCMGLQCIGEAFGGKIVR--SPFGV--MHGKSSPVHYDEKGEEGLFSGLPNPFTagryhSLVIEKDTFpSDE--- 164

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 429241401 168 tlgmgLQSTVISDDGLCEGIESKD-GLIIGVQWHPEAII 205
Cdd:PLN02335 165 -----LEVTAWTEDGLIMAARHRKyKHIQGVQFHPESII 198
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
47-222 5.41e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 36.78  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401  47 DGIILAGGESVHPNRYGEDFDPNAPKSVDVIRDSTEwgmidfALKKKIPILGICRGCQVLNVYFGG-------------S 113
Cdd:PRK08857  32 DEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIE------HFAGKLPILGVCLGHQAIAQVFGGqvvrarqvmhgktS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241401 114 LYQNVSSCGFRDIHRPSKPRHYlaHKVMAKPGKLKNILGsnvIDVNSIHDQGIKTLGMGLQSTVISddglcegieskdgl 193
Cdd:PRK08857 106 PIRHTGRSVFKGLNNPLTVTRY--HSLVVKNDTLPECFE---LTAWTELEDGSMDEIMGFQHKTLP-------------- 166

                        170       180
                 ....*....|....*....|....*....
gi 429241401 194 IIGVQWHPEAIIDKQPHslKLFQYFINRS 222
Cdd:PRK08857 167 IEAVQFHPESIKTEQGH--QLLANFLART 193
 
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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