NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499345678|ref|WP_011035217|]
View 

MULTISPECIES: type 1 glutamine amidotransferase [Methanosarcina]

Protein Classification

type 1 glutamine amidotransferase( domain architecture ID 11424847)

type 1 glutamine amidotransferase may be involved in the hydrolysis of ammonia from glutamine and the transfer of the amino group to an acceptor substrate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-227 3.51e-80

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: 239.46  E-value: 3.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   2 KIHCIQHVRFE--VPGTINEWIEEKNHLLSTTHAYESENFPETGS---FDLLLVMGGPMNIYEYDkyPWLKEEKKFLEKA 76
Cdd:COG0518    1 KILILDHDPFGgqYPGLIARRLREAGIELDVLRVYAGEILPYDPDledPDGLILSGGPMSVYDED--PWLEDEPALIREA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  77 VSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVKDGkselSILEGMPEKFTAFHWHGDTFG-LPEGAKRLFE 155
Cdd:COG0518   79 FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEAD----PLFAGLPDEFTVWMSHGDTVTeLPEGAEVLAS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499345678 156 SQACKNQGFIYGDRVIGLQFHLEMSEQSIRNVIENCRDEfvegkyIQRENEMLDRKDYLTESKKLMFRLMDN 227
Cdd:COG0518  155 SDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADE------LAAEELLAEASLHDPELREAGRRLLRN 220
 
Name Accession Description Interval E-value
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-227 3.51e-80

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: 239.46  E-value: 3.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   2 KIHCIQHVRFE--VPGTINEWIEEKNHLLSTTHAYESENFPETGS---FDLLLVMGGPMNIYEYDkyPWLKEEKKFLEKA 76
Cdd:COG0518    1 KILILDHDPFGgqYPGLIARRLREAGIELDVLRVYAGEILPYDPDledPDGLILSGGPMSVYDED--PWLEDEPALIREA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  77 VSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVKDGkselSILEGMPEKFTAFHWHGDTFG-LPEGAKRLFE 155
Cdd:COG0518   79 FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEAD----PLFAGLPDEFTVWMSHGDTVTeLPEGAEVLAS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499345678 156 SQACKNQGFIYGDRVIGLQFHLEMSEQSIRNVIENCRDEfvegkyIQRENEMLDRKDYLTESKKLMFRLMDN 227
Cdd:COG0518  155 SDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADE------LAAEELLAEASLHDPELREAGRRLLRN 220
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 2-178 2.19e-73

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: 220.96  E-value: 2.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   2 KIHCIQHVRFEVPGTINEWIEEKNHL---LSTTHAYESENFPETGSFDLLLVMGGPMNIyEYDKYPWLKEEKKFLEKAVS 78
Cdd:cd01741    1 RILILQHDTPEGPGLFEDLLREAGAEtieIDVVDVYAGELLPDLDDYDGLVILGGPMSV-DEDDYPWLKKLKELIRQALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  79 EGKAVLGICLGAQLLADVLKAKVFKNDYK-EIGWFPVSVVKDGKsELSILEGMPEKFTAFHWHGDTF-GLPEGAKRLFES 156
Cdd:cd01741   80 AGKPVLGICLGHQLLARALGGKVGRNPKGwEIGWFPVTLTEAGK-ADPLFAGLPDEFPVFHWHGDTVvELPPGAVLLASS 158

                        170       180
                 ....*....|....*....|..
gi 499345678 157 QACKNQGFIYGDRVIGLQFHLE 178
Cdd:cd01741  159 EACPNQAFRYGDRALGLQFHPE 180
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 1-231 9.34e-54

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 172.84  E-value: 9.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   1 MKIHCIQHVRFEVPGTINEWIEEKNHLLSTTHAYESENFPETGS-FDLLLVMGGPMN-IYEYDKYPWL--KEEKKFLEKA 76
Cdd:PRK08250   1 MRVHFIIHESFEAPGAYLKWAENRGYDISYSRVYAGEALPENADgFDLLIVMGGPQSpRTTREECPYFdsKAEQRLINQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  77 VSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVKDGKSElsilegmpEKFTAF-------HWHGDTFGLPEG 149
Cdd:PRK08250  81 IKAGKAVIGVCLGAQLIGEALGAKYEHSPEKEIGYFPITLTEAGLKD--------PLLSHFgstltvgHWHNDMPGLTDQ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678 150 AKRLFESQACKNQGFIYGDRVIGLQFHLEMSEQSIRNVIENCRDEFVEGK---YIQRENEMLDrKDYlTESKKLMFRLMD 226
Cdd:PRK08250 153 AKVLATSEGCPRQIVQYSNLVYGFQCHMEFTVEAVELLIAHSQQELSQAQgkrFVQSPEELRA-WDY-SEMNQKLFRFLD 230


                 ....*
gi 499345678 227 NIEKA 231
Cdd:PRK08250 231 KLTLA 235
GATase pfam00117
Glutamine amidotransferase class-I;
45-178 3.74e-16

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 73.81  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   45 FDLLLVMGGPMNIYEYDkypwlkEEKKFLEKAVSEGKAVLGICLGAQLLADVLKAKVFKN-DYKEIGWfpVSVVKDGKSE 123
Cdd:pfam00117  41 PDGIILSGGPGSPGAAG------GAIEAIREARELKIPILGICLGHQLLALAFGGKVVKAkKFGHHGK--NSPVGDDGCG 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  124 LsiLEGMPEKFTAFHWHGDTF---GLPEGAKRLFESQ-ACKNQGFIY-GDRVIGLQFHLE 178
Cdd:pfam00117 113 L--FYGLPNVFIVRRYHSYAVdpdTLPDGLEVTATSEnDGTIMGIRHkKLPIFGVQFHPE 170
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 68-198 1.84e-04

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 41.16  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   68 EEKKFLEKAVSEGKAVLGICLGAQLLAD------------VLKAKVFK-NDYK--EIGWFPVSVVKDGKselsILEGMPE 132
Cdd:TIGR01855  59 GLDLFVELVVRLGKPVLGICLGMQLLFErseegggvpglgLIKGNVVKlEARKvpHMGWNEVHPVKESP----LLNGIDE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499345678  133 KFTAFHWHgdTFGLPegakrlfesqaCKNQGFI----YG---------DRVIGLQFHLEMSEQSIRNVIENcrdeFVEG 198
Cdd:TIGR01855 135 GAYFYFVH--SYYAV-----------CEEEAVLayadYGekfpaavqkGNIFGTQFHPEKSGKTGLKLLEN----FLEL 196
 
Name Accession Description Interval E-value
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-227 3.51e-80

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: 239.46  E-value: 3.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   2 KIHCIQHVRFE--VPGTINEWIEEKNHLLSTTHAYESENFPETGS---FDLLLVMGGPMNIYEYDkyPWLKEEKKFLEKA 76
Cdd:COG0518    1 KILILDHDPFGgqYPGLIARRLREAGIELDVLRVYAGEILPYDPDledPDGLILSGGPMSVYDED--PWLEDEPALIREA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  77 VSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVKDGkselSILEGMPEKFTAFHWHGDTFG-LPEGAKRLFE 155
Cdd:COG0518   79 FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEAD----PLFAGLPDEFTVWMSHGDTVTeLPEGAEVLAS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499345678 156 SQACKNQGFIYGDRVIGLQFHLEMSEQSIRNVIENCRDEfvegkyIQRENEMLDRKDYLTESKKLMFRLMDN 227
Cdd:COG0518  155 SDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADE------LAAEELLAEASLHDPELREAGRRLLRN 220
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 2-178 2.19e-73

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: 220.96  E-value: 2.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   2 KIHCIQHVRFEVPGTINEWIEEKNHL---LSTTHAYESENFPETGSFDLLLVMGGPMNIyEYDKYPWLKEEKKFLEKAVS 78
Cdd:cd01741    1 RILILQHDTPEGPGLFEDLLREAGAEtieIDVVDVYAGELLPDLDDYDGLVILGGPMSV-DEDDYPWLKKLKELIRQALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  79 EGKAVLGICLGAQLLADVLKAKVFKNDYK-EIGWFPVSVVKDGKsELSILEGMPEKFTAFHWHGDTF-GLPEGAKRLFES 156
Cdd:cd01741   80 AGKPVLGICLGHQLLARALGGKVGRNPKGwEIGWFPVTLTEAGK-ADPLFAGLPDEFPVFHWHGDTVvELPPGAVLLASS 158

                        170       180
                 ....*....|....*....|..
gi 499345678 157 QACKNQGFIYGDRVIGLQFHLE 178
Cdd:cd01741  159 EACPNQAFRYGDRALGLQFHPE 180
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 1-231 9.34e-54

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 172.84  E-value: 9.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   1 MKIHCIQHVRFEVPGTINEWIEEKNHLLSTTHAYESENFPETGS-FDLLLVMGGPMN-IYEYDKYPWL--KEEKKFLEKA 76
Cdd:PRK08250   1 MRVHFIIHESFEAPGAYLKWAENRGYDISYSRVYAGEALPENADgFDLLIVMGGPQSpRTTREECPYFdsKAEQRLINQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  77 VSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVKDGKSElsilegmpEKFTAF-------HWHGDTFGLPEG 149
Cdd:PRK08250  81 IKAGKAVIGVCLGAQLIGEALGAKYEHSPEKEIGYFPITLTEAGLKD--------PLLSHFgstltvgHWHNDMPGLTDQ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678 150 AKRLFESQACKNQGFIYGDRVIGLQFHLEMSEQSIRNVIENCRDEFVEGK---YIQRENEMLDrKDYlTESKKLMFRLMD 226
Cdd:PRK08250 153 AKVLATSEGCPRQIVQYSNLVYGFQCHMEFTVEAVELLIAHSQQELSQAQgkrFVQSPEELRA-WDY-SEMNQKLFRFLD 230


                 ....*
gi 499345678 227 NIEKA 231
Cdd:PRK08250 231 KLTLA 235
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 1-184 1.87e-52

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 169.36  E-value: 1.87e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   1 MK-IHCIQHVRFEVPGTINEWIEEKNHLLSTTHAYESE-NFPETGSFDLLLVMGGPMNIYEYDKYPWLKEEKKFLEKAVS 78
Cdd:PRK07053   2 MKtAVAIRHVAFEDLGSFEQVLGARGYRVRYVDVGVDDlETLDALEPDLLVVLGGPIGVYDDELYPFLAPEIALLRQRLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  79 EGKAVLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVKDGKSelSILEGMPEKFTAFHWHGDTFGLPEGAKRLFESQA 158
Cdd:PRK07053  82 AGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPLTLTDAGRA--SPLRHLGAGTPVLHWHGDTFDLPEGATLLASTPA 159

                        170       180
                 ....*....|....*....|....*.
gi 499345678 159 CKNQGFIYGDRVIGLQFHLEMSEQSI 184
Cdd:PRK07053 160 CRHQAFAWGNHVLALQFHPEAREDRF 185
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 50-178 5.32e-27

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 103.50  E-value: 5.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  50 VMGGPM--NiyeyDKYPWLKEEKKFLEKAVSEGKAVLGICLGAQLLADVLKAKVFKND--YKEIGWFPVSVVKDGKSels 125
Cdd:PRK06490  58 IFGGPMsaN----DPDDFIRREIDWISVPLKENKPFLGICLGAQMLARHLGARVAPHPdgRVEIGYYPLRPTEAGRA--- 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499345678 126 iLEGMPEkfTAFHWHGDTFGLPEGAKRLFESQACKNQGFIYGDRVIGLQFHLE 178
Cdd:PRK06490 131 -LMHWPE--MVYHWHREGFDLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPE 180
GATase pfam00117
Glutamine amidotransferase class-I;
45-178 3.74e-16

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 73.81  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   45 FDLLLVMGGPMNIYEYDkypwlkEEKKFLEKAVSEGKAVLGICLGAQLLADVLKAKVFKN-DYKEIGWfpVSVVKDGKSE 123
Cdd:pfam00117  41 PDGIILSGGPGSPGAAG------GAIEAIREARELKIPILGICLGHQLLALAFGGKVVKAkKFGHHGK--NSPVGDDGCG 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  124 LsiLEGMPEKFTAFHWHGDTF---GLPEGAKRLFESQ-ACKNQGFIY-GDRVIGLQFHLE 178
Cdd:pfam00117 113 L--FYGLPNVFIVRRYHSYAVdpdTLPDGLEVTATSEnDGTIMGIRHkKLPIFGVQFHPE 170
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 52-178 2.02e-15

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: 71.41  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  52 GGPMNIYEyDKYPWLKEEkkflekAVSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGwfPVSVVKDGKSELsiLEGMP 131
Cdd:cd01742   49 GGPSSVYE-EDAPRVDPE------IFELGVPVLGICYGMQLIAKALGGKVERGDKREYG--KAEIEIDDSSPL--FEGLP 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499345678 132 EKFTAFHWHGDTFG-LPEGAKRLFESQACKNQGFIYGDRVI-GLQFHLE 178
Cdd:cd01742  118 DEQTVWMSHGDEVVkLPEGFKVIASSDNCPVAAIANEEKKIyGVQFHPE 166
PRK00758 PRK00758
GMP synthase subunit A; Validated
 83-194 4.29e-14

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 67.95  E-value: 4.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  83 VLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVKdgksELSILEGMPEKFTAFHWHGDTF-GLPEGAKRLFESQACKN 161
Cdd:PRK00758  70 ILGICLGHQLIAKAFGGEVGRGEYGEYALVEVEILD----EDDILKGLPPEIRVWASHADEVkELPDGFEILARSDICEV 145

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499345678 162 QGFIYGDRVI-GLQFHLEMS-----EQSIRNVIENCRDE 194
Cdd:PRK00758 146 EAMKHKEKPIyGVQFHPEVAhteygEEIFKNFLEICGKY 184
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 33-180 3.42e-13

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 66.52  E-value: 3.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  33 AYESENFPETGSFDLLLVMGGPMNIYeyDKYPWLKEEKKFLEKAVSEGKAVLGICLGAQLLADVLKAKVfknDY----KE 108
Cdd:PRK09065  43 VFAGEPLPAPDDFAGVIITGSWAMVT--DRLDWSERTADWLRQAAAAGMPLLGICYGHQLLAHALGGEV---GYnpagRE 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499345678 109 IGWFPVSVVKDGKSElSILEGMPEKFTAFHWHGDT-FGLPEGAKRLFESQACKNQGFIYGDRVIGLQFHLEMS 180
Cdd:PRK09065 118 SGTVTVELHPAAADD-PLFAGLPAQFPAHLTHLQSvLRLPPGAVVLARSAQDPHQAFRYGPHAWGVQFHPEFT 189
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 45-194 6.95e-12

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 63.04  E-value: 6.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  45 FDLLLVMGGPMNI--YEYDKYPWL----KEEKKFLEKAVSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVK 118
Cdd:PRK07567  52 YSGVIVGGSPFNVsdPAESKSPWQrrveAELSGLLDEVVARDFPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVSLTD 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499345678 119 DGKSElSILEGMPEKFTAFHWHGD-TFGLPEGAKRLFESQACKNQGFIYGDRVIGLQFHLEMSEQSIRNVIENCRDE 194
Cdd:PRK07567 132 AGRAD-PLLAGLPDTFTAFVGHKEaVSALPPGAVLLATSPTCPVQMFRVGENVYATQFHPELDADGLKTRIDFYRDH 207
PLN02347 PLN02347
GMP synthetase
 52-180 1.72e-10

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 60.08  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  52 GGPMNIYEyDKYPWLKEEkkFLEKAVSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGWFPVSVVKDgkSELSILEGMP 131
Cdd:PLN02347  61 GGPHSVHV-EGAPTVPEG--FFDYCRERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCG--SQLFGDLPSG 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499345678 132 EKFTAFHWHGD-TFGLPEGakrlFESQACKNQGFIYG-----DRVIGLQFHLEMS 180
Cdd:PLN02347 136 ETQTVWMSHGDeAVKLPEG----FEVVAKSVQGAVVAienreRRIYGLQYHPEVT 186
guaA PRK00074
GMP synthase; Reviewed
 52-178 1.87e-09

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 56.98  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  52 GGPMNIYEyDKYPwlkeekkFLEKAVSE-GKAVLGICLGAQLLADVLKAKVFKNDYKEIGwfPVSVVKDGKSELsiLEGM 130
Cdd:PRK00074  54 GGPASVYE-EGAP-------RADPEIFElGVPVLGICYGMQLMAHQLGGKVERAGKREYG--RAELEVDNDSPL--FKGL 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499345678 131 PEKFTAfhW--HGDTFG-LPEGAKRLFESQACKNQGFIYGDRVI-GLQFHLE 178
Cdd:PRK00074 122 PEEQDV--WmsHGDKVTeLPEGFKVIASTENCPIAAIANEERKFyGVQFHPE 171
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 45-93 2.16e-09

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: 53.76  E-value: 2.16e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 499345678  45 FDLLLVMGGPMNIYEYDkypWLKEEKKFLEKAVSEGKAVLGICLGAQLL 93
Cdd:cd01653   47 YDGLILPGGPGTPDDLA---RDEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 45-93 2.40e-09

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: 52.97  E-value: 2.40e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 499345678  45 FDLLLVMGGPMNIYEYDkypWLKEEKKFLEKAVSEGKAVLGICLGAQLL 93
Cdd:cd03128   47 YDGLILPGGPGTPDDLA---WDEALLALLREAAAAGKPVLGICLGAQLL 92
PRK05665 PRK05665
amidotransferase; Provisional
 40-200 3.41e-09

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 55.20  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  40 PETGSFDLLLVMGGPMNIYEYDkyPWLKEEKKFLEKAVSEGKAVLGICLGAQLLADVLKAKVFK---------NDYKEIG 110
Cdd:PRK05665  53 ADDEKFDAYLVTGSKADSFGTD--PWIQTLKTYLLKLYERGDKLLGVCFGHQLLALLLGGKAERasqgwgvgiHRYQLAA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678 111 WFP-VSVVKDgksELSILEGMPEKFTAfhwhgdtfgLPEGAKRLFESQACKNQGFIYGDRVIGLQFHLEMSEQSIRNVIE 189
Cdd:PRK05665 131 HAPwMSPAVT---ELTLLISHQDQVTA---------LPEGATVIASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLD 198

                        170
                 ....*....|.
gi 499345678 190 NCRDEFVEGKY 200
Cdd:PRK05665 199 LRQEHLGEEVY 209
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 70-193 5.19e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 51.41  E-value: 5.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  70 KKFLEKAVSEGKAVLGICLGAQLL------------ADVLKAKV--FKNDYK--EIGWFPVSVVKDGKselsILEGMPEK 133
Cdd:PRK13143  61 RDVILEAARSGKPFLGICLGMQLLfesseegggvrgLGLFPGRVvrFPAGVKvpHMGWNTVKVVKDCP----LFEGIDGE 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499345678 134 FTAF-H-WHGDT-----------FGLPegakrlFESQACKnqgfiygDRVIGLQFHLEMSEQS----IRNVIENCRD 193
Cdd:PRK13143 137 YVYFvHsYYAYPddedyvvattdYGIE------FPAAVCN-------DNVFGTQFHPEKSGETglkiLENFVELIKR 200
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 83-193 2.11e-05

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: 43.87  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  83 VLGICLGAQLLADVLKAKVFKNDY----KeigwfpVSVVK-DGKselSILEGMPEKFTA--FH-WHGDTFGLPEGakrlF 154
Cdd:COG0512   74 ILGVCLGHQAIGEAFGGKVVRAPEpmhgK------TSPIThDGS---GLFAGLPNPFTAtrYHsLVVDRETLPDE----L 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499345678 155 ESQACKNQGFIYG-----DRVIGLQFHLE--MSE---QSIRNVIENCRD 193
Cdd:COG0512  141 EVTAWTEDGEIMGirhreLPIEGVQFHPEsiLTEhghQLLANFLELAGE 189
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 71-189 8.65e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 42.16  E-value: 8.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  71 KFLEKAVSEGKAVLGICLGAQLLAD-----------VLKAKV--FKNDYK---EIGWFPVSVVKDGKselsILEGMPEKF 134
Cdd:PRK13181  63 EALKEHVEKKQPVLGICLGMQLLFEsseegnvkglgLIPGDVkrFRSEPLkvpQMGWNSVKPLKESP----LFKGIEEGS 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499345678 135 TAFHWHgdTFGLPegakrlfesqaCKNQGFI-----YG---------DRVIGLQFHLEMS----EQSIRNVIE 189
Cdd:PRK13181 139 YFYFVH--SYYVP-----------CEDPEDVlatteYGvpfcsavakDNIYAVQFHPEKSgkagLKLLKNFAE 198
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 70-133 1.21e-04

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 41.71  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  70 KKFLEKAVSEGKAVLGICLGAQLLA------------DVLKAKV--FKNDYKE----IGWFPVSVVKDGKselsILEGMP 131
Cdd:cd01748   61 IEALKEAIASGKPFLGICLGMQLLFesseegggtkglGLIPGKVvrFPASEGLkvphMGWNQLEITKESP----LFKGIP 136


                 ..
gi 499345678 132 EK 133
Cdd:cd01748  137 DG 138
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 71-132 1.32e-04

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


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 41.56  E-value: 1.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499345678  71 KFLEKAVSEGKAVLGICLGAQLLAD------------VLKAKVFK---NDYK--EIGWFPVSVVKDGKselsILEGMPE 132
Cdd:COG0118   64 EAIREAVAGGKPVLGICLGMQLLFErseengdteglgLIPGEVVRfpaSDLKvpHMGWNTVEIAKDHP----LFAGIPD 138
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 75-192 1.36e-04

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 41.27  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  75 KAVSEGKAVLGICLGAQLLADVLKAKVFKNdyKEI--GwfPVSVVK-DGKselSILEGMPEKFTAFHWH---GDTFGLPE 148
Cdd:PRK05670  67 REFAGKVPILGVCLGHQAIGEAFGGKVVRA--KEImhG--KTSPIEhDGS---GIFAGLPNPFTVTRYHslvVDRESLPD 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499345678 149 GakrlFESQACKNQGFIYG-----DRVIGLQFHLE--MSE---QSIRNVIENCR 192
Cdd:PRK05670 140 C----LEVTAWTDDGEIMGvrhkeLPIYGVQFHPEsiLTEhghKLLENFLELAR 189
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 68-198 1.84e-04

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 41.16  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   68 EEKKFLEKAVSEGKAVLGICLGAQLLAD------------VLKAKVFK-NDYK--EIGWFPVSVVKDGKselsILEGMPE 132
Cdd:TIGR01855  59 GLDLFVELVVRLGKPVLGICLGMQLLFErseegggvpglgLIKGNVVKlEARKvpHMGWNEVHPVKESP----LLNGIDE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499345678  133 KFTAFHWHgdTFGLPegakrlfesqaCKNQGFI----YG---------DRVIGLQFHLEMSEQSIRNVIENcrdeFVEG 198
Cdd:TIGR01855 135 GAYFYFVH--SYYAV-----------CEEEAVLayadYGekfpaavqkGNIFGTQFHPEKSGKTGLKLLEN----FLEL 196
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 71-180 3.06e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 40.50  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  71 KFLEKAVSEGKAVLGICLGAQLLAD------------VLKAKV----FKNDYK--EIGWFPVSVVKdgksELSILEGMPE 132
Cdd:PRK13141  63 EVIKEAVASGKPLLGICLGMQLLFEsseefgeteglgLLPGRVrrfpPEEGLKvpHMGWNQLELKK----ESPLLKGIPD 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499345678 133 ----------------------------KFTAFHWHgdtfglpegakrlfesqacknqgfiygDRVIGLQFHLEMS 180
Cdd:PRK13141 139 gayvyfvhsyyadpcdeeyvaattdygvEFPAAVGK---------------------------DNVFGAQFHPEKS 187
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 71-178 4.56e-04

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: 39.79  E-value: 4.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  71 KFLEKAVSEGKAVLGICLGAQLLADVLKAKVFK--------NdykeigwFPVSVVKDGKSELsilegmpekfTAfHWHG- 141
Cdd:cd01744   60 KTVRKLLGKKIPIFGICLGHQLLALALGAKTYKmkfghrgsN-------HPVKDLITGRVYI----------TS-QNHGy 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499345678 142 --DTFGLPEGAKRLFES---QAckNQGFIYGDR-VIGLQFHLE 178
Cdd:cd01744  122 avDPDSLPGGLEVTHVNlndGT--VEGIRHKDLpVFSVQFHPE 162
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
83-233 8.98e-04

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 40.08  E-value: 8.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  83 VLGICLGAQLL-----ADVLKAKVFKNDYKEigwfpvSVVKDGKselSILEGMPEKFTAFHWH---GDTFGLPEgakrLF 154
Cdd:PRK14607  76 ILGVCLGHQAIgyafgGKIVHAKRILHGKTS------PIDHNGK---GLFRGIPNPTVATRYHslvVEEASLPE----CL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678 155 ESQACKNQGFIYGDR-----VIGLQFHLEmseqSI-----RNVIENcrdeFVegkYIQRenEMLDRKDYL---TESKKLM 221
Cdd:PRK14607 143 EVTAKSDDGEIMGIRhkehpIFGVQFHPE----SIlteegKRILKN----FL---NYQR--EEIDIKSYLkklVEGEDLS 209

                        170
                 ....*....|..
gi 499345678 222 FRLMDNIEKAIM 233
Cdd:PRK14607 210 FEEAEDVMEDIT 221
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 75-188 1.28e-03

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: 38.28  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678  75 KAVSEGKAVLGICLGAQLLADVLKAKVFKNDYKEIGwfPVSVVKDGKSelSILEGMPEKFTA--FH-WHGDTFGLPEgak 151
Cdd:cd01743   66 RALAGKVPILGVCLGHQAIAEAFGGKVVRAPEPMHG--KTSEIHHDGS--GLFKGLPQPFTVgrYHsLVVDPDPLPD--- 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499345678 152 rLFESQACKNQGFIYG-----DRVIGLQFHLE--MSEQS---IRNVI 188
Cdd:cd01743  139 -LLEVTASTEDGVIMAlrhrdLPIYGVQFHPEsiLTEYGlrlLENFL 184
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 73-118 6.37e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 36.68  E-value: 6.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 499345678  73 LEKAVSEGKAVLGICLGAQLLADvlkAKVFKNDYKEIGWFPVSVVK 118
Cdd:PRK13146  70 IEAVLAAGRPFLGICVGMQLLFE---RGLEHGDTPGLGLIPGEVVR 112
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 70-103 7.99e-03

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: 36.92  E-value: 7.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 499345678  70 KKFLEKavseGKAVLGICLGAQLLADVLKAKVFK 103
Cdd:COG0505  241 RELLGK----GIPIFGICLGHQLLALALGAKTYK 270
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 41-121 8.94e-03

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 35.70  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499345678   41 ETGSFDLLLVMGGpmniYEYDKYPWLKEE-KKFLEKAVSEGKAVLGICLGAQLL--ADVLKAK------VFKNDYKEIG- 110
Cdd:pfam01965  58 KPDDYDALVLPGG----RAGPERLRDNEKlVEFVKDFYEKGKPVAAICHGPQVLaaAGVLKGRkvtshpAVKDDLINAGa 133

                          90
                  ....*....|..
gi 499345678  111 -WFPVSVVKDGK 121
Cdd:pfam01965 134 tYVDKPVVVDGN 145
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH