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Conserved domains on  [gi|958159531|pdb|4WIN|B]
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Chain B, GMP synthetase

Protein Classification

DJ-1/PfpI family protein; aminodeoxychorismate/anthranilate synthase component II( domain architecture ID 10109723)

DJ-1/PfpI family protein, similar to Escherichia coli YajL, a covalent chaperone that protects cells against protein sulfenylation| aminodeoxychorismate/anthranilate synthase component II is part of a complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA), and anthranilate, an intermediate in the biosynthesis of L-tryptophan, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 21-237 3.40e-84

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: 248.60  E-value: 3.40e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       21 ILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEYflekKIPIFGI 100
Cdd:cd01742   1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFEL----GVPVLGI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B      101 CYGMQEIAVQMNGEVKKSKTSEYGCTDVNILrndninnitycrnfgdsssamdlysnyklmnETCCLFENIkSDITTVWM 180
Cdd:cd01742  77 CYGMQLIAKALGGKVERGDKREYGKAEIEID-------------------------------DSSPLFEGL-PDEQTVWM 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
4WIN_B      181 NHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFA 237
Cdd:cd01742 125 SHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKEILKNFL 181
 
Name Accession Description Interval E-value
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 21-237 3.40e-84

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: 248.60  E-value: 3.40e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       21 ILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEYflekKIPIFGI 100
Cdd:cd01742   1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFEL----GVPVLGI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B      101 CYGMQEIAVQMNGEVKKSKTSEYGCTDVNILrndninnitycrnfgdsssamdlysnyklmnETCCLFENIkSDITTVWM 180
Cdd:cd01742  77 CYGMQLIAKALGGKVERGDKREYGKAEIEID-------------------------------DSSPLFEGL-PDEQTVWM 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
4WIN_B      181 NHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFA 237
Cdd:cd01742 125 SHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKEILKNFL 181
guaA PRK00074
GMP synthase; Reviewed
 19-249 2.93e-78

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 244.57  E-value: 2.93e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        19 DKILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEYflekKIPIF 98
Cdd:PRK00074   4 DKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFEL----GVPVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        99 GICYGMQEIAVQMNGEVKKSKTSEYGCTDVNILrndninnitycrnfgdsssamdlysnyklmnETCCLFENIKSDiTTV 178
Cdd:PRK00074  80 GICYGMQLMAHQLGGKVERAGKREYGRAELEVD-------------------------------NDSPLFKGLPEE-QDV 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4WIN_B       179 WMNHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFAYNICKCKKQFDP 249
Cdd:PRK00074 128 WMSHGDKVTELPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTM 198
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 21-244 7.57e-70

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: 212.56  E-value: 7.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B         21 ILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEYflekKIPIFGI 100
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFEL----GVPVLGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        101 CYGMQEIAVQMNGEVKKSKTSEYGCTDVNILRNDNinnitycrnfgdsssamdlysnyklmnetccLFENIKSDItTVWM 180
Cdd:TIGR00888  77 CYGMQLMAKQLGGEVGRAEKREYGKAELEILDEDD-------------------------------LFRGLPDES-TVWM 124

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
4WIN_B        181 NHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFAYNICKCK 244
Cdd:TIGR00888 125 SHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVYDVCGCE 188
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 20-226 2.37e-41

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: 141.24  E-value: 2.37e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       20 KILVLN---FGSQYFHLIVKRLNNIKIFSETkdYGVELKDI----KDM-NIKGVILSGGPYSVTEAGsPHLKKE--VFEY 89
Cdd:COG0518   1 KILILDhdpFGGQYPGLIARRLREAGIELDV--LRVYAGEIlpydPDLeDPDGLILSGGPMSVYDED-PWLEDEpaLIRE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       90 FLEKKIPIFGICYGMQEIAVQMNGEVKKSKTSEYGCTDVNILRNDNinnitycrnfgdsssamdlysnyklmnetccLFE 169
Cdd:COG0518  78 AFELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADP-------------------------------LFA 126

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
4WIN_B      170 NIKSDItTVWMNHNDEVTKIPENFYLVSSSENCLICSIYNKEyNIYGVQYHPEVYES 226
Cdd:COG0518 127 GLPDEF-TVWMSHGDTVTELPEGAEVLASSDNCPNQAFRYGR-RVYGVQFHPEVTHT 181
GATase pfam00117
Glutamine amidotransferase class-I;
22-240 7.67e-37

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 128.12  E-value: 7.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B         22 LVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFLEKKIPIFGIC 101
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAG---GAIEAIREARELKIPILGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        102 YGMQEIAVQMNGEVKKSKTSEYGctdvnilrndninnitycrnfgdsssamdlYSNYKLMNETCCLFENIKSDItTVWMN 181
Cdd:pfam00117  78 LGHQLLALAFGGKVVKAKKFGHH------------------------------GKNSPVGDDGCGLFYGLPNVF-IVRRY 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
4WIN_B        182 HNDEVTK--IPENFYLVSSSEN-CLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFAYNI 240
Cdd:pfam00117 127 HSYAVDPdtLPDGLEVTATSENdGTIMGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
 
Name Accession Description Interval E-value
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 21-237 3.40e-84

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: 248.60  E-value: 3.40e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       21 ILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEYflekKIPIFGI 100
Cdd:cd01742   1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFEL----GVPVLGI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B      101 CYGMQEIAVQMNGEVKKSKTSEYGCTDVNILrndninnitycrnfgdsssamdlysnyklmnETCCLFENIkSDITTVWM 180
Cdd:cd01742  77 CYGMQLIAKALGGKVERGDKREYGKAEIEID-------------------------------DSSPLFEGL-PDEQTVWM 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
4WIN_B      181 NHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFA 237
Cdd:cd01742 125 SHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYGVQFHPEVTHTEKGKEILKNFL 181
guaA PRK00074
GMP synthase; Reviewed
 19-249 2.93e-78

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 244.57  E-value: 2.93e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        19 DKILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEYflekKIPIF 98
Cdd:PRK00074   4 DKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFEL----GVPVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        99 GICYGMQEIAVQMNGEVKKSKTSEYGCTDVNILrndninnitycrnfgdsssamdlysnyklmnETCCLFENIKSDiTTV 178
Cdd:PRK00074  80 GICYGMQLMAHQLGGKVERAGKREYGRAELEVD-------------------------------NDSPLFKGLPEE-QDV 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4WIN_B       179 WMNHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFAYNICKCKKQFDP 249
Cdd:PRK00074 128 WMSHGDKVTELPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTM 198
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 21-244 7.57e-70

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: 212.56  E-value: 7.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B         21 ILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEYflekKIPIFGI 100
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFEL----GVPVLGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        101 CYGMQEIAVQMNGEVKKSKTSEYGCTDVNILRNDNinnitycrnfgdsssamdlysnyklmnetccLFENIKSDItTVWM 180
Cdd:TIGR00888  77 CYGMQLMAKQLGGEVGRAEKREYGKAELEILDEDD-------------------------------LFRGLPDES-TVWM 124

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
4WIN_B        181 NHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFAYNICKCK 244
Cdd:TIGR00888 125 SHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVYDVCGCE 188
PLN02347 PLN02347
GMP synthetase
 10-242 4.21e-57

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 190.28  E-value: 4.21e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        10 GSMAEGEEYDKILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEY 89
Cdd:PLN02347   2 ESEAAKSYLDVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPEGFFDY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        90 FLEKKIPIFGICYGMQEIAVQMNGEVKKSKTSEYGCTDVNILRNdninnityCRNFGDSSSamdlysnyklmnetcclfe 169
Cdd:PLN02347  82 CRERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCG--------SQLFGDLPS------------------- 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4WIN_B       170 nikSDITTVWMNHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFAYNICK 242
Cdd:PLN02347 135 ---GETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCG 204
PRK00758 PRK00758
GMP synthase subunit A; Validated
 20-242 3.33e-50

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 162.33  E-value: 3.33e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        20 KILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNiKGVILSGGPySVTEAGSphlkkeVFEYFLEKKIPIFG 99
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAFE-DGLILSGGP-DIERAGN------CPEYLKELDVPILG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       100 ICYGMQEIAVQMNGEVKKSKTSEYGCTDVNILRNDNInnitycrnfgdsssamdlysnyklmnetcclFENIkSDITTVW 179
Cdd:PRK00758  73 ICLGHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDI-------------------------------LKGL-PPEIRVW 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
4WIN_B       180 MNHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFaYNICK 242
Cdd:PRK00758 121 ASHADEVKELPDGFEILARSDICEVEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNF-LEICG 182
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 20-226 2.37e-41

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: 141.24  E-value: 2.37e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       20 KILVLN---FGSQYFHLIVKRLNNIKIFSETkdYGVELKDI----KDM-NIKGVILSGGPYSVTEAGsPHLKKE--VFEY 89
Cdd:COG0518   1 KILILDhdpFGGQYPGLIARRLREAGIELDV--LRVYAGEIlpydPDLeDPDGLILSGGPMSVYDED-PWLEDEpaLIRE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       90 FLEKKIPIFGICYGMQEIAVQMNGEVKKSKTSEYGCTDVNILRNDNinnitycrnfgdsssamdlysnyklmnetccLFE 169
Cdd:COG0518  78 AFELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADP-------------------------------LFA 126

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
4WIN_B      170 NIKSDItTVWMNHNDEVTKIPENFYLVSSSENCLICSIYNKEyNIYGVQYHPEVYES 226
Cdd:COG0518 127 GLPDEF-TVWMSHGDTVTELPEGAEVLASSDNCPNQAFRYGR-RVYGVQFHPEVTHT 181
GATase pfam00117
Glutamine amidotransferase class-I;
22-240 7.67e-37

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 128.12  E-value: 7.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B         22 LVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFLEKKIPIFGIC 101
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAG---GAIEAIREARELKIPILGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        102 YGMQEIAVQMNGEVKKSKTSEYGctdvnilrndninnitycrnfgdsssamdlYSNYKLMNETCCLFENIKSDItTVWMN 181
Cdd:pfam00117  78 LGHQLLALAFGGKVVKAKKFGHH------------------------------GKNSPVGDDGCGLFYGLPNVF-IVRRY 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
4WIN_B        182 HNDEVTK--IPENFYLVSSSEN-CLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFAYNI 240
Cdd:pfam00117 127 HSYAVDPdtLPDGLEVTATSENdGTIMGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 52-236 8.45e-18

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: 78.54  E-value: 8.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       52 VELKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFlEKKIPIFGICYGMQEIAVQMNGEVKKS------KTSEygc 125
Cdd:COG0512  33 ITLEEIEALAPDGIVLSPGPGTPEEAG---ISLEVIRAF-AGKIPILGVCLGHQAIGEAFGGKVVRApepmhgKTSP--- 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B      126 tdvniLRNDNinnitycrnfgdsssamdlysnyklmnetCCLFENIKSDIT-------TVwmnhndEVTKIPENFYLVSS 198
Cdd:COG0512 106 -----ITHDG-----------------------------SGLFAGLPNPFTatryhslVV------DRETLPDELEVTAW 145

                       170       180       190
                ....*....|....*....|....*....|....*...
4WIN_B      199 SENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNF 236
Cdd:COG0512 146 TEDGEIMGIRHRELPIEGVQFHPESILTEHGHQLLANF 183
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 61-222 1.17e-16

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: 75.36  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       61 NIKGVILSGGPYSVTEAGSPHLKKEV-F-EYFLEKKIPIFGICYGMQEIAVQMNGEVKKS-KTSEYGCTDVNilRNDNIN 137
Cdd:cd01741  46 DYDGLVILGGPMSVDEDDYPWLKKLKeLiRQALAAGKPVLGICLGHQLLARALGGKVGRNpKGWEIGWFPVT--LTEAGK 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B      138 NITYCRNFGDSSSAMdlysnyklmnetcclfeniksdittVWmnHNDEVTKIPENFYLVSSSENCLIcSIYNKEYNIYGV 217
Cdd:cd01741 124 ADPLFAGLPDEFPVF-------------------------HW--HGDTVVELPPGAVLLASSEACPN-QAFRYGDRALGL 175


                ....*
4WIN_B      218 QYHPE 222
Cdd:cd01741 176 QFHPE 180
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 22-236 1.46e-14

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: 69.49  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       22 LVLNFGSQYFHLIVKRLNNIKifsetkdygveLKDIKDMNIKGVILSGGPysvteaGSPH---LKKEVFEYFlEKKIPIF 98
Cdd:cd01743  14 LVQYLRELGAEVVVVRNDEIT-----------LEELELLNPDAIVISPGP------GHPEdagISLEIIRAL-AGKVPIL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       99 GICYGMQEIAVQMNGEVKKSKTSEYGCTDVNILRNDNInnitycrnfgdsssamdlysnyklmnetcclFENIKSDITTV 178
Cdd:cd01743  76 GVCLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGL-------------------------------FKGLPQPFTVG 124

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
4WIN_B      179 ----WMnhndeVTKIPENFYLV--SSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNF 236
Cdd:cd01743 125 ryhsLV-----VDPDPLPDLLEvtASTEDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENF 183
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 54-236 3.71e-13

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 65.92  E-value: 3.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        54 LKDIKDMNIKGVILSGGPYSVTEAG-SPHLKKEvfeyfLEKKIPIFGICYGMQEIAVQMNGEVKKSKTSEYGCTDVniLR 132
Cdd:PRK05670  36 LEEIEALNPDAIVLSPGPGTPAEAGiSLELIRE-----FAGKVPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTSP--IE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       133 NDNinnitycrnfgdsssamdlysnyklmnetCCLFENIKSDITtVWMNHNDEVTK--IPENFYLVSSSENCLICSIYNK 210
Cdd:PRK05670 109 HDG-----------------------------SGIFAGLPNPFT-VTRYHSLVVDResLPDCLEVTAWTDDGEIMGVRHK 158

                        170       180
                 ....*....|....*....|....*.
4WIN_B       211 EYNIYGVQYHPEVYESLDGELMFYNF 236
Cdd:PRK05670 159 ELPIYGVQFHPESILTEHGHKLLENF 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
54-238 7.34e-12

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 64.74  E-value: 7.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        54 LKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFlEKKIPIFGICYGMQEIAVQMNGEVKKSKTSEYGCTdvnilrn 133
Cdd:PRK14607  37 IEEIEALNPSHIVISPGPGRPEEAG---ISVEVIRHF-SGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKT------- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       134 dninnitycrnfgdssSAMDLYSNyklmnetcCLFENIKSDIT-TVWMNHNDEVTKIPENFYLVSSSENCLICSIYNKEY 212
Cdd:PRK14607 106 ----------------SPIDHNGK--------GLFRGIPNPTVaTRYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKEH 161

                        170       180
                 ....*....|....*....|....*.
4WIN_B       213 NIYGVQYHPEVYESLDGELMFYNFAY 238
Cdd:PRK14607 162 PIFGVQFHPESILTEEGKRILKNFLN 187
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 21-222 4.70e-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: 4.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       21 ILVLNFGSQyfHLIVKRLN----NIKIFSETKDYgvelKDIKDMNIKGVILSGGPysvteaGSPHLKKEVFEY---FLEK 93
Cdd:cd01744   1 VVVIDFGVK--HNILRELLkrgcEVTVVPYNTDA----EEILKLDPDGIFLSNGP------GDPALLDEAIKTvrkLLGK 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       94 KIPIFGICYGMQEIAVQMNGEVKKSKtseYGctdvnilrndninnitycrNFGdsssamdlysnyklMNETCCLFENIKS 173
Cdd:cd01744  69 KIPIFGICLGHQLLALALGAKTYKMK---FG-------------------HRG--------------SNHPVKDLITGRV 112

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
4WIN_B      174 DITTvwMNHNDEVTK--IPENFYLVSSSEN-CLICSIYNKEYNIYGVQYHPE 222
Cdd:cd01744 113 YITS--QNHGYAVDPdsLPGGLEVTHVNLNdGTVEGIRHKDLPVFSVQFHPE 162
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
33-236 1.06e-10

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 59.05  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        33 LIVKRLNNIKIfsetkdygvelKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFlEKKIPIFGICYGMQEIAVQMN 112
Cdd:PRK07649  26 LVVKRNDEVTI-----------SDIENMKPDFLMISPGPCSPNEAG---ISMEVIRYF-AGKIPIFGVCLGHQSIAQVFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       113 GEVKKSKTSEYGCTDvnilrndninnitycrnfgdsssamdlysnyKLMNETCCLFENIKSDITTVwMNHNDEVTK--IP 190
Cdd:PRK07649  91 GEVVRAERLMHGKTS-------------------------------LMHHDGKTIFSDIPNPFTAT-RYHSLIVKKetLP 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
4WIN_B       191 ENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNF 236
Cdd:PRK07649 139 DCLEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQNF 184
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
20-222 2.97e-10

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 59.32  E-value: 2.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        20 KILVLNFGsqyfhliVKRlnNIkiFSETKDYGVEL---------KDIKDMNIKGVILSGGPysvteaGSPHLKKEVFE-- 88
Cdd:PRK12564 179 KVVAIDFG-------VKR--NI--LRELAERGCRVtvvpatttaEEILALNPDGVFLSNGP------GDPAALDYAIEmi 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        89 -YFLEKKIPIFGICYGMQEIAVQMNGEVKKSKtseygctdvnilrndninnitycrnFGDSSS---AMDLYSNyklmnet 164
Cdd:PRK12564 242 rELLEKKIPIFGICLGHQLLALALGAKTYKMK-------------------------FGHRGAnhpVKDLETG------- 289

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
4WIN_B       165 cclfeniKSDITTvwMNHN---DEVTkIPENFYLvssSENCL----ICSIYNKEYNIYGVQYHPE 222
Cdd:PRK12564 290 -------KVEITS--QNHGfavDEDS-LPANLEV---THVNLndgtVEGLRHKDLPAFSVQYHPE 341
trpG CHL00101
anthranilate synthase component 2
 52-236 1.72e-09

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 55.89  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        52 VELKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFLEKkIPIFGICYGMQEIAVQMNGEVKKSKTSEYGCTdvnil 131
Cdd:CHL00101  34 IDLSKIKNLNIRHIIISPGPGHPRDSG---ISLDVISSYAPY-IPILGVCLGHQSIGYLFGGKIIKAPKPMHGKT----- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       132 rndninNITYCRNFGdsssamdlysnyklmnetccLFENIKSDIT-TVWMNHNDEVTKIPENFYLVSSSENCLICSIYNK 210
Cdd:CHL00101 105 ------SKIYHNHDD--------------------LFQGLPNPFTaTRYHSLIIDPLNLPSPLEITAWTEDGLIMACRHK 158

                        170       180
                 ....*....|....*....|....*..
4WIN_B       211 EYN-IYGVQYHPEVYESLDGELMFYNF 236
Cdd:CHL00101 159 KYKmLRGIQFHPESLLTTHGQQILRNF 185
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 21-109 1.20e-08

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 51.83  E-value: 1.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       21 ILVLNFGSQY---FHLIVKRLN----NIKIFSETKDYGVELKDIKDmnIKGVILSGGPYSVTEAGSPHLKKEVFEYFLEK 93
Cdd:cd01653   1 VAVLLFPGFEeleLASPLDALReagaEVDVVSPDGGPVESDVDLDD--YDGLILPGGPGTPDDLARDEALLALLREAAAA 78

                        90
                ....*....|....*.
4WIN_B       94 KIPIFGICYGMQEIAV 109
Cdd:cd01653  79 GKPILGICLGAQLLVL 94
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 22-236 1.24e-08

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: 53.25  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B         22 LVLNFGSQYFHLIVKRLNNIkifsetkdygvELKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFlEKKIPIFGIC 101
Cdd:TIGR00566  15 LVQYFCELGAEVVVKRNDSL-----------TLQEIEALLPLLIVISPGPCTPNEAG---ISLEAIRHF-AGKLPILGVC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        102 YGMQEIAVQMNGEVKKSKTSEYGCTdvnilrndninnitycrnfgdsssamdlySNYKLMNET--CCLFENIKSditTVW 179
Cdd:TIGR00566  80 LGHQAMGQAFGGDVVRANTVMHGKT-----------------------------SEIEHNGAGifRGLFNPLTA---TRY 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
4WIN_B        180 MNHNDEVTKIPENFYLVS-SSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNF 236
Cdd:TIGR00566 128 HSLVVEPETLPTCFPVTAwEEENIEIMAIRHRDLPLEGVQFHPESILSEQGHQLLANF 185
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 21-105 5.87e-08

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: 49.12  E-value: 5.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       21 ILVLNFGSQY---FHLIVKRLN----NIKIFSETKDYGVELKDIKDmnIKGVILSGGPYSVTEAGSPHLKKEVFEYFLEK 93
Cdd:cd03128   1 VAVLLFGGSEeleLASPLDALReagaEVDVVSPDGGPVESDVDLDD--YDGLILPGGPGTPDDLAWDEALLALLREAAAA 78

                        90
                ....*....|..
4WIN_B       94 KIPIFGICYGMQ 105
Cdd:cd03128  79 GKPVLGICLGAQ 90
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 61-113 9.02e-08

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: 50.65  E-value: 9.02e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
4WIN_B       61 NIKGVILSGG-----------PYSVTEAGSPhlKKEVFE-----YFLEKKIPIFGICYGMQEIAVQMNG 113
Cdd:cd01745  53 LLDGLLLTGGgdvdpplygeePHPELGPIDP--ERDAFElallrAALERGKPILGICRGMQLLNVALGG 119
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 20-119 1.84e-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: 51.17  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       20 KILVLNFGsqyfhliVKRlnNIkiFSETKDYGVELK---------DIKDMNIKGVILSGGPysvteaGSP-HLKK--EVF 87
Cdd:COG0505 178 HVVALDFG-------VKR--NI--LRELAERGCRVTvvpattsaeEILALNPDGVFLSNGP------GDPaALDYaiETI 240

                        90       100       110
                ....*....|....*....|....*....|..
4WIN_B       88 EYFLEKKIPIFGICYGMQEIAVQMNGEVKKSK 119
Cdd:COG0505 241 RELLGKGIPIFGICLGHQLLALALGAKTYKLK 272
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
52-236 2.75e-07

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 49.49  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        52 VELKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFLEKkIPIFGICYGMQEIAVQMNGEVKKSKTSEYGCTDvnil 131
Cdd:PRK08857  34 IDIDGIEALNPTHLVISPGPCTPNEAG---ISLQAIEHFAGK-LPILGVCLGHQAIAQVFGGQVVRARQVMHGKTS---- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       132 rndninnitycrnfgdsssamdlysnyKLMNETCCLFENIKSDItTVWMNHNDEVTK--IPENFYLVSSSENC-----LI 204
Cdd:PRK08857 106 ---------------------------PIRHTGRSVFKGLNNPL-TVTRYHSLVVKNdtLPECFELTAWTELEdgsmdEI 157

                        170       180       190
                 ....*....|....*....|....*....|..
4WIN_B       205 CSIYNKEYNIYGVQYHPEVYESLDGELMFYNF 236
Cdd:PRK08857 158 MGFQHKTLPIEAVQFHPESIKTEQGHQLLANF 189
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 64-109 2.95e-07

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: 49.78  E-value: 2.95e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
4WIN_B       64 GVILSGGP------YSvtEAGSPHLKK----------EVFEYFLEKKIPIFGICYGMQEIAV 109
Cdd:COG2071  52 GLVLTGGAdvdpalYG--EEPHPELGPidperdafelALIRAALERGKPVLGICRGMQLLNV 111
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
52-236 3.99e-06

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 46.06  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        52 VELKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFlEKKIPIFGICYGMQEIAVQMNGEVKKS------KTSEYGC 125
Cdd:PRK08007  34 LTLADIDALKPQKIVISPGPCTPDEAG---ISLDVIRHY-AGRLPILGVCLGHQAMAQAFGGKVVRAakvmhgKTSPITH 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       126 TDVNILRNDNiNNITYCRnfgdsssamdlysnyklmnetcclFENIKSDITTvwmnhndevtkIPENFYLVSSSENCLIC 205
Cdd:PRK08007 110 NGEGVFRGLA-NPLTVTR------------------------YHSLVVEPDS-----------LPACFEVTAWSETREIM 153

                        170       180       190
                 ....*....|....*....|....*....|.
4WIN_B       206 SIYNKEYNIYGVQYHPEVYESLDGELMFYNF 236
Cdd:PRK08007 154 GIRHRQWDLEGVQFHPESILSEQGHQLLANF 184
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 20-119 4.07e-06

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 47.10  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        20 KILVLNFGSQYFhlIVKRLNN----IKIFSETKDYgvelKDIKDMNIKGVILSGGPysvteaGSP---HLKKEVFEYFLE 92
Cdd:CHL00197 194 KIIVIDFGVKYN--ILRRLKSfgcsITVVPATSPY----QDILSYQPDGILLSNGP------GDPsaiHYGIKTVKKLLK 261

                         90       100
                 ....*....|....*....|....*..
4WIN_B        93 KKIPIFGICYGMQEIAVQMNGEVKKSK 119
Cdd:CHL00197 262 YNIPIFGICMGHQILSLALEAKTFKLK 288
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 61-222 5.67e-06

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: 46.10  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B         61 NIKGVILSGGP------YSV--TEAGSPH------LKKEVFEYFLEKKIPIFGICYGMQEIAVQMNGevkksktSEYgcT 126
Cdd:pfam07722  58 RLDGLLLTGGPnvdphfYGEepSESGGPYdpardaYELALIRAALARGKPILGICRGFQLLNVALGG-------TLY--Q 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        127 DVNILrNDNINNITYCRNFGDSSS-AMDLysnyklmNETCCLFENIKSDITTVWMNHNDEVTKIPENFYLVSSSENCLI- 204
Cdd:pfam07722 129 DIQEQ-PGFTDHREHCQVAPYAPShAVNV-------EPGSLLASLLGSEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIe 200

                         170
                  ....*....|....*....
4WIN_B        205 -CSIYNKEYNIYGVQYHPE 222
Cdd:pfam07722 201 aIESPNAKGFALGVQWHPE 219
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 20-117 7.18e-06

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 46.42  E-value: 7.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        20 KILVLNFGsqYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPysvteaGSPhlkKEVFEYF-----LEKK 94
Cdd:PRK12838 169 HVALIDFG--YKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGP------GDP---KELQPYLpeikkLISS 237

                         90       100
                 ....*....|....*....|...
4WIN_B        95 IPIFGICYGMQEIAVQMNGEVKK 117
Cdd:PRK12838 238 YPILGICLGHQLIALALGADTEK 260
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
29-236 5.48e-05

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 42.93  E-value: 5.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        29 QYF-----HLIVKRLNNIkifsetkdygvELKDIKDMNIKGVILSGGPYSVTEAGsphLKKEVFEYFLEKkIPIFGICYG 103
Cdd:PRK06774  17 QYFcelgtEVMVKRNDEL-----------QLTDIEQLAPSHLVISPGPCTPNEAG---ISLAVIRHFADK-LPILGVCLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       104 MQEIAVQMNGEVKKSKTSEYGCTDVnilrndninnITYCRN--FGDSSSAMDLYSNYKLMNETCCL---FEniksdiTTV 178
Cdd:PRK06774  82 HQALGQAFGARVVRARQVMHGKTSA----------ICHSGQgvFRGLNQPLTVTRYHSLVIAADSLpgcFE------LTA 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
4WIN_B       179 WMNHNDEVTKipenfylvsssenclICSIYNKEYNIYGVQYHPEVYESLDGELMFYNF 236
Cdd:PRK06774 146 WSERGGEMDE---------------IMGIRHRTLPLEGVQFHPESILSEQGHQLLDNF 188
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
64-235 1.47e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 41.57  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        64 GVILSGGPYSVTEAGsphLKKEVFEYFLEKKIPIFGICYGMQEIAVQMNGEVKKS------KTSEYGCTDVNILRnDNIN 137
Cdd:PRK07765  49 GVLLSPGPGTPERAG---ASIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRApellhgKTSSVHHTGVGVLA-GLPD 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       138 NITYCRnfgdsssamdlYSNYKLMNETcclfeniksdittvwmnhndevtkIPENFYLVSSSENCLICSIYNKEYNIYGV 217
Cdd:PRK07765 125 PFTATR-----------YHSLTILPET------------------------LPAELEVTARTDSGVIMAVRHRELPIHGV 169

                        170
                 ....*....|....*...
4WIN_B       218 QYHPEVYESLDGELMFYN 235
Cdd:PRK07765 170 QFHPESVLTEGGHRMLAN 187
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 62-113 4.29e-04

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 40.65  E-value: 4.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
4WIN_B        62 IKGVILSGGPYSVteagSPHLKKE-----------------VFEYFLEKKIPIFGICYGMQEIAVQMNG 113
Cdd:PRK11366  62 LDGIYLPGSPSNV----QPHLYGEngdepdadpgrdllsmaLINAALERRIPIFAICRGLQELVVATGG 126
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 14-124 8.30e-04

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 39.96  E-value: 8.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        14 EGEEYdKILVLNFGSQyfHLIVKRLNN----IKIFSETKDYGVELKdikdMNIKGVILSGGPYSvtEAGSPHLKKEVFEy 89
Cdd:PLN02771 237 DGESY-HVIAYDFGIK--HNILRRLASygckITVVPSTWPASEALK----MKPDGVLFSNGPGD--PSAVPYAVETVKE- 306

                         90       100       110
                 ....*....|....*....|....*....|....*
4WIN_B        90 fLEKKIPIFGICYGMQEIAVQMNGEVKKSKTSEYG 124
Cdd:PLN02771 307 -LLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHG 340
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 64-232 9.43e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 39.54  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B        64 GVILSGGPYSVT---EAGSP---HLKKE---VFEYFLEKKIPIFGICYGMQEIAVQMNGEVKksktseygctdvnilrnd 134
Cdd:PRK07567  54 GVIVGGSPFNVSdpaESKSPwqrRVEAElsgLLDEVVARDFPFLGACYGVGTLGHHQGGVVD------------------ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       135 ninnitycRNFGDSSSAMdlysnyklmneTCCLFENIKSD-IT-------TVWMNHNDEVTKIPENFYLVSSSENCLICS 206
Cdd:PRK07567 116 --------RTYGEPVGAV-----------TVSLTDAGRADpLLaglpdtfTAFVGHKEAVSALPPGAVLLATSPTCPVQM 176

                        170       180
                 ....*....|....*....|....*.
4WIN_B       207 IYNKEyNIYGVQYHPEvyesLDGELM 232
Cdd:PRK07567 177 FRVGE-NVYATQFHPE----LDADGL 197
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 62-222 1.05e-03

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 39.61  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B       62 IKGVILSGGpySVTEAGSPHLK--KEVFEYFLEKKI-----PIFGICYGMQEIAVQMNGEVkksktseygctdvNILRND 134
Cdd:cd01747  55 INGILFPGG--AVDIDTSGYARtaKIIYNLALERNDagdyfPVWGTCLGFELLTYLTSGET-------------LLLEAT 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4WIN_B      135 NINNItycrnfgdsSSAMDLYSNYKlmneTCCLFENIKSDITT-------VWMNH-------NDEVTKIPENFYLVSS-- 198
Cdd:cd01747 120 EATNS---------ALPLNFTEDAL----QSRLFKRFPPDLLKslateplTMNNHrygispeNFTENGLLSDFFNVLTtn 186

                       170       180
                ....*....|....*....|....*..
4WIN_B      199 ---SENCLICSIYNKEYNIYGVQYHPE 222
Cdd:cd01747 187 ddwNGVEFISTVEAYKYPIYGVQWHPE 213
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 89-109 2.11e-03

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


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 38.84  E-value: 2.11e-03
                        10        20
                ....*....|....*....|.
4WIN_B       89 YFLEKKIPIFGICYGMQeIAV 109
Cdd:COG0504 368 YARENKIPFLGICLGMQ-LAV 387
PRK05665 PRK05665
amidotransferase; Provisional
 177-232 3.00e-03

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 37.87  E-value: 3.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
4WIN_B       177 TVWMNHNDEVTKIPENFYLVSSSENCLICSiYNKEYNIYGVQYHPEVYESLDGELM 232
Cdd:PRK05665 143 TLLISHQDQVTALPEGATVIASSDFCPFAA-YHIGDQVLCFQGHPEFVHDYSRALL 197
pyrG PRK05380
CTP synthetase; Validated
 89-109 5.46e-03

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 37.69  E-value: 5.46e-03
                         10        20
                 ....*....|....*....|.
4WIN_B        89 YFLEKKIPIFGICYGMQeIAV 109
Cdd:PRK05380 367 YARENNIPFLGICLGMQ-LAV 386
 
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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