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Conserved domains on  [gi|612672724|gb|EZS88794|]
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phosphoribosylformylglycinamidine synthase 1 [Staphylococcus aureus VET0159R]

Protein Classification

phosphoribosylformylglycinamidine synthase subunit PurQ( domain architecture ID 10012055)

phosphoribosylformylglycinamidine synthase subunit PurQ is part of the complex that catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate; subunit PurQ produces an ammonia molecule by converting glutamine to glutamate

CATH:  3.40.50.880
EC:  6.3.5.3|3.5.1.2
Gene Ontology:  GO:0005524|GO:0004642
PubMed:  10387030
SCOP:  3001405

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-217 4.98e-143

phosphoribosylformylglycinamidine synthase subunit PurQ;


:

Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 397.95  E-value: 4.98e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   1 MKFAVLVFPGSNCDRDMFNAA-IKSGVEAEYVDYRETSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEGK 79
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALrDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  80 PVLGVCNGFQILTEIGLLPGALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQLKAN 159
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612672724 160 NQIILKYA-NNPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDSGVKLFEAMVKS 217
Cdd:PRK03619 161 GQVVFRYCdENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-217 4.98e-143

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 397.95  E-value: 4.98e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   1 MKFAVLVFPGSNCDRDMFNAA-IKSGVEAEYVDYRETSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEGK 79
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALrDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  80 PVLGVCNGFQILTEIGLLPGALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQLKAN 159
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612672724 160 NQIILKYA-NNPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDSGVKLFEAMVKS 217
Cdd:PRK03619 161 GQVVFRYCdENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-218 5.98e-137

phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273782 [Multi-domain]  Cd Length: 227  Bit Score: 382.88  E-value: 5.98e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724    1 MKFAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRETSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEGKP 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   81 VLGVCNGFQILTEIGLLPGALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQLKANN 160
Cdd:TIGR01737  81 VLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESND 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672724  161 QIILKY---------ANNPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDSGVKLFEAMVKSW 218
Cdd:TIGR01737 161 QVVFRYcdedgdvaeEANPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVEWL 227
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-219 4.21e-117

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


Pssm-ID: 439817 [Multi-domain]  Cd Length: 236  Bit Score: 333.18  E-value: 4.21e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   1 MKFAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRE--TSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEG 78
Cdd:COG0047    1 PKVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDlrTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  79 KPVLGVCNGFQILTEIGLLPG---ALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQ 155
Cdd:COG0047   81 GLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLAE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672724 156 LKANNQIILKYAN---------NPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDS---GVKLFEAMVKSWR 219
Cdd:COG0047  161 LEANGQVAFRYVDadgnvtypaNPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGPGEstdGLRIFRSAVKYFG 236
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-215 2.87e-96

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 280.27  E-value: 2.87e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   3 FAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRET-----SLSGFDGVLIPGGFSFGDYLRSGAMASVAP-IISEVKRLAA 76
Cdd:cd01740    1 VAVLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLlagrkDLDDYDGVVLPGGFSYGDYLRAGAIAAASPlLMEEVKEFAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  77 EGKPVLGVCNGFQILTEIGLLPGALLHNDSHLFISRNE----ELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEI 152
Cdd:cd01740   81 RGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQnrfvTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDET 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672724 153 YQQLKANNQII----------LKYANNPNGSYDDIAGIVNEKGNVCGMMPHPERALET-----LLGTDSGVKLFEAMV 215
Cdd:cd01740  161 LAELEENGQIAqyvdddgnvtERYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPwqwerLLGGSDGLKLFRNAV 238
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 2-216 2.74e-54

CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not found in pfam00310, pfam07685 and pfam13230.


Pssm-ID: 463904 [Multi-domain]  Cd Length: 260  Bit Score: 174.22  E-value: 2.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724    2 KFAVLVFPGSNCDRDMFNAAIKSGVEAEYV-----DYRETSLSGFDGVLIPGGFSFGDYLRSG-AMASV----APIISEV 71
Cdd:pfam13507   3 RVAILREPGTNGEYEMAAAFERAGFDAVDVhmsdlLSGRVSLDDFQGLAAPGGFSYGDVLGSGkGWAASilfnPKLRDAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   72 KR-LAAEGKPVLGVCNGFQILTEIGLLPG----------ALLHNDSHLFISRNEELEIVNNQTAFTNlyeQGEKVIY-PV 139
Cdd:pfam13507  83 EAfFNRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRWVNVKISEKSPSVFL---RGMDGSGlPV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  140 AHGEGH-YYCTDEIYQQLKANNQIILKYAN-----------NPNGSYDDIAGIVNEKGNVCGMMPHPERALETL------ 201
Cdd:pfam13507 160 AHGEGRfVFRSEEVLARLEANGQVALRYVDnagnpteeypfNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWqwphwp 239

                         250
                  ....*....|....*....
gi 612672724  202 ---LGTDS-GVKLFEAMVK 216
Cdd:pfam13507 240 pgeWEEVSpWLRLFRNARK 258
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-217 4.98e-143

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 397.95  E-value: 4.98e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   1 MKFAVLVFPGSNCDRDMFNAA-IKSGVEAEYVDYRETSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEGK 79
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALrDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  80 PVLGVCNGFQILTEIGLLPGALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQLKAN 159
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612672724 160 NQIILKYA-NNPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDSGVKLFEAMVKS 217
Cdd:PRK03619 161 GQVVFRYCdENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-218 5.98e-137

phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273782 [Multi-domain]  Cd Length: 227  Bit Score: 382.88  E-value: 5.98e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724    1 MKFAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRETSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEGKP 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   81 VLGVCNGFQILTEIGLLPGALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQLKANN 160
Cdd:TIGR01737  81 VLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESND 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672724  161 QIILKY---------ANNPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDSGVKLFEAMVKSW 218
Cdd:TIGR01737 161 QVVFRYcdedgdvaeEANPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVEWL 227
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-219 4.21e-117

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


Pssm-ID: 439817 [Multi-domain]  Cd Length: 236  Bit Score: 333.18  E-value: 4.21e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   1 MKFAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRE--TSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEG 78
Cdd:COG0047    1 PKVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDlrTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  79 KPVLGVCNGFQILTEIGLLPG---ALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQ 155
Cdd:COG0047   81 GLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLAE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672724 156 LKANNQIILKYAN---------NPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDS---GVKLFEAMVKSWR 219
Cdd:COG0047  161 LEANGQVAFRYVDadgnvtypaNPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGPGEstdGLRIFRSAVKYFG 236
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-215 2.87e-96

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 280.27  E-value: 2.87e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   3 FAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRET-----SLSGFDGVLIPGGFSFGDYLRSGAMASVAP-IISEVKRLAA 76
Cdd:cd01740    1 VAVLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLlagrkDLDDYDGVVLPGGFSYGDYLRAGAIAAASPlLMEEVKEFAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  77 EGKPVLGVCNGFQILTEIGLLPGALLHNDSHLFISRNE----ELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEI 152
Cdd:cd01740   81 RGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQnrfvTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDET 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672724 153 YQQLKANNQII----------LKYANNPNGSYDDIAGIVNEKGNVCGMMPHPERALET-----LLGTDSGVKLFEAMV 215
Cdd:cd01740  161 LAELEENGQIAqyvdddgnvtERYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPwqwerLLGGSDGLKLFRNAV 238
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 1-197 4.90e-62

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 194.21  E-value: 4.90e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   1 MKFAVLVFPGSNCDRDMFNAAIKSGVEAEYV-----DYRETSLSGFDGVLIPGGFSFGDYLRSGAM--ASVAPII-SEVK 72
Cdd:PRK01175   4 IRVAVLRMEGTNCEDETVKAFRRLGVEPEYVhindlAAERKSVSDYDCLVIPGGFSAGDYIRAGAIfaARLKAVLrKDIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  73 RLAAEGKPVLGVCNGFQILTEIGLLPG----------ALLHNDSHLFISRNEELEIVNNQTAFTNLYeQGEKVIYPVAHG 142
Cdd:PRK01175  84 EFIDEGYPIIGICNGFQVLVELGLLPGfdeiaekpemALTVNESNRFECRPTYLKKENRKCIFTKLL-KKDVFQVPVAHA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672724 143 EGH-YYCTDEIYQQLKANNQIILKYAN----------NPNGSYDDIAGIVNEKGNVCGMMPHPERA 197
Cdd:PRK01175 163 EGRvVFSEEEILERLIENDQIVFRYVDengnyagypwNPNGSIYNIAGITNEKGNVIGLMPHPERA 228
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 2-216 2.74e-54

CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not found in pfam00310, pfam07685 and pfam13230.


Pssm-ID: 463904 [Multi-domain]  Cd Length: 260  Bit Score: 174.22  E-value: 2.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724    2 KFAVLVFPGSNCDRDMFNAAIKSGVEAEYV-----DYRETSLSGFDGVLIPGGFSFGDYLRSG-AMASV----APIISEV 71
Cdd:pfam13507   3 RVAILREPGTNGEYEMAAAFERAGFDAVDVhmsdlLSGRVSLDDFQGLAAPGGFSYGDVLGSGkGWAASilfnPKLRDAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   72 KR-LAAEGKPVLGVCNGFQILTEIGLLPG----------ALLHNDSHLFISRNEELEIVNNQTAFTNlyeQGEKVIY-PV 139
Cdd:pfam13507  83 EAfFNRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRWVNVKISEKSPSVFL---RGMDGSGlPV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  140 AHGEGH-YYCTDEIYQQLKANNQIILKYAN-----------NPNGSYDDIAGIVNEKGNVCGMMPHPERALETL------ 201
Cdd:pfam13507 160 AHGEGRfVFRSEEVLARLEANGQVALRYVDnagnpteeypfNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWqwphwp 239

                         250
                  ....*....|....*....
gi 612672724  202 ---LGTDS-GVKLFEAMVK 216
Cdd:pfam13507 240 pgeWEEVSpWLRLFRNARK 258
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
 2-197 7.74e-26

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 104.85  E-value: 7.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724    2 KFAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRE-----TSLSGFDGVLIPGGFSFGDYLRS--GAMASV---APIISEV 71
Cdd:PLN03206 1039 KVAIIREEGSNGDREMAAAFYAAGFEPWDVTMSDllngrISLDDFRGIVFVGGFSYADVLDSakGWAGSIrfnEPLLQQF 1118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   72 KRL-AAEGKPVLGVCNGFQILTEIGLLPGA----------------LLHNDSHLFISRNEELEIVNNQTAFTNLYEqGEK 134
Cdd:PLN03206 1119 QEFyNRPDTFSLGVCNGCQLMALLGWVPGPqvggglgaggdpsqprFVHNESGRFECRFTSVTIEDSPAIMLKGME-GST 1197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672724  135 VIYPVAHGEGHYYCTDE-IYQQLKANNQIILKYAN-----------NPNGSYDDIAGIVNEKGNVCGMMPHPERA 197
Cdd:PLN03206 1198 LGVWAAHGEGRAYFPDEsVLDEVLKSNLAPVRYCDddgepteqypfNPNGSPLGIAALCSPDGRHLAMMPHPERC 1272
PRK05297 PRK05297
phosphoribosylformylglycinamidine synthase; Provisional
 2-196 2.86e-25

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 235394 [Multi-domain]  Cd Length: 1290  Bit Score: 103.34  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724    2 KFAVLVFPGSNCDRDMFNAAIKSGVEAeyVDY--------RETsLSGFDGVLIPGGFSFGDYLrsGAMASVAPIISEVKR 73
Cdd:PRK05297 1037 KVAILREQGVNSHVEMAAAFDRAGFDA--IDVhmsdllagRVT-LEDFKGLVACGGFSYGDVL--GAGEGWAKSILFNPR 1111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   74 LAAE-----GKP---VLGVCNGFQILTEIGLL-PGA-----LLHNDSHLFISRNEELEIVNNQTAFTNLYEqGEKVIYPV 139
Cdd:PRK05297 1112 LRDQfeaffARPdtfALGVCNGCQMMSNLKEIiPGAehwprFVRNRSEQFEARFSLVEVQESPSIFLQGMA-GSRLPIAV 1190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672724  140 AHGEGHYYCTDEIYQQLKANNQIILKYAN-----------NPNGSYDDIAGIVNEKGNVCGMMPHPER 196
Cdd:PRK05297 1191 AHGEGRAEFPDAHLAALEAKGLVALRYVDnhgqvtetypaNPNGSPNGITGLTTADGRVTIMMPHPER 1258
FGAM_synt TIGR01735
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ...
 2-197 3.75e-25

phosphoribosylformylglycinamidine synthase, single chain form; This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This form is found mostly in eukaryotes and Proteobacteria. In Bacillus subtilis PurL (FGAM synthase II) and PurQ (FGAM synthase I), homologous to different parts of this model, perform the equivalent function; the unrelated small protein PurS is also required and may be a third subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 188163 [Multi-domain]  Cd Length: 1310  Bit Score: 102.94  E-value: 3.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724     2 KFAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRE-----TSLSGFDGVLIPGGFSFGDYLRSGA--MASV---APIISEV 71
Cdd:TIGR01735 1057 KVAILREQGVNGDREMAAAFDRAGFEAWDVHMSDllagrVHLDEFRGLAACGGFSYGDVLGAGKgwAKSIlfnPRLRDQF 1136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724    72 KRLAAegKP---VLGVCNGFQILTEI-GLLPG-----ALLHNDSHLFISRNEELEIVNNQTAFTNLYEqGEKVIYPVAHG 142
Cdd:TIGR01735 1137 QAFFK--RPdtfSLGVCNGCQMLSNLlEWIPGtenwpHFVRNNSERFEARVASVRVGESPSIMLRGMA-GSRLPVAVAHG 1213

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672724   143 EGH-YYCTDEIYQQLKANNQIILKYAN-----------NPNGSYDDIAGIVNEKGNVCGMMPHPERA 197
Cdd:TIGR01735 1214 EGYaAFSSPELQAQADASGLAALRYIDddgnpteayplNPNGSPGGIAGITSCDGRVTIMMPHPERV 1280
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-91 1.37e-13

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: 64.93  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   4 AVLVFPGSNCD--RDMFNAAIKSGVEAEYVDYRE------TSLSGFDGVLIPGGFSFGDylrsgAMASVAPIISEVKRLA 75
Cdd:cd01653    2 AVLLFPGFEELelASPLDALREAGAEVDVVSPDGgpvesdVDLDDYDGLILPGGPGTPD-----DLARDEALLALLREAA 76

                         90
                 ....*....|....*.
gi 612672724  76 AEGKPVLGVCNGFQIL 91
Cdd:cd01653   77 AAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-91 1.28e-12

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: 61.45  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   4 AVLVFPGSNCD--RDMFNAAIKSGVEAEYVDYRE------TSLSGFDGVLIPGGFSFGDylrsgAMASVAPIISEVKRLA 75
Cdd:cd03128    2 AVLLFGGSEELelASPLDALREAGAEVDVVSPDGgpvesdVDLDDYDGLILPGGPGTPD-----DLAWDEALLALLREAA 76

                         90
                 ....*....|....*.
gi 612672724  76 AEGKPVLGVCNGFQIL 91
Cdd:cd03128   77 AAGKPVLGICLGAQLL 92
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 38-196 8.94e-10

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 56.29  E-value: 8.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  38 LSGFDGVLIPGGFSFGDylrsgAMASV--APIISEVKRLAAEGKPVLGVCNGFQILTE----------IGLLPGALLHnd 105
Cdd:PRK13141  35 ILAADGVILPGVGAFPD-----AMANLreRGLDEVIKEAVASGKPLLGICLGMQLLFEsseefgetegLGLLPGRVRR-- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724 106 shlFISRNEE---------LEIVNNQTAFTNLyEQGEKViYPVaHGeghYYCTDEiyqqlkaNNQIILKYANnpngsYD- 175
Cdd:PRK13141 108 ---FPPEEGLkvphmgwnqLELKKESPLLKGI-PDGAYV-YFV-HS---YYADPC-------DEEYVAATTD-----YGv 166

                        170       180
                 ....*....|....*....|.
gi 612672724 176 DIAGIVnEKGNVCGMMPHPER 196
Cdd:PRK13141 167 EFPAAV-GKDNVFGAQFHPEK 186
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 21-91 8.13e-09

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 53.40  E-value: 8.13e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672724  21 AIKSGVEAEYVDYREtSLSGFDGVLIPGGFS-FGD--YLRSGAMASvapiisEVKRLAAEGKPVLGVCNGFQIL 91
Cdd:cd01750   19 AREPGVDVRYVEVPE-GLGDADLIILPGSKDtIQDlaWLRKRGLAE------AIKNYARAGGPVLGICGGYQML 85
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 19-196 2.24e-08

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: 52.11  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  19 NAAIKSGVEAEYVDyRETSLSGFDGVLIPGGFSFGDylrsgAMASVA--PIISEVKRLAAEGKPVLGVCNGFQILTE--- 93
Cdd:cd01748   16 NALERLGAEVIITS-DPEEILSADKLILPGVGAFGD-----AMANLRerGLIEALKEAIASGKPFLGICLGMQLLFEsse 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  94 -------IGLLPGALLH-NDSHLF----ISRNeELEIVNNQTAFTNLyEQGEKViYPVahgegH-YY--CTDEIYqqlka 158
Cdd:cd01748   90 egggtkgLGLIPGKVVRfPASEGLkvphMGWN-QLEITKESPLFKGI-PDGSYF-YFV-----HsYYapPDDPDY----- 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 612672724 159 nnqiILKYANnpngsYD-DIAGIVnEKGNVCGMMPHPER 196
Cdd:cd01748  157 ----ILATTD-----YGgKFPAAV-EKDNIFGTQFHPEK 185
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 35-99 5.68e-07

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 47.79  E-value: 5.68e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672724  35 ETSLSGFDGVLIPGGFSFGDYLRSGAmasvaPIISEVKRLAAEGKPVLGVCNGFQILTEIGLLPG 99
Cdd:COG0693   59 DVDPDDYDALVLPGGHGAPDDLREDP-----DVVALVREFYEAGKPVAAICHGPAVLAAAGLLKG 118
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 35-99 7.83e-07

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: 47.25  E-value: 7.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612672724   35 ETSLSGFDGVLIPGGFSFGDYLRSGAMAsvapiISEVKRLAAEGKPVLGVCNGFQILTEIGLLPG 99
Cdd:pfam01965  56 DVKPDDYDALVLPGGRAGPERLRDNEKL-----VEFVKDFYEKGKPVAAICHGPQVLAAAGVLKG 115
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 2-93 1.07e-06

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 47.24  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   2 KFAVLV---FPGSNCDRDMFNAAIKSGVEAEYVDYRE----TSLSGFDGVLIPGGfsfgdylRSGAMASVAPIISEVKRL 74
Cdd:cd01741    1 RILILQhdtPEGPGLFEDLLREAGAETIEIDVVDVYAgellPDLDDYDGLVILGG-------PMSVDEDDYPWLKKLKEL 73

                         90       100
                 ....*....|....*....|...
gi 612672724  75 ----AAEGKPVLGVCNGFQILTE 93
Cdd:cd01741   74 irqaLAAGKPVLGICLGHQLLAR 96
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 4-91 1.30e-06

Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441101 [Multi-domain]  Cd Length: 493  Bit Score: 48.13  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   4 AVLVFPG-SNCDrDmFNA-AIKSGVEAEYVDyRETSLSGFDGVLIPGgfS---FGD--YLRSGAMASvapiisEVKRLAA 76
Cdd:COG1492  255 AVIRLPRiSNFT-D-FDPlAAEPGVRLRYVR-PPEELGDADLVILPG--SkntIADlaWLRESGLDD------AIRAHAR 323

                         90
                 ....*....|....*
gi 612672724  77 EGKPVLGVCNGFQIL 91
Cdd:COG1492  324 RGGPVLGICGGYQML 338
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 41-99 1.70e-06

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 46.38  E-value: 1.70e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612672724  41 FDGVLIPGGFSfGDYLRSGAMAsvapiISEVKRLAAEGKPVLGVCNGFQILTEIGLLPG 99
Cdd:cd03134   63 YDALVIPGGTN-PDKLRRDPDA-----VAFVRAFAEAGKPVAAICHGPWVLISAGVVRG 115
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 31-99 6.23e-06

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 44.95  E-value: 6.23e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672724  31 VDYRETSLSGFDGVLIPGGfSFGDYLRSGAMAsvapiISEVKRLAAEGKPVLGVCNGFQILTEIGLLPG 99
Cdd:cd03169   67 ADFDEVDPDDYDALVIPGG-RAPEYLRLDEKV-----LAIVRHFAEANKPVAAICHGPQILAAAGVLKG 129
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 42-99 9.17e-06

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: 44.64  E-value: 9.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672724  42 DGVLIPG-GfSFGDylrsgAMASV--APIISEVKRLAAEGKPVLGVCNGFQILTE----------IGLLPG 99
Cdd:COG0118   40 DRLVLPGvG-AFGD-----AMENLreRGLDEAIREAVAGGKPVLGICLGMQLLFErseengdtegLGLIPG 104
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
4-98 1.45e-05

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 44.15  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724    4 AVLVFPG-SNCDRDMFNA-AIKSGVEAEYVDYRETSL-SGFDGVLIPGGFSFGD---YLRSGAMASvapiisEVKRLAAE 77
Cdd:pfam07685   3 AVIRLPRiSNYTDDNLDPlRYEPAVRVRFVPLPDESLgPDADLIILPGGKPTIQdlaLLRNSGMDE------AIKEAAED 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 612672724   78 GKPVLGVCNGFQILTE------------IGLLP 98
Cdd:pfam07685  77 GGPVLGICGGYQMLGEtiedpegvriegLGLLD 109
PRK13896 PRK13896
cobyrinic acid a,c-diamide synthase; Provisional
 42-93 1.71e-05

cobyrinic acid a,c-diamide synthase; Provisional


Pssm-ID: 184379 [Multi-domain]  Cd Length: 433  Bit Score: 44.75  E-value: 1.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 612672724  42 DGVLIPGGFSfgdYLRSGAMASvAPIISEVKRLAAEGKPVLGVCNGFQILTE 93
Cdd:PRK13896 276 DGVYLPGGYP---ELHADALAD-SPALDELADRAADGLPVLGECGGLMALAE 323
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 32-91 2.96e-05

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: 42.87  E-value: 2.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  32 DYRETSLSGFDGVLIPGGfsfgdylrSGAMASVAPIISEVKRLAAEGKPVLGVCNGFQIL 91
Cdd:cd01744   31 DAEEILKLDPDGIFLSNG--------PGDPALLDEAIKTVRKLLGKKIPIFGICLGHQLL 82
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 25-91 3.33e-05

Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only];


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 43.63  E-value: 3.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  25 GVEAEYVDYR---ETSLSGFDGVLIPGGfsfGDYLRSGAMASVAPIISEVKRLAAEGKPVLGVCNGFQIL 91
Cdd:COG3442   32 GIDVEVVEVNpgdDLPFDDVDIVFIGGG---QDREQEIVADDLLRIKDALRAAIEDGVPVLAICGGYQLL 98
PRK00784 PRK00784
cobyric acid synthase;
4-91 3.46e-05

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 43.92  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   4 AVLVFPG-SNCDrDmFNA-AIKSGVEAEYVDyRETSLSGFDGVLIPGgfS---FGD--YLRSGAMASvapiisEVKRLAA 76
Cdd:PRK00784 255 AVIRLPRiSNFT-D-FDPlRAEPGVDVRYVR-PGEPLPDADLVILPG--SkntIADlaWLRESGWDE------AIRAHAR 323

                         90
                 ....*....|....*
gi 612672724  77 EGKPVLGVCNGFQIL 91
Cdd:PRK00784 324 RGGPVLGICGGYQML 338
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 42-99 7.09e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 42.16  E-value: 7.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612672724  42 DGVLIPGGFSFGDylrsgAMASVAPIISEVKRLAAEGKPVLGVCNGFQILTE----------IGLLPG 99
Cdd:PRK13143  40 DGIVLPGVGAFGA-----AMENLSPLRDVILEAARSGKPFLGICLGMQLLFEsseegggvrgLGLFPG 102
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 1-93 7.49e-05

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 42.39  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   1 MKFAVLVFPGSncdrdmFN---AAIKS-GVEAeyVDYRETS-LSGFDGVLIPGGfsfgdylRSGAMASVAP---IISEVK 72
Cdd:PLN02832   2 MAIGVLALQGS------FNehiAALRRlGVEA--VEVRKPEqLEGVSGLIIPGG-------ESTTMAKLAErhnLFPALR 66

                         90       100
                 ....*....|....*....|.
gi 612672724  73 RLAAEGKPVLGVCNGFQILTE 93
Cdd:PLN02832  67 EFVKSGKPVWGTCAGLIFLAE 87
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 41-99 1.03e-04

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 41.25  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 612672724   41 FDGVLIPGGFSfGDYLRSGAMAsvapiISEVKRLAAEGKPVLGVCNGFQILTEIGLLPG 99
Cdd:TIGR01382  61 YDALVIPGGRA-PEYLRLNNKA-----VRLVREFVEKGKPVAAICHGPQLLISAGVLRG 113
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 19-99 1.14e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 41.77  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  19 NAAIKSGVEAEYVDYRETsLSGFDGVLIPGGFSFGD---YLRSGAMASVapiiseVKRLAAEGKPVLGVCNGFQILTE-- 93
Cdd:PRK13181  17 NALKRLGVEAVVSSDPEE-IAGADKVILPGVGAFGQamrSLRESGLDEA------LKEHVEKKQPVLGICLGMQLLFEss 89

                         90
                 ....*....|...
gi 612672724  94 -------IGLLPG 99
Cdd:PRK13181  90 eegnvkgLGLIPG 102
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 20-90 4.53e-04

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 40.23  E-value: 4.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  20 AAIKSG--VEAEYVD-------YRETSLSGFDGVLIPGGFSFGDYlrSGAMASVapiisevkRLAAE-GKPVLGVCNGFQ 89
Cdd:cd01746   26 AGIALGvkLEIKWIDsedleeeNAEEALKGADGILVPGGFGIRGV--EGKILAI--------KYAREnNIPFLGICLGMQ 95


                 .
gi 612672724  90 I 90
Cdd:cd01746   96 L 96
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 16-87 4.66e-04

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 39.87  E-value: 4.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612672724  16 DMFNAAIKS-GVEAEYVDYRETS-LSGFDGVLIPGGFSfgdyLRSGAMASVAPIISEVKRLAAEGKPVLGVCNG 87
Cdd:PRK13527  17 DALKRALDElGIDGEVVEVRRPGdLPDCDALIIPGGES----TTIGRLMKREGILDEIKEKIEEGLPILGTCAG 86
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 42-99 5.01e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 39.77  E-value: 5.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612672724  42 DGVLIPGGFSFGDYLRS-GAMASVAPIISEVkrlAAEGKPVLGVCNGFQILTE----------IGLLPG 99
Cdd:PRK13146  43 DRVVLPGVGAFADCMRGlRAVGLGEAVIEAV---LAAGRPFLGICVGMQLLFErglehgdtpgLGLIPG 108
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
32-85 5.85e-04

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 39.77  E-value: 5.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612672724  32 DYRETSLSGFDGVLIPGGF----SFGDYLRSGAMASVAPiisEVKRL----AAEGKPVLGVC 85
Cdd:PRK11780  77 DLAEADAEDFDALIVPGGFgaakNLSNFAVKGAECTVNP---DVKALvrafHQAGKPIGFIC 135
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 38-91 6.42e-04

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: 39.48  E-value: 6.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612672724  38 LSGFDGVLIPGGFSFGDYLRSG-AMASVAPIISE--------VKRLAAEGKPVLGVCNGFQIL 91
Cdd:cd01745   51 LELLDGLLLTGGGDVDPPLYGEePHPELGPIDPErdafelalLRAALERGKPILGICRGMQLL 113
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 25-87 6.91e-04

Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (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. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 39.05  E-value: 6.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612672724  25 GVEAEYVDYRETsLSGFDGVLIPGGfsfgdylRSGAMASVA---PIISEVKRLAAEGKPVLGVCNG 87
Cdd:cd01749   21 GVEVIEVRTPED-LEGIDGLIIPGG-------ESTTIGKLLrrtGLLDPLREFIRAGKPVFGTCAG 78
GATase pfam00117
Glutamine amidotransferase class-I;
41-93 1.39e-03

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 38.37  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 612672724   41 FDGVLIPGGFsfGDYLRSGAMasvapiISEVKRLAAEGKPVLGVCNGFQILTE 93
Cdd:pfam00117  41 PDGIILSGGP--GSPGAAGGA------IEAIREARELKIPILGICLGHQLLAL 85
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 38-212 1.56e-03

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: 38.07  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724   38 LSGFDGVLIPGGFSFGDylrsgAMASVAPIISEVKR--LAAEGKPVLGVCNGFQILTE----------IGLLPGAllhnd 105
Cdd:TIGR01855  34 AELADKLILPGVGAFGA-----AMARLRENGLDLFVelVVRLGKPVLGICLGMQLLFErseegggvpgLGLIKGN----- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  106 shlfISRNEELEIvnNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQLKANNqiILKYANnpngsY-DDIAGIVnEK 184
Cdd:TIGR01855 104 ----VVKLEARKV--PHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEEA--VLAYAD-----YgEKFPAAV-QK 169

                         170       180
                  ....*....|....*....|....*...
gi 612672724  185 GNVCGMMPHPERALETllgtdsGVKLFE 212
Cdd:TIGR01855 170 GNIFGTQFHPEKSGKT------GLKLLE 191
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
42-99 5.45e-03

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 37.42  E-value: 5.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612672724  42 DGVLIPGGFSfgdYLRSGAMASVAPIISEVKRLAAEGKPVLGVCNGFQILTE------------IGLLPG 99
Cdd:PRK01077 289 DGLYLGGGYP---ELFAAELAANTSMRASIRAAAAAGKPIYAECGGLMYLGEsledadgerhpmVGLLPG 355
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
23-87 5.85e-03

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 36.29  E-value: 5.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612672724  23 KSGVEAEYVDYREtSLSGFDGVLIPGGFS--FGDYLRSGAMASvapiisEVKRLAAEGKPVLGVCNG 87
Cdd:PRK13525  22 ALGAEAVEVRRPE-DLDEIDGLILPGGESttMGKLLRDFGLLE------PLREFIASGLPVFGTCAG 81
PLN02327 PLN02327
CTP synthase
 38-90 6.14e-03

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 37.31  E-value: 6.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612672724  38 LSGFDGVLIPGGfsFGDYLRSGamasvapiisevKRLAAE-----GKPVLGVCNGFQI 90
Cdd:PLN02327 360 LKGADGILVPGG--FGDRGVEG------------KILAAKyarenKVPYLGICLGMQI 403
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 41-99 6.46e-03

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153232 [Multi-domain]  Cd Length: 195  Bit Score: 36.47  E-value: 6.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612672724  41 FDGVLIPGgfsFGDYLRSGAMASVAPIISEVKRLAAEGKPVLGVCNGFQILTEIGLLPG 99
Cdd:cd03138   70 PDLVIVPG---LGGDPDELLLADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDG 125
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 31-91 9.48e-03

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: 36.08  E-value: 9.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612672724   31 VDYRETSLSGFDGVLIPGGFSFgDYLRSGAMASVA--PIISE--------VKRLAAEGKPVLGVCNGFQIL 91
Cdd:pfam07722  49 PEDAAAILDRLDGLLLTGGPNV-DPHFYGEEPSESggPYDPArdayelalIRAALARGKPILGICRGFQLL 118
 
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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