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Conserved domains on  [gi|502275031|ref|WP_012749004|]
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MULTISPECIES: phosphoribosylformylglycinamidine synthase subunit PurQ [Bacillaceae]

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

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List of domain hits

 Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-219 1.59e-172

phosphoribosylformylglycinamidine synthase subunit PurQ;


:

Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 472.68  E-value: 1.59e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   1 MKFAVIVFPGSNCDVDMYHAIADELGEEVEYVWHDAENLDRFDAILLPGGFSYGDYLRSGAIARFSNVMKAVKKAADEGK 80
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  81 PVLGVCNGFQILLEAGLLPGAMRRNNSLKFICRPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQTLKRLIEN 160
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502275031 161 RQIVFRYHGENPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSLLGSADGLKLFQSIVKY 219
Cdd:PRK03619 161 GQVVFRYCDENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-219 1.59e-172

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 472.68  E-value: 1.59e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   1 MKFAVIVFPGSNCDVDMYHAIADELGEEVEYVWHDAENLDRFDAILLPGGFSYGDYLRSGAIARFSNVMKAVKKAADEGK 80
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  81 PVLGVCNGFQILLEAGLLPGAMRRNNSLKFICRPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQTLKRLIEN 160
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502275031 161 RQIVFRYHGENPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSLLGSADGLKLFQSIVKY 219
Cdd:PRK03619 161 GQVVFRYCDENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-221 1.57e-143

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: 400.20  E-value: 1.57e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   1 MKFAVIVFPGSNCDVDMYHAIaDELGEEVEYVWHD--AENLDRFDAILLPGGFSYGDYLRSGAIARFSNVMKAVKKAADE 78
Cdd:COG0047    1 PKVAILVFPGSNCDRDMAAAF-ERAGAEAEDVWHSdlRTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  79 GKPVLGVCNGFQILLEAGLLPG---AMRRNNSLKFICRPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQTLK 155
Cdd:COG0047   80 GGLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502275031 156 RLIENRQIVFRYHGE--------NPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSLLG---SADGLKLFQSIVKYWR 221
Cdd:COG0047  160 ELEANGQVAFRYVDAdgnvtypaNPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGpgeSTDGLRIFRSAVKYFG 236
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-220 2.15e-129

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: 364.01  E-value: 2.15e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031    1 MKFAVIVFPGSNCDVDMYHAIAdELGEEVEYVWHDAENLDRFDAILLPGGFSYGDYLRSGAIARFSNVMKAVKKAADEGK 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALR-LLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   81 PVLGVCNGFQILLEAGLLPGAMRRNNSLKFICRPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQTLKRLIEN 160
Cdd:TIGR01737  80 PVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502275031  161 RQIVFRYHGE--------NPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSLLGSADGLKLFQSIVKYW 220
Cdd:TIGR01737 160 DQVVFRYCDEdgdvaeeaNPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVEWL 227
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-217 2.00e-118

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: 336.89  E-value: 2.00e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   3 FAVIVFPGSNCDVDMYHAIAdELGEEVEYVWHD-----AENLDRFDAILLPGGFSYGDYLRSGAIARFS-NVMKAVKKAA 76
Cdd:cd01740    1 VAVLRFPGSNCDRDMAYAFE-LAGFEAEDVWHNdllagRKDLDDYDGVVLPGGFSYGDYLRAGAIAAASpLLMEEVKEFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  77 DEGKPVLGVCNGFQILLEAGLLPGAMRRNNSLKFIC----RPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQ 152
Cdd:cd01740   80 ERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICrwqnRFVTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502275031 153 TLKRLIENRQIVFRY---------HGENPNGSLDDIAGIVNEKGNVLGMMPHPERAVDS-----LLGSADGLKLFQSIV 217
Cdd:cd01740  160 TLAELEENGQIAQYVdddgnvterYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPwqwerLLGGSDGLKLFRNAV 238
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 2-219 3.54e-60

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: 189.63  E-value: 3.54e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031    2 KFAVIVFPGSNCDVDMYHAIaDELGEEVEYVwH------DAENLDRFDAILLPGGFSYGDYLRSG-AIARFSNVMKAVKK 74
Cdd:pfam13507   3 RVAILREPGTNGEYEMAAAF-ERAGFDAVDV-HmsdllsGRVSLDDFQGLAAPGGFSYGDVLGSGkGWAASILFNPKLRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   75 A-----ADEGKPVLGVCNGFQILLEAGLLPGAMR----------RNNSLKFICRPVSLRVENNETMFtsAYKQGEVITIP 139
Cdd:pfam13507  81 AfeaffNRPDTFSLGICNGCQLLSKLGLIPGGEGdlaerwptltRNDSGRFESRWVNVKISEKSPSV--FLRGMDGSGLP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  140 IAHGEGN-YYCDEQTLKRLIENRQIVFRYHGE----------NPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSL----- 203
Cdd:pfam13507 159 VAHGEGRfVFRSEEVLARLEANGQVALRYVDNagnpteeypfNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWqwphw 238

                         250       260
                  ....*....|....*....|.
gi 502275031  204 -----LGSADGLKLFQSIVKY 219
Cdd:pfam13507 239 ppgewEEVSPWLRLFRNARKW 259
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-219 1.59e-172

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 472.68  E-value: 1.59e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   1 MKFAVIVFPGSNCDVDMYHAIADELGEEVEYVWHDAENLDRFDAILLPGGFSYGDYLRSGAIARFSNVMKAVKKAADEGK 80
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  81 PVLGVCNGFQILLEAGLLPGAMRRNNSLKFICRPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQTLKRLIEN 160
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502275031 161 RQIVFRYHGENPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSLLGSADGLKLFQSIVKY 219
Cdd:PRK03619 161 GQVVFRYCDENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-221 1.57e-143

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: 400.20  E-value: 1.57e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   1 MKFAVIVFPGSNCDVDMYHAIaDELGEEVEYVWHD--AENLDRFDAILLPGGFSYGDYLRSGAIARFSNVMKAVKKAADE 78
Cdd:COG0047    1 PKVAILVFPGSNCDRDMAAAF-ERAGAEAEDVWHSdlRTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  79 GKPVLGVCNGFQILLEAGLLPG---AMRRNNSLKFICRPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQTLK 155
Cdd:COG0047   80 GGLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502275031 156 RLIENRQIVFRYHGE--------NPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSLLG---SADGLKLFQSIVKYWR 221
Cdd:COG0047  160 ELEANGQVAFRYVDAdgnvtypaNPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGpgeSTDGLRIFRSAVKYFG 236
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-220 2.15e-129

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: 364.01  E-value: 2.15e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031    1 MKFAVIVFPGSNCDVDMYHAIAdELGEEVEYVWHDAENLDRFDAILLPGGFSYGDYLRSGAIARFSNVMKAVKKAADEGK 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALR-LLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   81 PVLGVCNGFQILLEAGLLPGAMRRNNSLKFICRPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQTLKRLIEN 160
Cdd:TIGR01737  80 PVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502275031  161 RQIVFRYHGE--------NPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSLLGSADGLKLFQSIVKYW 220
Cdd:TIGR01737 160 DQVVFRYCDEdgdvaeeaNPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVEWL 227
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-217 2.00e-118

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: 336.89  E-value: 2.00e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   3 FAVIVFPGSNCDVDMYHAIAdELGEEVEYVWHD-----AENLDRFDAILLPGGFSYGDYLRSGAIARFS-NVMKAVKKAA 76
Cdd:cd01740    1 VAVLRFPGSNCDRDMAYAFE-LAGFEAEDVWHNdllagRKDLDDYDGVVLPGGFSYGDYLRAGAIAAASpLLMEEVKEFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  77 DEGKPVLGVCNGFQILLEAGLLPGAMRRNNSLKFIC----RPVSLRVENNETMFTSAYKQGEVITIPIAHGEGNYYCDEQ 152
Cdd:cd01740   80 ERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICrwqnRFVTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502275031 153 TLKRLIENRQIVFRY---------HGENPNGSLDDIAGIVNEKGNVLGMMPHPERAVDS-----LLGSADGLKLFQSIV 217
Cdd:cd01740  160 TLAELEENGQIAQYVdddgnvterYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPwqwerLLGGSDGLKLFRNAV 238
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 1-224 1.43e-72

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 221.56  E-value: 1.43e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   1 MKFAVIVFPGSNCDVDMYHAIAdELGEEVEYVwH--DAEN----LDRFDAILLPGGFSYGDYLRSGAI--ARFSNV-MKA 71
Cdd:PRK01175   4 IRVAVLRMEGTNCEDETVKAFR-RLGVEPEYV-HinDLAAerksVSDYDCLVIPGGFSAGDYIRAGAIfaARLKAVlRKD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  72 VKKAADEGKPVLGVCNGFQILLEAGLLPG----------AMRRNNSLKFICRPVSLRVENNETMFTSAYKqGEVITIPIA 141
Cdd:PRK01175  82 IEEFIDEGYPIIGICNGFQVLVELGLLPGfdeiaekpemALTVNESNRFECRPTYLKKENRKCIFTKLLK-KDVFQVPVA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031 142 HGEGN-YYCDEQTLKRLIENRQIVFRYHGE---------NPNGSLDDIAGIVNEKGNVLGMMPHPERA--------VDSL 203
Cdd:PRK01175 161 HAEGRvVFSEEEILERLIENDQIVFRYVDEngnyagypwNPNGSIYNIAGITNEKGNVIGLMPHPERAfygyqhpyWEKE 240

                        250       260
                 ....*....|....*....|.
gi 502275031 204 LGSADGLKLFQSIVKYWRETH 224
Cdd:PRK01175 241 EDYGDGKIFFDSLINYLRKVH 261
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 2-219 3.54e-60

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: 189.63  E-value: 3.54e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031    2 KFAVIVFPGSNCDVDMYHAIaDELGEEVEYVwH------DAENLDRFDAILLPGGFSYGDYLRSG-AIARFSNVMKAVKK 74
Cdd:pfam13507   3 RVAILREPGTNGEYEMAAAF-ERAGFDAVDV-HmsdllsGRVSLDDFQGLAAPGGFSYGDVLGSGkGWAASILFNPKLRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   75 A-----ADEGKPVLGVCNGFQILLEAGLLPGAMR----------RNNSLKFICRPVSLRVENNETMFtsAYKQGEVITIP 139
Cdd:pfam13507  81 AfeaffNRPDTFSLGICNGCQLLSKLGLIPGGEGdlaerwptltRNDSGRFESRWVNVKISEKSPSV--FLRGMDGSGLP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  140 IAHGEGN-YYCDEQTLKRLIENRQIVFRYHGE----------NPNGSLDDIAGIVNEKGNVLGMMPHPERAVDSL----- 203
Cdd:pfam13507 159 VAHGEGRfVFRSEEVLARLEANGQVALRYVDNagnpteeypfNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWqwphw 238

                         250       260
                  ....*....|....*....|.
gi 502275031  204 -----LGSADGLKLFQSIVKY 219
Cdd:pfam13507 239 ppgewEEVSPWLRLFRNARKW 259
PRK05297 PRK05297
phosphoribosylformylglycinamidine synthase; Provisional
 10-200 1.97e-28

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 235394 [Multi-domain]  Cd Length: 1290  Bit Score: 112.59  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   10 GSNCDVDMYHAIaDELGEEVeyvwHD---------AENLDRFDAILLPGGFSYGDYLRSG-----AIaRFSNvmkavkKA 75
Cdd:PRK05297 1045 GVNSHVEMAAAF-DRAGFDA----IDvhmsdllagRVTLEDFKGLVACGGFSYGDVLGAGegwakSI-LFNP------RL 1112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   76 ADE-----GKP---VLGVCNGFQILLE-AGLLPGA-----MRRNNSLKFICRPVSLRV-ENNETMFTSAykQGEVITIPI 140
Cdd:PRK05297 1113 RDQfeaffARPdtfALGVCNGCQMMSNlKEIIPGAehwprFVRNRSEQFEARFSLVEVqESPSIFLQGM--AGSRLPIAV 1190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  141 AHGEGNYYCDEQTLKRLIENRQIVFRY---HGE-------NPNGSLDDIAGIVNEKGNVLGMMPHPERAV 200
Cdd:PRK05297 1191 AHGEGRAEFPDAHLAALEAKGLVALRYvdnHGQvtetypaNPNGSPNGITGLTTADGRVTIMMPHPERVF 1260
FGAM_synt TIGR01735
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ...
 2-200 1.26e-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: 104.48  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031     2 KFAVIVFPGSNCDVDMYHAIADELGEEVEYVWHD----AENLDRFDAILLPGGFSYGDYLRSG----AIARFSNVMKAVK 73
Cdd:TIGR01735 1057 KVAILREQGVNGDREMAAAFDRAGFEAWDVHMSDllagRVHLDEFRGLAACGGFSYGDVLGAGkgwaKSILFNPRLRDQF 1136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031    74 KA--ADEGKPVLGVCNGFQILLE-AGLLPG-----AMRRNNSLKFICRPVSLRVENNETMFTSAYkQGEVITIPIAHGEG 145
Cdd:TIGR01735 1137 QAffKRPDTFSLGVCNGCQMLSNlLEWIPGtenwpHFVRNNSERFEARVASVRVGESPSIMLRGM-AGSRLPVAVAHGEG 1215

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502275031   146 N-YYCDEQTLKRLIENRQIVFRY---HGE-------NPNGSLDDIAGIVNEKGNVLGMMPHPERAV 200
Cdd:TIGR01735 1216 YaAFSSPELQAQADASGLAALRYiddDGNpteayplNPNGSPGGIAGITSCDGRVTIMMPHPERVF 1281
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
 2-199 1.77e-25

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 104.08  E-value: 1.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031    2 KFAVIVFPGSNCDVDMYHAIADELGEEVEYVWHDAEN----LDRFDAILLPGGFSYGDYLRSG----AIARFS----NVM 69
Cdd:PLN03206 1039 KVAIIREEGSNGDREMAAAFYAAGFEPWDVTMSDLLNgrisLDDFRGIVFVGGFSYADVLDSAkgwaGSIRFNepllQQF 1118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   70 KAVKKAADEGKpvLGVCNGFQILLEAGLLPGAMR----------------RNNSLKFICRPVSLRVENNET-MFTSAykQ 132
Cdd:PLN03206 1119 QEFYNRPDTFS--LGVCNGCQLMALLGWVPGPQVggglgaggdpsqprfvHNESGRFECRFTSVTIEDSPAiMLKGM--E 1194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502275031  133 GEVITIPIAHGEGN-YYCDEQTLKRLIENRQIVFRY---HGE-------NPNGSLDDIAGIVNEKGNVLGMMPHPERA 199
Cdd:PLN03206 1195 GSTLGVWAAHGEGRaYFPDESVLDEVLKSNLAPVRYcddDGEpteqypfNPNGSPLGIAALCSPDGRHLAMMPHPERC 1272
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-93 8.68e-16

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: 70.71  E-value: 8.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   4 AVIVFPGSNC-DVDMYHAIADELGEEVEYVWHD------AENLDRFDAILLPGGFSYGDYLRsgaiaRFSNVMKAVKKAA 76
Cdd:cd01653    2 AVLLFPGFEElELASPLDALREAGAEVDVVSPDggpvesDVDLDDYDGLILPGGPGTPDDLA-----RDEALLALLREAA 76

                         90
                 ....*....|....*..
gi 502275031  77 DEGKPVLGVCNGFQILL 93
Cdd:cd01653   77 AAGKPILGICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-92 5.60e-15

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: 68.00  E-value: 5.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   4 AVIVFPGSNC-DVDMYHAIADELGEEVEYVWHD------AENLDRFDAILLPGGFSYGDYLRsgaiaRFSNVMKAVKKAA 76
Cdd:cd03128    2 AVLLFGGSEElELASPLDALREAGAEVDVVSPDggpvesDVDLDDYDGLILPGGPGTPDDLA-----WDEALLALLREAA 76

                         90
                 ....*....|....*.
gi 502275031  77 DEGKPVLGVCNGFQIL 92
Cdd:cd03128   77 AAGKPVLGICLGAQLL 92
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 4-92 3.97e-11

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: 59.95  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   4 AVIVFP-GSNcdVDMYHAIADELGEEVEYVwHDAENLDRFDAILLPGGFSYG---DYLRSGAIARfsnvmkAVKKAADEG 79
Cdd:cd01750    2 AVIRYPdISN--FTDLDPLAREPGVDVRYV-EVPEGLGDADLIILPGSKDTIqdlAWLRKRGLAE------AIKNYARAG 72

                         90
                 ....*....|...
gi 502275031  80 KPVLGVCNGFQIL 92
Cdd:cd01750   73 GPVLGICGGYQML 85
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 23-212 5.31e-11

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 59.76  E-value: 5.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  23 DELGEEVEyVWHDAENLDRFDAILLPGGFSYGDylrsgAIA--RFSNVMKAVKKAADEGKPVLGVCNGFQILLEA----- 95
Cdd:PRK13141  20 ERLGAEAV-ITSDPEEILAADGVILPGVGAFPD-----AMAnlRERGLDEVIKEAVASGKPLLGICLGMQLLFESseefg 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  96 -----GLLPGAMRR---NNSLKficrpV------SLRVENNETMFTsAYKQGE----VitipiaHGegnYYCDeqtlkrl 157
Cdd:PRK13141  94 eteglGLLPGRVRRfppEEGLK-----VphmgwnQLELKKESPLLK-GIPDGAyvyfV------HS---YYAD------- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502275031 158 IENRQIVFRY--HGEnpngsldDIAGIVnEKGNVLGMMPHPERavdsllgSAD-GLKL 212
Cdd:PRK13141 152 PCDEEYVAATtdYGV-------EFPAAV-GKDNVFGAQFHPEK-------SGDvGLKI 194
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 29-100 1.92e-10

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: 57.65  E-value: 1.92e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502275031   29 VEYVWHDAeNLDRFDAILLPGGFSYGDYLRSGAIarfsnVMKAVKKAADEGKPVLGVCNGFQILLEAGLLPG 100
Cdd:pfam01965  50 VDASLDDV-KPDDYDALVLPGGRAGPERLRDNEK-----LVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKG 115
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 40-100 2.11e-10

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: 57.55  E-value: 2.11e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502275031  40 DRFDAILLPGGFSyGDYLRsgaiaRFSNVMKAVKKAADEGKPVLGVCNGFQILLEAGLLPG 100
Cdd:cd03134   61 DDYDALVIPGGTN-PDKLR-----RDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRG 115
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 38-100 6.82e-10

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: 56.27  E-value: 6.82e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502275031  38 NLDRFDAILLPGGFSYGDYLRsgaiaRFSNVMKAVKKAADEGKPVLGVCNGFQILLEAGLLPG 100
Cdd:COG0693   61 DPDDYDALVLPGGHGAPDDLR-----EDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKG 118
GATase pfam00117
Glutamine amidotransferase class-I;
15-218 1.66e-09

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 55.32  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   15 VDMY----HAIAD---ELGEEVEYVWHDAENL----DRFDAILLPGGFsygdylrsGAIARFSNVMKAVKKAADEGKPVL 83
Cdd:pfam00117   3 IDNGdsftYNLARalrELGVEVTVVPNDTPAEeileENPDGIILSGGP--------GSPGAAGGAIEAIREARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   84 GVCNGFQIL-LEAGLLPGAMRrnnslKFICRPVSLRVENNETmfTSAYKQGEVITIPIAHGegnYYCDEQTLKRLIEnrq 162
Cdd:pfam00117  75 GICLGHQLLaLAFGGKVVKAK-----KFGHHGKNSPVGDDGC--GLFYGLPNVFIVRRYHS---YAVDPDTLPDGLE--- 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 502275031  163 IVFryhgENPNGslDDIAGIVNEKGNVLGMMPHPEravdSLLGSADGLKLFQSIVK 218
Cdd:pfam00117 142 VTA----TSEND--GTIMGIRHKKLPIFGVQFHPE----SILTPHGPEILFNFFIK 187
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 23-104 4.18e-09

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: 54.43  E-value: 4.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  23 DELGEEVEYVwHDAENLDRFDAILLPGGFSYGDylrsgAIARF--SNVMKAVKKAADEGKPVLGVCNGFQILLEA----- 95
Cdd:cd01748   19 ERLGAEVIIT-SDPEEILSADKLILPGVGAFGD-----AMANLreRGLIEALKEAIASGKPFLGICLGMQLLFESseegg 92

                         90
                 ....*....|....
gi 502275031  96 -----GLLPGAMRR 104
Cdd:cd01748   93 gtkglGLIPGKVVR 106
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 25-104 6.45e-09

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: 53.89  E-value: 6.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  25 LGEEVEyVWHDAENLDRFDAILLPG-GfSYGD---YLRSgaiarfSNVMKAVKKAADEGKPVLGVCNGFQILLEA----- 95
Cdd:COG0118   23 LGAEVV-VTSDPDEIRAADRLVLPGvG-AFGDameNLRE------RGLDEAIREAVAGGKPVLGICLGMQLLFERseeng 94

                         90
                 ....*....|....
gi 502275031  96 -----GLLPGAMRR 104
Cdd:COG0118   95 dteglGLIPGEVVR 108
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 4-92 1.07e-08

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: 54.68  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   4 AVIVFPG-SN-CDVDmyhAIADELGEEVEYVwHDAENLDRFDAILLPGgfS---YGD--YLRSGAIArfsnvmKAVKKAA 76
Cdd:COG1492  255 AVIRLPRiSNfTDFD---PLAAEPGVRLRYV-RPPEELGDADLVILPG--SkntIADlaWLRESGLD------DAIRAHA 322

                         90
                 ....*....|....*.
gi 502275031  77 DEGKPVLGVCNGFQIL 92
Cdd:COG1492  323 RRGGPVLGICGGYQML 338
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 19-100 1.95e-08

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: 52.27  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  19 HAIADELGEE--VEYVWH--------DAENLDRFDAILLPGGFSyGDYLRSGAiarfsNVMKAVKKAADEGKPVLGVCNG 88
Cdd:cd03169   44 TAIHDFPGWQtyTEKPGHrfavtadfDEVDPDDYDALVIPGGRA-PEYLRLDE-----KVLAIVRHFAEANKPVAAICHG 117

                         90
                 ....*....|..
gi 502275031  89 FQILLEAGLLPG 100
Cdd:cd03169  118 PQILAAAGVLKG 129
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
4-92 3.11e-08

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 51.86  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031    4 AVIVFPG-SN---CDVDMYHAIADELGEEVEYvwHDAENLDRFDAILLPGGFsygDYLRSGAIARFSNVMKAVKKAADEG 79
Cdd:pfam07685   3 AVIRLPRiSNytdDNLDPLRYEPAVRVRFVPL--PDESLGPDADLIILPGGK---PTIQDLALLRNSGMDEAIKEAAEDG 77

                          90
                  ....*....|...
gi 502275031   80 KPVLGVCNGFQIL 92
Cdd:pfam07685  78 GPVLGICGGYQML 90
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 38-100 6.83e-08

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: 50.49  E-value: 6.83e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502275031   38 NLDRFDAILLPGGFSyGDYLRSGaiarfSNVMKAVKKAADEGKPVLGVCNGFQILLEAGLLPG 100
Cdd:TIGR01382  57 NPEEYDALVIPGGRA-PEYLRLN-----NKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRG 113
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 26-222 1.15e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 50.25  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  26 GEEVEyVWHDAENLDRFDAILLPGGFSYGDylrsgAIARFSNVMKAVKKAADEGKPVLGVCNGFQILLEA---------- 95
Cdd:PRK13143  24 GAEVV-ITSDPEEILDADGIVLPGVGAFGA-----AMENLSPLRDVILEAARSGKPFLGICLGMQLLFESseegggvrgl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  96 GLLPGAMRR-NNSLKficrpV------SLRVENNetmftsaykqgevitIPIAHG-EGNYYcdeqtlkrlienrQIVFRY 167
Cdd:PRK13143  98 GLFPGRVVRfPAGVK-----VphmgwnTVKVVKD---------------CPLFEGiDGEYV-------------YFVHSY 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502275031 168 H-----GENPNGSLD---DIAGIVNeKGNVLGMMPHPERAvdsllgSADGLKLFQSIVKYWRE 222
Cdd:PRK13143 145 YaypddEDYVVATTDygiEFPAAVC-NDNVFGTQFHPEKS------GETGLKILENFVELIKR 200
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 16-91 1.98e-07

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: 49.86  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  16 DMYHAI-------ADELGEEVEYVWHDAEN---------LDRFDAILLPGGFSYgdylrsgaiaR-FSNVMKAVKKAADE 78
Cdd:cd01746   14 DAYLSVlealkhaGIALGVKLEIKWIDSEDleeenaeeaLKGADGILVPGGFGI----------RgVEGKILAIKYAREN 83

                         90
                 ....*....|...
gi 502275031  79 GKPVLGVCNGFQI 91
Cdd:cd01746   84 NIPFLGICLGMQL 96
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 35-100 2.00e-07

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 49.09  E-value: 2.00e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502275031  35 DAENLDRFDAILLPGGFSYGDYLRSGAIarfsnVMKAVKKAADEGKPVLGVCNGFQILLEAGLLPG 100
Cdd:cd03135   54 SDVNLDDYDAIVIPGGLPGAQNLADNEK-----LIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKG 114
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 35-104 1.85e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 46.78  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  35 DAENLDRFDAILLPGGFSYGDylrsgAIARF--SNVMKAVKKAADEGKPVLGVCNGFQILLEA---------GLLPGAMR 103
Cdd:PRK13181  31 DPEEIAGADKVILPGVGAFGQ-----AMRSLreSGLDEALKEHVEKKQPVLGICLGMQLLFESseegnvkglGLIPGDVK 105


                 .
gi 502275031 104 R 104
Cdd:PRK13181 106 R 106
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-93 2.25e-06

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 46.80  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   1 MKFAVIVFPGsncDV----DMYHAIADELGEEVEYVW-HDAENLDRFDAILLPGGfsygdylRSGAIARF---SNVMKAV 72
Cdd:PRK13527   1 MKIGVLALQG---DVeehiDALKRALDELGIDGEVVEvRRPGDLPDCDALIIPGG-------ESTTIGRLmkrEGILDEI 70

                         90       100
                 ....*....|....*....|.
gi 502275031  73 KKAADEGKPVLGVCNGFqILL 93
Cdd:PRK13527  71 KEKIEEGLPILGTCAGL-ILL 90
PRK00784 PRK00784
cobyric acid synthase;
4-92 2.38e-06

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 47.39  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   4 AVIVFPG-SN-CDVDmyhAIADELGEEVEYVwHDAENLDRFDAILLPGgfS---YGD--YLRSGAIArfsnvmKAVKKAA 76
Cdd:PRK00784 255 AVIRLPRiSNfTDFD---PLRAEPGVDVRYV-RPGEPLPDADLVILPG--SkntIADlaWLRESGWD------EAIRAHA 322

                         90
                 ....*....|....*.
gi 502275031  77 DEGKPVLGVCNGFQIL 92
Cdd:PRK00784 323 RRGGPVLGICGGYQML 338
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 39-92 3.13e-06

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: 46.32  E-value: 3.13e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502275031  39 LDRFDAILLPGG-----FSYGD--YLRSGAI--ARFSNVMKAVKKAADEGKPVLGVCNGFQIL 92
Cdd:COG2071   47 LDRLDGLVLTGGadvdpALYGEepHPELGPIdpERDAFELALIRAALERGKPVLGICRGMQLL 109
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 19-93 3.31e-06

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: 45.98  E-value: 3.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502275031  19 HAIA-DELGEEVEYVWhDAENLDRFDAILLPGGfsygdylRSGAIARF---SNVMKAVKKAADEGKPVLGVCNGFqILL 93
Cdd:cd01749   13 HIRAlERLGVEVIEVR-TPEDLEGIDGLIIPGG-------ESTTIGKLlrrTGLLDPLREFIRAGKPVFGTCAGL-ILL 82
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 36-95 1.84e-05

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: 43.72  E-value: 1.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502275031  36 AENLDRFDAILLPGG-----FSYGDYL--RSGAIA----RFSnvMKAVKKAADEGKPVLGVCNGFQILLEA 95
Cdd:cd01745   48 EQYLELLDGLLLTGGgdvdpPLYGEEPhpELGPIDperdAFE--LALLRAALERGKPILGICRGMQLLNVA 116
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 25-104 2.29e-05

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: 43.85  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   25 LGEEVEYVwHDAENLDRFDAILLPGGFSYGDYLRSgaiARFSNVMKAVKKAADEGKPVLGVCNGFQILLEA--------- 95
Cdd:TIGR01855  21 VGAEPVVV-KDSKEAELADKLILPGVGAFGAAMAR---LRENGLDLFVELVVRLGKPVLGICLGMQLLFERseegggvpg 96

                          90
                  ....*....|
gi 502275031   96 -GLLPGAMRR 104
Cdd:TIGR01855  97 lGLIKGNVVK 106
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 14-95 3.69e-05

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: 43.00  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  14 DVDMYHAIADELGEEveyvwhdaenLDRFDAILLPGGFSYGDYLRSGAIARfsnVMKAVKKAADEGKPVLGVCNGFQILL 93
Cdd:cd01741   29 EIDVVDVYAGELLPD----------LDDYDGLVILGGPMSVDEDDYPWLKK---LKELIRQALAAGKPVLGICLGHQLLA 95


                 ..
gi 502275031  94 EA 95
Cdd:cd01741   96 RA 97
PRK06186 PRK06186
hypothetical protein; Validated
 12-94 4.03e-05

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 43.41  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  12 NCDVDMYHAI-------ADELGEEVEYVW------HDAENLDRFDAILLPGGFSYGDylRSGAIArfsnvmkAVKKAADE 78
Cdd:PRK06186  11 NPDVTAHQAIplaldlaAAVLGLPVDYEWlptpeiTDPEDLAGFDGIWCVPGSPYRN--DDGALT-------AIRFAREN 81

                         90
                 ....*....|....*..
gi 502275031  79 GKPVLGVCNGFQ-ILLE 94
Cdd:PRK06186  82 GIPFLGTCGGFQhALLE 98
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 1-98 5.11e-05

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 43.22  E-value: 5.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   1 MKFAVIVFPGSN-----CDVDMYHAIADELGEEVeYVW---------------------HDAENLDRFDAILLPGGFSYG 54
Cdd:COG4977    1 LRVAFLLLPGFSlldlaGPLEVFRLANRLAGRPL-YRWrlvsldggpvrsssgltvapdHGLADLAAADTLIVPGGLDPA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502275031  55 DYLRSGAIArfsnvmkAVKKAADEGKPVLGVCNGFQILLEAGLL 98
Cdd:COG4977   80 AAADPALLA-------WLRRAAARGARLASICTGAFLLAAAGLL 116
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 26-104 6.22e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 42.46  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  26 GEEVEyVWHDAENLDRFDAILLPGGFSYGDYLRS-GAIARFSNVMKAVKKAadeGKPVLGVCNGFQILLEA--------- 95
Cdd:PRK13146  27 GADVV-VTADPDAVAAADRVVLPGVGAFADCMRGlRAVGLGEAVIEAVLAA---GRPFLGICVGMQLLFERglehgdtpg 102

                         90
                 ....*....|
gi 502275031  96 -GLLPGAMRR 104
Cdd:PRK13146 103 lGLIPGEVVR 112
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 32-100 1.46e-04

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: 41.48  E-value: 1.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502275031  32 VWHDAENLDRFDAILLPGgFSYGDylRSGAIARFSNVMKAVKKAADEGKPVLGVCNGFQILLEAGLLPG 100
Cdd:cd03138   60 PDATLADVPAPDLVIVPG-LGGDP--DELLLADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDG 125
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 25-92 1.67e-04

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: 41.47  E-value: 1.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502275031   25 LGEEVEYVwhdAENLDRFDAILLPGGFS-----YGD--YLRSGAI--ARFSNVMKAVKKAADEGKPVLGVCNGFQIL 92
Cdd:pfam07722  45 ILGDPEDA---AAILDRLDGLLLTGGPNvdphfYGEepSESGGPYdpARDAYELALIRAALARGKPILGICRGFQLL 118
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 34-92 3.13e-04

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


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 40.55  E-value: 3.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502275031  34 HDAENLDRFDAILLPGGfsyGDYLRSGAIARFSNVMKAVKKAADEGKPVLGVCNGFQIL 92
Cdd:COG3442   43 GDDLPFDDVDIVFIGGG---QDREQEIVADDLLRIKDALRAAIEDGVPVLAICGGYQLL 98
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 3-100 3.17e-04

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. 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 some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153230 [Multi-domain]  Cd Length: 185  Bit Score: 40.26  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031   3 FAVIVFPGSN-----CDVDMYHAIADELGEEVeYVWH---------------------DAENLDRFDAILLPGGFSYGDY 56
Cdd:cd03136    1 FGFLLLPGFSllalaSAIEPLRAANRLAGREL-YRWRvlsldgapvtssnglrvapdaALEDAPPLDYLFVVGGLGARRA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502275031  57 LRSGAIArfsnvmkAVKKAADEGKPVLGVCNGFQILLEAGLLPG 100
Cdd:cd03136   80 VTPALLA-------WLRRAARRGVALGGIDTGAFLLARAGLLDG 116
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
36-105 4.03e-04

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 39.76  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  36 AENLDRFDAILLPGGFSygdyLRSGAIARFSNVMKAVKKAADEGKPVLGVCNGFqILLeA-----------GLLPGAMRR 104
Cdd:PRK13525  33 PEDLDEIDGLILPGGES----TTMGKLLRDFGLLEPLREFIASGLPVFGTCAGM-ILL-AkeiegyeqehlGLLDITVRR 106


                 .
gi 502275031 105 N 105
Cdd:PRK13525 107 N 107
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 34-104 4.33e-04

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: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 39.79  E-value: 4.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502275031  34 HDAENLDRFDAILLPGGFSYGDYLRSGAiarfsnVMKAVKKAADEGKPVLGVCNGFQILLEAGLLPGamRR 104
Cdd:cd03137   57 AGLDALAAADTVIVPGGPDVDGRPPPPA------LLAALRRAAARGARVASVCTGAFVLAEAGLLDG--RR 119
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
24-100 5.51e-04

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 40.50  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  24 ELGEEVEYV--WHDaENLDRFDAILLPGGFSYgdyLRSGAIARFSNVMKAVKKAADEGKPVLGVCNGFQILLE------- 94
Cdd:PRK01077 269 AAGAELVFFspLAD-EALPDCDGLYLGGGYPE---LFAAELAANTSMRASIRAAAAAGKPIYAECGGLMYLGEsledadg 344

                         90
                 ....*....|.
gi 502275031  95 -----AGLLPG 100
Cdd:PRK01077 345 erhpmVGLLPG 355
pyrG PRK05380
CTP synthetase; Validated
 28-91 5.83e-04

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 40.39  E-value: 5.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502275031  28 EVEYVWHDAENLDR---------FDAILLPGGFsyGDylR--SGAIArfsnvmkAVKKAADEGKPVLGVCNGFQI 91
Cdd:PRK05380 321 KVNIKWIDSEDLEEenvaellkgVDGILVPGGF--GE--RgiEGKIL-------AIRYARENNIPFLGICLGMQL 384
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 24-95 7.14e-04

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: 39.05  E-value: 7.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502275031  24 ELGEEVEYVWHDA-----ENLDRFDAILL-PGgfsYGDYLRSGaiarfsnVMKAVKKAADEGKPVLGVCNGFQILLEA 95
Cdd:cd01743   20 ELGAEVVVVRNDEitleeLELLNPDAIVIsPG---PGHPEDAG-------ISLEIIRALAGKVPILGVCLGHQAIAEA 87
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 18-95 1.36e-03

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: 38.48  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  18 YHAIAdELGEEVEYVWHDAENLD-----RFDAILL---PGgfsygdylrsgaIARFSNVMKAVKKAADEGKPVLGVCNGF 89
Cdd:COG0512   15 VQYLG-ELGAEVVVVRNDEITLEeiealAPDGIVLspgPG------------TPEEAGISLEVIRAFAGKIPILGVCLGH 81


                 ....*.
gi 502275031  90 QILLEA 95
Cdd:COG0512   82 QAIGEA 87
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 25-114 1.43e-03

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 39.31  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  25 LGEEVEYVwHDAENLDRFDAILLPGGFSYG---DYLRSGAIArfsnvmKAVKKAADEGKPVLGVCNGFQILLEA------ 95
Cdd:PLN02617  29 LGFTIKDV-QTPEDILNADRLIFPGVGAFGsamDVLNNRGMA------EALREYIQNDRPFLGICLGLQLLFESseengp 101

                         90       100
                 ....*....|....*....|...
gi 502275031  96 ----GLLPGAMRRNNSLKFICRP 114
Cdd:PLN02617 102 veglGVIPGVVGRFDSSNGLRVP 124
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 16-92 1.69e-03

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: 38.39  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  16 DMYHAIADELGEEVEYV-------WHDAENLDRFDAILLPGG----FSYGDYLRsgaiarfsNVMKAVKKAADEGKPVLG 84
Cdd:COG0518   16 GLIARRLREAGIELDVLrvyageiLPYDPDLEDPDGLILSGGpmsvYDEDPWLE--------DEPALIREAFELGKPVLG 87


                 ....*...
gi 502275031  85 VCNGFQIL 92
Cdd:COG0518   88 ICYGAQLL 95
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 43-110 2.58e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB 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 CobB.


Pssm-ID: 153224 [Multi-domain]  Cd Length: 198  Bit Score: 37.58  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502275031  43 DAILLPGGFSYgdyLRSGAIARFSNVMKAVKKAADEGKPVLGVCNGFQILLE------------AGLLPGAMRRNNSLKF 110
Cdd:cd03130   42 DGLYLGGGYPE---LFAEELSANQSMRESIRAFAESGGPIYAECGGLMYLGEslddeegqsypmAGVLPGDARMTKRLGL 118
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 35-95 2.63e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 37.58  E-value: 2.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502275031  35 DAENLDRFDAILLPGGfsyGDYLRSGAIARFSNVMKAVKKAADEGKPVLGVCNGFQILLEA 95
Cdd:PRK14004  31 DPETIENSKALILPGD---GHFDKAMENLNSTGLRSTIDKHVESGKPLFGICIGFQILFES 88
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 28-91 3.99e-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: 37.68  E-value: 3.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502275031  28 EVEYVWHDAENLDR---------FDAILLPGGFsyGDylR--SGAIArfsnvmkAVKKAADEGKPVLGVCNGFQI 91
Cdd:COG0504  322 KVNIKWIDSEDLEEenaeellkgVDGILVPGGF--GE--RgiEGKIA-------AIRYARENKIPFLGICLGMQL 385
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 40-92 4.07e-03

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: 36.71  E-value: 4.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502275031  40 DRFDAILLPGGfsygdylrSGAIARFSNVMKAVKKAADEGKPVLGVCNGFQIL 92
Cdd:cd01744   38 LDPDGIFLSNG--------PGDPALLDEAIKTVRKLLGKKIPIFGICLGHQLL 82
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 34-100 4.67e-03

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: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 36.75  E-value: 4.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502275031  34 HDAENLDRFDAILLPGGfsYGDYLrsgAIARfSNVMKAVKKAADEGKPVLGVCNGFQILLEAGLLPG 100
Cdd:cd03139   55 TSFADPPDLDVLLVPGG--GGTRA---LVND-PALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDG 115
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 34-98 5.41e-03

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: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 36.43  E-value: 5.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502275031  34 HDAENLDRFDAILLPGGFSYgDYLRSGAIARFsnvmkaVKKAADEGKPVLGVCNGFQILLEAGLL 98
Cdd:cd03140   53 LDDLPPEDYDLLILPGGDSW-DNPEAPDLAGL------VRQALKQGKPVAAICGATLALARAGLL 110
PLN02327 PLN02327
CTP synthase
 16-91 9.26e-03

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 36.93  E-value: 9.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502275031  16 DMYHAIADELGEEVEYVWhdaENLDRFDAILLPGGFsyGDYLRSGAIArfsnvmkAVKKAADEGKPVLGVCNGFQI 91
Cdd:PLN02327 340 DLEDETAKETPDAYAAAW---KLLKGADGILVPGGF--GDRGVEGKIL-------AAKYARENKVPYLGICLGMQI 403
 
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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