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Conserved domains on  [gi|1698401979|ref|WP_141603123|]
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MULTISPECIES: phosphoribosylformylglycinamidine synthase subunit PurQ [Ureibacillus]

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;
1-218 1.12e-173

phosphoribosylformylglycinamidine synthase subunit PurQ;


:

Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 475.37  E-value: 1.12e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGSNCDVDMYHAIKDELGEEVEFVWHDATDLSGFDAILIPGGFSYGDYLRCGAMASQSNVMKAVKEAAEEGK 80
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  81 PILGVCNGFQILTEAGLLPGALLRNKNLKFICRTVPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEETLKKLKEN 160
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698401979 161 NQIVFTYAGENPNGSLENIAGIVNERGNVLGMMPHPERAVDALLGSADGLALFKSIVK 218
Cdd:PRK03619  161 GQVVFRYCDENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-218 1.12e-173

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 475.37  E-value: 1.12e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGSNCDVDMYHAIKDELGEEVEFVWHDATDLSGFDAILIPGGFSYGDYLRCGAMASQSNVMKAVKEAAEEGK 80
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  81 PILGVCNGFQILTEAGLLPGALLRNKNLKFICRTVPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEETLKKLKEN 160
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698401979 161 NQIVFTYAGENPNGSLENIAGIVNERGNVLGMMPHPERAVDALLGSADGLALFKSIVK 218
Cdd:PRK03619  161 GQVVFRYCDENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-221 3.06e-144

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: 401.74  E-value: 3.06e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGSNCDVDMYHAIKDeLGEEVEFVWHD--ATDLSGFDAILIPGGFSYGDYLRCGAMASQSNVMKAVKEAAEE 78
Cdd:COG0047     1 PKVAILVFPGSNCDRDMAAAFER-AGAEAEDVWHSdlRTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  79 GKPILGVCNGFQILTEAGLLPG---ALLRNKNLKFICRTVPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEETLK 155
Cdd:COG0047    80 GGLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698401979 156 KLKENNQIVFTYAGE--------NPNGSLENIAGIVNERGNVLGMMPHPERAVDALLG---SADGLALFKSIVKQWR 221
Cdd:COG0047   160 ELEANGQVAFRYVDAdgnvtypaNPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGpgeSTDGLRIFRSAVKYFG 236
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-220 7.14e-132

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: 370.17  E-value: 7.14e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGSNCDVDMYHAIKdELGEEVEFVWHDATDLSGFDAILIPGGFSYGDYLRCGAMASQSNVMKAVKEAAEEGK 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALR-LLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  81 PILGVCNGFQILTEAGLLPGALLRNKNLKFICRTVPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEETLKKLKEN 160
Cdd:TIGR01737  80 PVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698401979 161 NQIVFTYAGE--------NPNGSLENIAGIVNERGNVLGMMPHPERAVDALLGSADGLALFKSIVKQW 220
Cdd:TIGR01737 160 DQVVFRYCDEdgdvaeeaNPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVEWL 227
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-217 4.60e-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: 335.74  E-value: 4.60e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   3 FAVLVFPGSNCDVDMYHAIKdELGEEVEFVWHD-----ATDLSGFDAILIPGGFSYGDYLRCGAMASQS-NVMKAVKEAA 76
Cdd:cd01740     1 VAVLRFPGSNCDRDMAYAFE-LAGFEAEDVWHNdllagRKDLDDYDGVVLPGGFSYGDYLRAGAIAAASpLLMEEVKEFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  77 EEGKPILGVCNGFQILTEAGLLPGALLRNKNLKFICRT----VPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEE 152
Cdd:cd01740    80 ERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWqnrfVTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698401979 153 TLKKLKENNQIVFTYA---------GENPNGSLENIAGIVNERGNVLGMMPHPERAVDA-----LLGSADGLALFKSIV 217
Cdd:cd01740   160 TLAELEENGQIAQYVDddgnvteryPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPwqwerLLGGSDGLKLFRNAV 238
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 2-218 1.81e-56

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: 180.00  E-value: 1.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   2 KFAVLVFPGSNCDVDMYHAIKDElGEEVEFVwH------DATDLSGFDAILIPGGFSYGDYLrcGAMASQSNVMK---AV 72
Cdd:pfam13507   3 RVAILREPGTNGEYEMAAAFERA-GFDAVDV-HmsdllsGRVSLDDFQGLAAPGGFSYGDVL--GSGKGWAASILfnpKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  73 KEA-----AEEGKPILGVCNGFQILTEAGLLPG----------ALLRNKNLKFICRTVPLKVENNQTMFTNQydQGQIIH 137
Cdd:pfam13507  79 RDAfeaffNRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRWVNVKISEKSPSVFLR--GMDGSG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 138 IPIAHGEGN-YYCDEETLKKLKENNQIVFTYAGE----------NPNGSLENIAGIVNERGNVLGMMPHPERAVDAL--- 203
Cdd:pfam13507 157 LPVAHGEGRfVFRSEEVLARLEANGQVALRYVDNagnpteeypfNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWqwp 236

                         250       260
                  ....*....|....*....|..
gi 1698401979 204 -------LGSADGLALFKSIVK 218
Cdd:pfam13507 237 hwppgewEEVSPWLRLFRNARK 258
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-218 1.12e-173

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 475.37  E-value: 1.12e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGSNCDVDMYHAIKDELGEEVEFVWHDATDLSGFDAILIPGGFSYGDYLRCGAMASQSNVMKAVKEAAEEGK 80
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  81 PILGVCNGFQILTEAGLLPGALLRNKNLKFICRTVPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEETLKKLKEN 160
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698401979 161 NQIVFTYAGENPNGSLENIAGIVNERGNVLGMMPHPERAVDALLGSADGLALFKSIVK 218
Cdd:PRK03619  161 GQVVFRYCDENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-221 3.06e-144

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: 401.74  E-value: 3.06e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGSNCDVDMYHAIKDeLGEEVEFVWHD--ATDLSGFDAILIPGGFSYGDYLRCGAMASQSNVMKAVKEAAEE 78
Cdd:COG0047     1 PKVAILVFPGSNCDRDMAAAFER-AGAEAEDVWHSdlRTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  79 GKPILGVCNGFQILTEAGLLPG---ALLRNKNLKFICRTVPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEETLK 155
Cdd:COG0047    80 GGLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698401979 156 KLKENNQIVFTYAGE--------NPNGSLENIAGIVNERGNVLGMMPHPERAVDALLG---SADGLALFKSIVKQWR 221
Cdd:COG0047   160 ELEANGQVAFRYVDAdgnvtypaNPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGpgeSTDGLRIFRSAVKYFG 236
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-220 7.14e-132

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: 370.17  E-value: 7.14e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGSNCDVDMYHAIKdELGEEVEFVWHDATDLSGFDAILIPGGFSYGDYLRCGAMASQSNVMKAVKEAAEEGK 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALR-LLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  81 PILGVCNGFQILTEAGLLPGALLRNKNLKFICRTVPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEETLKKLKEN 160
Cdd:TIGR01737  80 PVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698401979 161 NQIVFTYAGE--------NPNGSLENIAGIVNERGNVLGMMPHPERAVDALLGSADGLALFKSIVKQW 220
Cdd:TIGR01737 160 DQVVFRYCDEdgdvaeeaNPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVEWL 227
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-217 4.60e-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: 335.74  E-value: 4.60e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   3 FAVLVFPGSNCDVDMYHAIKdELGEEVEFVWHD-----ATDLSGFDAILIPGGFSYGDYLRCGAMASQS-NVMKAVKEAA 76
Cdd:cd01740     1 VAVLRFPGSNCDRDMAYAFE-LAGFEAEDVWHNdllagRKDLDDYDGVVLPGGFSYGDYLRAGAIAAASpLLMEEVKEFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  77 EEGKPILGVCNGFQILTEAGLLPGALLRNKNLKFICRT----VPLKVENNQTMFTNQYDQGQIIHIPIAHGEGNYYCDEE 152
Cdd:cd01740    80 ERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWqnrfVTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698401979 153 TLKKLKENNQIVFTYA---------GENPNGSLENIAGIVNERGNVLGMMPHPERAVDA-----LLGSADGLALFKSIV 217
Cdd:cd01740   160 TLAELEENGQIAQYVDddgnvteryPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPwqwerLLGGSDGLKLFRNAV 238
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 1-224 8.37e-69

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 211.54  E-value: 8.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGSNCDVDMYHAIKdELGEEVEFVwH--DATD----LSGFDAILIPGGFSYGDYLRCGAMAS---QSNVMKA 71
Cdd:PRK01175    4 IRVAVLRMEGTNCEDETVKAFR-RLGVEPEYV-HinDLAAerksVSDYDCLVIPGGFSAGDYIRAGAIFAarlKAVLRKD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  72 VKEAAEEGKPILGVCNGFQILTEAGLLPG----------ALLRNKNLKFICRTVPLKVENNQTMFTNQYDQGqIIHIPIA 141
Cdd:PRK01175   82 IEEFIDEGYPIIGICNGFQVLVELGLLPGfdeiaekpemALTVNESNRFECRPTYLKKENRKCIFTKLLKKD-VFQVPVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 142 HGEGN-YYCDEETLKKLKENNQIVFTYAGE---------NPNGSLENIAGIVNERGNVLGMMPHPERA--------VDAL 203
Cdd:PRK01175  161 HAEGRvVFSEEEILERLIENDQIVFRYVDEngnyagypwNPNGSIYNIAGITNEKGNVIGLMPHPERAfygyqhpyWEKE 240

                         250       260
                  ....*....|....*....|.
gi 1698401979 204 LGSADGLALFKSIVKQWRETH 224
Cdd:PRK01175  241 EDYGDGKIFFDSLINYLRKVH 261
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 2-218 1.81e-56

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: 180.00  E-value: 1.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   2 KFAVLVFPGSNCDVDMYHAIKDElGEEVEFVwH------DATDLSGFDAILIPGGFSYGDYLrcGAMASQSNVMK---AV 72
Cdd:pfam13507   3 RVAILREPGTNGEYEMAAAFERA-GFDAVDV-HmsdllsGRVSLDDFQGLAAPGGFSYGDVL--GSGKGWAASILfnpKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  73 KEA-----AEEGKPILGVCNGFQILTEAGLLPG----------ALLRNKNLKFICRTVPLKVENNQTMFTNQydQGQIIH 137
Cdd:pfam13507  79 RDAfeaffNRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRWVNVKISEKSPSVFLR--GMDGSG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 138 IPIAHGEGN-YYCDEETLKKLKENNQIVFTYAGE----------NPNGSLENIAGIVNERGNVLGMMPHPERAVDAL--- 203
Cdd:pfam13507 157 LPVAHGEGRfVFRSEEVLARLEANGQVALRYVDNagnpteeypfNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWqwp 236

                         250       260
                  ....*....|....*....|..
gi 1698401979 204 -------LGSADGLALFKSIVK 218
Cdd:pfam13507 237 hwppgewEEVSPWLRLFRNARK 258
PRK05297 PRK05297
phosphoribosylformylglycinamidine synthase; Provisional
 2-200 3.60e-25

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 235394 [Multi-domain]  Cd Length: 1290  Bit Score: 102.96  E-value: 3.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979    2 KFAVLVFPGSNCDVDMYHAikdelgeeveFvwhdatDLSGFDAI------LIP--------------GGFSYGDYLrcGA 61
Cdd:PRK05297  1037 KVAILREQGVNSHVEMAAA----------F------DRAGFDAIdvhmsdLLAgrvtledfkglvacGGFSYGDVL--GA 1098

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   62 ---MAsqsnvmKAVK---EAAEE-----GKP---ILGVCNGFQILTE-AGLLPGA-----LLRNKNLKFICRTVPLKVEN 121
Cdd:PRK05297  1099 gegWA------KSILfnpRLRDQfeaffARPdtfALGVCNGCQMMSNlKEIIPGAehwprFVRNRSEQFEARFSLVEVQE 1172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  122 N-----QTMftnqydQGQIIHIPIAHGEGNYYCDEETLKKLKENNQIVFTY---AGE-------NPNGSLENIAGIVNER 186
Cdd:PRK05297  1173 SpsiflQGM------AGSRLPIAVAHGEGRAEFPDAHLAALEAKGLVALRYvdnHGQvtetypaNPNGSPNGITGLTTAD 1246

                          250
                   ....*....|....
gi 1698401979  187 GNVLGMMPHPERAV 200
Cdd:PRK05297  1247 GRVTIMMPHPERVF 1260
FGAM_synt TIGR01735
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ...
 2-202 7.30e-24

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: 99.09  E-value: 7.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979    2 KFAVLVFPGSNCDVDMYHAIKDELGEEVEFVWHD----ATDLSGFDAILIPGGFSYGDYLRCG---AMASQSNVMKAVKE 74
Cdd:TIGR01735 1057 KVAILREQGVNGDREMAAAFDRAGFEAWDVHMSDllagRVHLDEFRGLAACGGFSYGDVLGAGkgwAKSILFNPRLRDQF 1136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   75 AAEEGKP---ILGVCNGFQILTE-AGLLPG-----ALLRNKNLKFICRTVPLKVENNQTMFTNQYdQGQIIHIPIAHGEG 145
Cdd:TIGR01735 1137 QAFFKRPdtfSLGVCNGCQMLSNlLEWIPGtenwpHFVRNNSERFEARVASVRVGESPSIMLRGM-AGSRLPVAVAHGEG 1215

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698401979  146 N-YYCDEETLKKLKENNQIVFTYAGE----------NPNGSLENIAGIVNERGNVLGMMPHPERAVDA 202
Cdd:TIGR01735 1216 YaAFSSPELQAQADASGLAALRYIDDdgnpteayplNPNGSPGGIAGITSCDGRVTIMMPHPERVFRA 1283
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
 2-199 7.48e-21

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 90.60  E-value: 7.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979    2 KFAVLVFPGSNCDVDMYHAIKDELGEEVEFVWHDATD----LSGFDAILIPGGFSYGDYLRCGAMASQS-----NVMKAV 72
Cdd:PLN03206  1039 KVAIIREEGSNGDREMAAAFYAAGFEPWDVTMSDLLNgrisLDDFRGIVFVGGFSYADVLDSAKGWAGSirfnePLLQQF 1118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   73 KEAAEEGKPI-LGVCNGFQILTEAGLLPGA----------------LLRNKNLKFICRTVPLKVENNQT-MFTNQydQGQ 134
Cdd:PLN03206  1119 QEFYNRPDTFsLGVCNGCQLMALLGWVPGPqvggglgaggdpsqprFVHNESGRFECRFTSVTIEDSPAiMLKGM--EGS 1196

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698401979  135 IIHIPIAHGEGN-YYCDEETLKKLKENNQIVFTY---AGE-------NPNGSLENIAGIVNERGNVLGMMPHPERA 199
Cdd:PLN03206  1197 TLGVWAAHGEGRaYFPDESVLDEVLKSNLAPVRYcddDGEpteqypfNPNGSPLGIAALCSPDGRHLAMMPHPERC 1272
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-92 6.65e-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: 71.09  E-value: 6.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   4 AVLVFPGSNC-DVDMYHAIKDELGEEVEFVWHD------ATDLSGFDAILIPGGFSYGDylrcgAMASQSNVMKAVKEAA 76
Cdd:cd01653     2 AVLLFPGFEElELASPLDALREAGAEVDVVSPDggpvesDVDLDDYDGLILPGGPGTPD-----DLARDEALLALLREAA 76

                          90
                  ....*....|....*.
gi 1698401979  77 EEGKPILGVCNGFQIL 92
Cdd:cd01653    77 AAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-92 2.25e-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: 68.77  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   4 AVLVFPGSNC-DVDMYHAIKDELGEEVEFVWHD------ATDLSGFDAILIPGGFSYGDylrcgAMASQSNVMKAVKEAA 76
Cdd:cd03128     2 AVLLFGGSEElELASPLDALREAGAEVDVVSPDggpvesDVDLDDYDGLILPGGPGTPD-----DLAWDEALLALLREAA 76

                          90
                  ....*....|....*.
gi 1698401979  77 EEGKPILGVCNGFQIL 92
Cdd:cd03128    77 AAGKPVLGICLGAQLL 92
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 23-220 2.70e-13

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 65.92  E-value: 2.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  23 DELGEEVeFVWHDATDLSGFDAILIPGGFSYGDylrcgAMAS--QSNVMKAVKEAAEEGKPILGVCNGFQILTEA----- 95
Cdd:PRK13141   20 ERLGAEA-VITSDPEEILAADGVILPGVGAFPD-----AMANlrERGLDEVIKEAVASGKPLLGICLGMQLLFESseefg 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  96 -----GLLPGALLR---NKNLKficrtVP------LKVENNQTMFTNqydqgqiihIPiahgEGN-------YYCDeetl 154
Cdd:PRK13141   94 eteglGLLPGRVRRfppEEGLK-----VPhmgwnqLELKKESPLLKG---------IP----DGAyvyfvhsYYAD---- 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698401979 155 kklKENNQIVFTYA--GenpngslENIAGIVnERGNVLGMMPHPERavdallgSAD-GLAL---FKSIVKQW 220
Cdd:PRK13141  152 ---PCDEEYVAATTdyG-------VEFPAAV-GKDNVFGAQFHPEK-------SGDvGLKIlknFVEMVEEC 205
GATase pfam00117
Glutamine amidotransferase class-I;
24-197 1.04e-12

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 64.18  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  24 ELGEEVEFVWHDATDLS----GFDAILIPGGFsyGDYLRCGamasqsNVMKAVKEAAEEGKPILGVCNGFQILTEAglLP 99
Cdd:pfam00117  19 ELGVEVTVVPNDTPAEEileeNPDGIILSGGP--GSPGAAG------GAIEAIREARELKIPILGICLGHQLLALA--FG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 100 GALLRNKNLKFICRTVPLKvENNQTMFtnqYDQGQIIHIPIAHGegnYYCDEETLKKlkennqiVFTYAGENPNGslENI 179
Cdd:pfam00117  89 GKVVKAKKFGHHGKNSPVG-DDGCGLF---YGLPNVFIVRRYHS---YAVDPDTLPD-------GLEVTATSEND--GTI 152

                         170
                  ....*....|....*...
gi 1698401979 180 AGIVNERGNVLGMMPHPE 197
Cdd:pfam00117 153 MGIRHKKLPIFGVQFHPE 170
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 23-214 6.19e-11

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: 59.43  E-value: 6.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  23 DELGEEVEFVwHDATDLSGFDAILIPGGFSYGDylrcgAMAS--QSNVMKAVKEAAEEGKPILGVCNGFQILTEA----- 95
Cdd:cd01748    19 ERLGAEVIIT-SDPEEILSADKLILPGVGAFGD-----AMANlrERGLIEALKEAIASGKPFLGICLGMQLLFESseegg 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  96 -----GLLPGALLRnknlkfICRTVPLKVEN---NQTMFTNQydqgqiihIPIAHGEGN---------YYCDEEtlkklk 158
Cdd:cd01748    93 gtkglGLIPGKVVR------FPASEGLKVPHmgwNQLEITKE--------SPLFKGIPDgsyfyfvhsYYAPPD------ 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698401979 159 ENNQIVFT--YAGEnpngslenIAGIVnERGNVLGMMPHPERAvdallgSADGLALFK 214
Cdd:cd01748   153 DPDYILATtdYGGK--------FPAAV-EKDNIFGTQFHPEKS------GKAGLKLLK 195
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 42-100 4.06e-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: 56.40  E-value: 4.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1698401979  42 FDAILIPGGFSyGDYLRCGAmasqsNVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:cd03134    63 YDALVIPGGTN-PDKLRRDP-----DAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRG 115
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 40-100 4.32e-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: 56.50  E-value: 4.32e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698401979  40 SGFDAILIPGGFSYGDYLRCGAMasqsnVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:pfam01965  60 DDYDALVLPGGRAGPERLRDNEK-----LVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKG 115
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 16-91 9.50e-10

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: 56.79  E-value: 9.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  16 DMYHAIKD-------ELGEEVEFVWHDATD---------LSGFDAILIPGGFSY-GdylrcgamasQSNVMKAVKEAAEE 78
Cdd:cd01746    14 DAYLSVLEalkhagiALGVKLEIKWIDSEDleeenaeeaLKGADGILVPGGFGIrG----------VEGKILAIKYAREN 83

                          90
                  ....*....|...
gi 1698401979  79 GKPILGVCNGFQI 91
Cdd:cd01746    84 NIPFLGICLGMQL 96
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 35-100 1.09e-09

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: 55.49  E-value: 1.09e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698401979  35 DATDLSGFDAILIPGGFSYGDYLRcgamASQsNVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:COG0693    58 DDVDPDDYDALVLPGGHGAPDDLR----EDP-DVVALVREFYEAGKPVAAICHGPAVLAAAGLLKG 118
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 19-100 1.48e-09

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: 55.35  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  19 HAIKDELGEE--VEFVWH--------DATDLSGFDAILIPGGFSyGDYLRCGAmasqsNVMKAVKEAAEEGKPILGVCNG 88
Cdd:cd03169    44 TAIHDFPGWQtyTEKPGHrfavtadfDEVDPDDYDALVIPGGRA-PEYLRLDE-----KVLAIVRHFAEANKPVAAICHG 117

                          90
                  ....*....|..
gi 1698401979  89 FQILTEAGLLPG 100
Cdd:cd03169   118 PQILAAAGVLKG 129
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 4-92 5.06e-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: 54.17  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   4 AVLVFP-GSNcdVDMYHAIKDELGEEVEFVwHDATDLSGFDAILIPGGFSYG---DYLRCGAMAsqsnvmKAVKEAAEEG 79
Cdd:cd01750     2 AVIRYPdISN--FTDLDPLAREPGVDVRYV-EVPEGLGDADLIILPGSKDTIqdlAWLRKRGLA------EAIKNYARAG 72

                          90
                  ....*....|...
gi 1698401979  80 KPILGVCNGFQIL 92
Cdd:cd01750    73 GPVLGICGGYQML 85
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 25-109 5.29e-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: 5.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  25 LGEEVEfVWHDATDLSGFDAILIPG-GfSYGDylrcgAMAS--QSNVMKAVKEAAEEGKPILGVCNGFQILTEA------ 95
Cdd:COG0118    23 LGAEVV-VTSDPDEIRAADRLVLPGvG-AFGD-----AMENlrERGLDEAIREAVAGGKPVLGICLGMQLLFERseengd 95

                          90       100
                  ....*....|....*....|
gi 1698401979  96 ----GLLPGA--LLRNKNLK 109
Cdd:COG0118    96 teglGLIPGEvvRFPASDLK 115
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 35-100 2.58e-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: 51.65  E-value: 2.58e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698401979  35 DATDLSGFDAILIPGGFSyGDYLRcgamaSQSNVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:TIGR01382  54 DEVNPEEYDALVIPGGRA-PEYLR-----LNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRG 113
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
14-94 4.71e-08

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 51.09  E-value: 4.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  14 DVDMYHAIKDELGEEVEFvwHDATDLSGFDAILIPGGFSYGDYLRcgamASQSNVM-KAVKEAAEEGKPILGVCNGFQIL 92
Cdd:pfam07685  17 NLDPLRYEPAVRVRFVPL--PDESLGPDADLIILPGGKPTIQDLA----LLRNSGMdEAIKEAAEDGGPVLGICGGYQML 90


                  ..
gi 1698401979  93 TE 94
Cdd:pfam07685  91 GE 92
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-88 5.52e-08

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 51.04  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGsncDV-DMYHAIK---DELGEEVEFVW-HDATDLSGFDAILIPGGFSygdyLRCGAMASQSNVMKAVKEA 75
Cdd:PRK13527    1 MKIGVLALQG---DVeEHIDALKralDELGIDGEVVEvRRPGDLPDCDALIIPGGES----TTIGRLMKREGILDEIKEK 73

                          90
                  ....*....|...
gi 1698401979  76 AEEGKPILGVCNG 88
Cdd:PRK13527   74 IEEGLPILGTCAG 86
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 35-218 6.94e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 51.02  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  35 DATDLSGFDAILIPGGFSYGDylrcgAMAS--QSNVMKAVKEAAEEGKPILGVCNGFQILTEA---------GLLPGALL 103
Cdd:PRK13181   31 DPEEIAGADKVILPGVGAFGQ-----AMRSlrESGLDEALKEHVEKKQPVLGICLGMQLLFESseegnvkglGLIPGDVK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 104 RnknLKFICRTVP------LKVENNQTMFTNQYDQGqiiHIPIAHgegNYYCDEEtlkklKENNQIVFTYAGENPNGSLe 177
Cdd:PRK13181  106 R---FRSEPLKVPqmgwnsVKPLKESPLFKGIEEGS---YFYFVH---SYYVPCE-----DPEDVLATTEYGVPFCSAV- 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1698401979 178 niagivnERGNVLGMMPHPERAVDAllgsadGLALFKSIVK 218
Cdd:PRK13181  171 -------AKDNIYAVQFHPEKSGKA------GLKLLKNFAE 198
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 4-92 1.02e-07

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: 51.60  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   4 AVLVFPG-SN-CDVDmyhAIKDELGEEVEFVwHDATDLSGFDAILIPGgfS---YGD--YLRcgamasQSNVMKAVKEAA 76
Cdd:COG1492   255 AVIRLPRiSNfTDFD---PLAAEPGVRLRYV-RPPEELGDADLVILPG--SkntIADlaWLR------ESGLDDAIRAHA 322

                          90
                  ....*....|....*.
gi 1698401979  77 EEGKPILGVCNGFQIL 92
Cdd:COG1492   323 RRGGPVLGICGGYQML 338
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 20-88 1.98e-07

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: 49.45  E-value: 1.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698401979  20 AIKDELGEEVEFVWhDATDLSGFDAILIPGGFSygdylrcGAM---ASQSNVMKAVKEAAEEGKPILGVCNG 88
Cdd:cd01749    15 RALERLGVEVIEVR-TPEDLEGIDGLIIPGGES-------TTIgklLRRTGLLDPLREFIRAGKPVFGTCAG 78
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 26-222 1.98e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 49.48  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  26 GEEVEFVwHDATDLSGFDAILIPGGFSYGDylrcgAMASQSNVMKAVKEAAEEGKPILGVCNGFQIL----TEAGLLPG- 100
Cdd:PRK13143   24 GAEVVIT-SDPEEILDADGIVLPGVGAFGA-----AMENLSPLRDVILEAARSGKPFLGICLGMQLLfessEEGGGVRGl 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 101 ALLRNKNLKFI-CRTVP------LKVENNQtmftnqydqgqiihiPIAHG-EGNYYcdeetlkklkennQIVFTYaGENP 172
Cdd:PRK13143   98 GLFPGRVVRFPaGVKVPhmgwntVKVVKDC---------------PLFEGiDGEYV-------------YFVHSY-YAYP 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1698401979 173 NgSLENIAGIVN---------ERGNVLGMMPHPERAvdallgSADGLALFKSIVKQWRE 222
Cdd:PRK13143  149 D-DEDYVVATTDygiefpaavCNDNVFGTQFHPEKS------GETGLKILENFVELIKR 200
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 18-95 6.54e-07

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: 48.11  E-value: 6.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  18 YHAIKdELGEEVEFVWHDATDLS-----GFDAILI---PGGfsygdylrcgamASQSNVMKAVKEAAEEGKPILGVCNGF 89
Cdd:COG0512    15 VQYLG-ELGAEVVVVRNDEITLEeiealAPDGIVLspgPGT------------PEEAGISLEVIRAFAGKIPILGVCLGH 81


                  ....*.
gi 1698401979  90 QILTEA 95
Cdd:COG0512    82 QAIGEA 87
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 35-100 1.24e-06

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: 46.78  E-value: 1.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698401979  35 DATDLSGFDAILIPGGFSYGDYLRcgamASQsNVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:cd03135    54 SDVNLDDYDAIVIPGGLPGAQNLA----DNE-KLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKG 114
PRK06186 PRK06186
hypothetical protein; Validated
 12-90 1.54e-06

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 47.27  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  12 NCDVDMYHAI-------KDELGEEVEFVW------HDATDLSGFDAI-LIPGGfSYgdylrcgamASQSNVMKAVKEAAE 77
Cdd:PRK06186   11 NPDVTAHQAIplaldlaAAVLGLPVDYEWlptpeiTDPEDLAGFDGIwCVPGS-PY---------RNDDGALTAIRFARE 80

                          90
                  ....*....|...
gi 1698401979  78 EGKPILGVCNGFQ 90
Cdd:PRK06186   81 NGIPFLGTCGGFQ 93
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 29-217 1.83e-06

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: 46.93  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  29 VEFVWHDATDLSGFDAILIPGGFSYGDylrcgAMA--SQSNVMKAVKEAAEEGKPILGVCNGFQIL----TEAGLLPG-A 101
Cdd:TIGR01855  24 EPVVVKDSKEAELADKLILPGVGAFGA-----AMArlRENGLDLFVELVVRLGKPVLGICLGMQLLfersEEGGGVPGlG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 102 LLRNKNLKFICRTVP------LKVENNQTMFTNQYDQGQI--IHipiahgegNYYCdeetlkKLKENNQIVFTYAGenpn 173
Cdd:TIGR01855  99 LIKGNVVKLEARKVPhmgwneVHPVKESPLLNGIDEGAYFyfVH--------SYYA------VCEEEAVLAYADYG---- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1698401979 174 gslENIAGIVnERGNVLGMMPHPERAVDAllgsadGLALFKSIV 217
Cdd:TIGR01855 161 ---EKFPAAV-QKGNIFGTQFHPEKSGKT------GLKLLENFL 194
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
24-100 8.79e-06

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 45.89  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  24 ELGEEVEFV--WHDATdLSGFDAILIPGGFSYgdyLRCGAMASQSNVMKAVKEAAEEGKPILGVCNGFQILTE------- 94
Cdd:PRK01077  269 AAGAELVFFspLADEA-LPDCDGLYLGGGYPE---LFAAELAANTSMRASIRAAAAAGKPIYAECGGLMYLGEsledadg 344

                          90
                  ....*....|.
gi 1698401979  95 -----AGLLPG 100
Cdd:PRK01077  345 erhpmVGLLPG 355
pyrG PRK05380
CTP synthetase; Validated
 28-91 9.43e-06

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 45.78  E-value: 9.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698401979  28 EVEFVWHDATD---------LSGFDAILIPGGFsyGDylRcGAmasqSNVMKAVKEAAEEGKPILGVCNGFQI 91
Cdd:PRK05380  321 KVNIKWIDSEDleeenvaelLKGVDGILVPGGF--GE--R-GI----EGKILAIRYARENNIPFLGICLGMQL 384
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 14-95 1.05e-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: 44.54  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  14 DVDMYHAIKDELGEevefvwhdatDLSGFDAILIPGGFSygdylrcGAMASQSNVMKAVKE----AAEEGKPILGVCNGF 89
Cdd:cd01741    29 EIDVVDVYAGELLP----------DLDDYDGLVILGGPM-------SVDEDDYPWLKKLKElirqALAAGKPVLGICLGH 91


                  ....*.
gi 1698401979  90 QILTEA 95
Cdd:cd01741    92 QLLARA 97
PRK00784 PRK00784
cobyric acid synthase;
4-92 1.23e-05

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 45.46  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   4 AVLVFPG-SN-CDVDmyhAIKDELGEEVEFVwHDATDLSGFDAILIPGgfS---YGD--YLRCGAMAsqsnvmKAVKEAA 76
Cdd:PRK00784  255 AVIRLPRiSNfTDFD---PLRAEPGVDVRYV-RPGEPLPDADLVILPG--SkntIADlaWLRESGWD------EAIRAHA 322

                          90
                  ....*....|....*.
gi 1698401979  77 EEGKPILGVCNGFQIL 92
Cdd:PRK00784  323 RRGGPVLGICGGYQML 338
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 28-91 2.10e-05

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: 44.61  E-value: 2.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698401979  28 EVEFVWHDATD---------LSGFDAILIPGGFsyGDylRcGA--MasqsnvMKAVKEAAEEGKPILGVCNGFQI 91
Cdd:COG0504   322 KVNIKWIDSEDleeenaeelLKGVDGILVPGGF--GE--R-GIegK------IAAIRYARENKIPFLGICLGMQL 385
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 43-101 4.24e-05

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: 42.97  E-value: 4.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698401979  43 DAILIPGGFSYgdyLRCGAMASQSNVMKAVKEAAEEGKPILGVCNGFQILTE------------AGLLPGA 101
Cdd:cd03130    42 DGLYLGGGYPE---LFAEELSANQSMRESIRAFAESGGPIYAECGGLMYLGEslddeegqsypmAGVLPGD 109
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 14-95 7.12e-05

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: 42.63  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  14 DVDMYHAIKDELgeevefvWHDATDLSGFDAILIPGG----FSYGDYLRcgamasqsNVMKAVKEAAEEGKPILGVCNGF 89
Cdd:COG0518    28 ELDVLRVYAGEI-------LPYDPDLEDPDGLILSGGpmsvYDEDPWLE--------DEPALIREAFELGKPVLGICYGA 92


                  ....*.
gi 1698401979  90 QILTEA 95
Cdd:COG0518    93 QLLAHA 98
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 34-92 7.74e-05

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


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 42.47  E-value: 7.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698401979  34 HDATDLSGFDAILIPGGfsygdylrcgAMASQSNVM-------KAVKEAAEEGKPILGVCNGFQIL 92
Cdd:COG3442    43 GDDLPFDDVDIVFIGGG----------QDREQEIVAddllrikDALRAAIEDGVPVLAICGGYQLL 98
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 32-98 8.42e-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: 42.45  E-value: 8.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698401979  32 VWHDATDLSGFDAILIPGGFSYgdylrcgAMASQSNVMKAVKEAAEEGKPILGVCNGFQILTEAGLL 98
Cdd:COG4977    57 PDHGLADLAAADTLIVPGGLDP-------AAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLL 116
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 36-92 8.46e-05

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: 42.08  E-value: 8.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698401979  36 ATDLSGFDAILIPGG-----FSYGD--YLRCGAM-----ASQsnvMKAVKEAAEEGKPILGVCNGFQIL 92
Cdd:COG2071    44 DELLDRLDGLVLTGGadvdpALYGEepHPELGPIdperdAFE---LALIRAALERGKPVLGICRGMQLL 109
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 42-197 1.04e-04

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 41.33  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  42 FDAILIPGGfsYGDYLRCgamasqSNVMKAVKEAAEEGKPILGVCNGFQILteaGLLPGAllrnknlkficRTVPLKVEN 121
Cdd:cd01744    40 PDGIFLSNG--PGDPALL------DEAIKTVRKLLGKKIPIFGICLGHQLL---ALALGA-----------KTYKMKFGH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 122 ---NQTM---FTNQydqgqiIHIpIAHGEGnYYCDEETLKKlkennQIVFTYagENPN-GSLEniaGIVNERGNVLGMMP 194
Cdd:cd01744    98 rgsNHPVkdlITGR------VYI-TSQNHG-YAVDPDSLPG-----GLEVTH--VNLNdGTVE---GIRHKDLPVFSVQF 159


                  ...
gi 1698401979 195 HPE 197
Cdd:cd01744   160 HPE 162
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 3-100 1.74e-04

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: 40.99  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   3 FAVLVFPGsncdVDM----------YHAIKDELGEEVEFVW-----------------HDATDLSGFDAILIPGGfsYGD 55
Cdd:cd03139     1 VGILLFPG----VEVldvigpyevfGRAPRLAAPFEVFLVSetggpvssrsgltvlpdTSFADPPDLDVLLVPGG--GGT 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1698401979  56 YlrcgAMASQSNVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:cd03139    75 R----ALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDG 115
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 39-95 2.04e-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: 40.64  E-value: 2.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698401979  39 LSGFDAILIPGGFSYGDYLRcGAMASQSNV----------MKAVKEAAEEGKPILGVCNGFQILTEA 95
Cdd:cd01745    51 LELLDGLLLTGGGDVDPPLY-GEEPHPELGpidperdafeLALLRAALERGKPILGICRGMQLLNVA 116
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 39-92 2.19e-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: 41.09  E-value: 2.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698401979  39 LSGFDAILIPGGFSYgDYLRCGAMASQSN----------VMKAVKEAAEEGKPILGVCNGFQIL 92
Cdd:pfam07722  56 LDRLDGLLLTGGPNV-DPHFYGEEPSESGgpydpardayELALIRAALARGKPILGICRGFQLL 118
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 24-95 2.94e-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: 40.21  E-value: 2.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698401979  24 ELGEEVEFVWHDATDLS-----GFDAILI-PGgfsYGDylrcgamASQSNVMKAVKEAAEEGKPILGVCNGFQILTEA 95
Cdd:cd01743    20 ELGAEVVVVRNDEITLEelellNPDAIVIsPG---PGH-------PEDAGISLEIIRALAGKVPILGVCLGHQAIAEA 87
PRK06278 PRK06278
cobyrinic acid a,c-diamide synthase; Validated
 43-195 5.19e-04

cobyrinic acid a,c-diamide synthase; Validated


Pssm-ID: 180505 [Multi-domain]  Cd Length: 476  Bit Score: 40.40  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  43 DAILIPGGfsygDYLRCGAMasqSNVMKavKEAAEEGKPILGVCNGFQILTEA----------------GLLpgallrNK 106
Cdd:PRK06278   38 DGLIIPGG----SLVESGSL---TDELK--KEILNFDGYIIGICSGFQILSEKidigrkspvpiikeglGLL------DV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 107 NLK-FICRT-VPLKVENNqTMFTNQYDQGQIIHipiAHGEGNYYCDEETLKKLKEN-NQIVFTYAGENpngslENIAGIV 183
Cdd:PRK06278  103 EFSpLICTDrVEFKIEDD-SLFTKKNERGTGFH---CHTYGNIEINGDTKILTYSKiQKLNYKMVGEK-----EILSGVF 173

                         170
                  ....*....|..
gi 1698401979 184 neRGNVLGMMPH 195
Cdd:PRK06278  174 --KGKVFGTMVH 183
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 26-97 5.50e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 39.77  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  26 GEEVEfVWHDATDLSGFDAILIPGgfsygdylrCGAMASqsnVMK---------AVKEAAEE-GKPILGVCNGFQILTEA 95
Cdd:PRK13146   27 GADVV-VTADPDAVAAADRVVLPG---------VGAFAD---CMRglravglgeAVIEAVLAaGRPFLGICVGMQLLFER 93


                  ..
gi 1698401979  96 GL 97
Cdd:PRK13146   94 GL 95
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-88 5.51e-04

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 39.37  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979   1 MKFAVLVFPGsncDVDMYHAIKDELGEEVEFVWHdATDLSGFDAILIPGGFSygdylrcGAM---ASQSNVMKAVKEAAE 77
Cdd:PRK13525    2 MKIGVLALQG---AVREHLAALEALGAEAVEVRR-PEDLDEIDGLILPGGES-------TTMgklLRDFGLLEPLREFIA 70

                          90
                  ....*....|.
gi 1698401979  78 EGKPILGVCNG 88
Cdd:PRK13525   71 SGLPVFGTCAG 81
PLN02327 PLN02327
CTP synthase
 39-91 8.15e-04

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 40.01  E-value: 8.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1698401979  39 LSGFDAILIPGGFsygdylrcGAMASQSNVMkAVKEAAEEGKPILGVCNGFQI 91
Cdd:PLN02327  360 LKGADGILVPGGF--------GDRGVEGKIL-AAKYARENKVPYLGICLGMQI 403
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
42-86 9.15e-04

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 39.00  E-value: 9.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1698401979  42 FDAILIPGGF----SYGDYLRCGAMAS-QSNVMKAVKEAAEEGKPILGVC 86
Cdd:PRK11780   86 FDALIVPGGFgaakNLSNFAVKGAECTvNPDVKALVRAFHQAGKPIGFIC 135
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 34-100 1.18e-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: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 38.64  E-value: 1.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698401979  34 HDATDLSGFDAILIPGGFSYGdylrcgAMASQSNVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:cd03137    57 AGLDALAAADTVIVPGGPDVD------GRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDG 117
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 38-131 1.81e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.


Pssm-ID: 153235 [Multi-domain]  Cd Length: 221  Bit Score: 38.31  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  38 DLSGFDAILIPGGFsygdylrcGAM---ASQSNVMKAVKEAAEEGKPILGVCNGfqilteagllPGALL--RNKNLKFIC 112
Cdd:cd03141    87 DPSDYDAIFIPGGH--------GPMfdlPDNPDLQDLLREFYENGKVVAAVCHG----------PAALLnvKLSDGKSLV 148

                          90       100
                  ....*....|....*....|.
gi 1698401979 113 --RTVplkvennqTMFTNQYD 131
Cdd:cd03141   149 agKTV--------TGFTNEEE 161
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 26-100 2.26e-03

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: 37.57  E-value: 2.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698401979  26 GEEVEfVWHDATDLSGFDAILIPGGFSygdylrcGAMASQSNVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:cd03136    50 GLRVA-PDAALEDAPPLDYLFVVGGLG-------ARRAVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDG 116
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 20-104 2.84e-03

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 38.15  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  20 AIKdELGEEVEFVwHDATDLSGFDAILIPGGFSYG---DYLRCGAMAsqsnvmKAVKEAAEEGKPILGVCNGFQILTEA- 95
Cdd:PLN02617   25 AIR-HLGFTIKDV-QTPEDILNADRLIFPGVGAFGsamDVLNNRGMA------EALREYIQNDRPFLGICLGLQLLFESs 96

                          90
                  ....*....|....*...
gi 1698401979  96 ---------GLLPGALLR 104
Cdd:PLN02617   97 eengpveglGVIPGVVGR 114
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 32-100 3.26e-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: 37.24  E-value: 3.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698401979  32 VWHDATDLSGFDAILIPGgFSYGDylRCGAMASQSNVMKAVKEAAEEGKPILGVCNGFQILTEAGLLPG 100
Cdd:cd03138    60 PDATLADVPAPDLVIVPG-LGGDP--DELLLADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDG 125
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 36-219 3.53e-03

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 37.17  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979  36 ATDLSGFDAILIPGGFSYGDYLRcgaMASQSNVMKAVKEAAEEGKPILGVCNGFQIL---TEAGLLPGALLRNKNLKFIC 112
Cdd:CHL00188   34 ESELAQVHALVLPGVGSFDLAMK---KLEKKGLITPIKKWIAEGNPFIGICLGLHLLfetSEEGKEEGLGIYKGQVKRLK 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698401979 113 RTVPLKVEN---NQTMFTNQYDQGQIIHI-------PIAHGEGNYYcdeetlkkLKENNQIVFTYAgeNPNGSLENIAGI 182
Cdd:CHL00188  111 HSPVKVIPHmgwNRLECQNSECQNSEWVNwkawplnPWAYFVHSYG--------VMPKSQACATTT--TFYGKQQMVAAI 180

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1698401979 183 vnERGNVLGMMPHPERAvdallgSADGLALFKSIVKQ 219
Cdd:CHL00188  181 --EYDNIFAMQFHPEKS------GEFGLWLLREFMKK 209
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 30-95 7.45e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 36.42  E-value: 7.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698401979  30 EFVW-HDATDLSGFDAILIPGGfsyGDYLRCGAMASQSNVMKAVKEAAEEGKPILGVCNGFQILTEA 95
Cdd:PRK14004   25 DFVFtSDPETIENSKALILPGD---GHFDKAMENLNSTGLRSTIDKHVESGKPLFGICIGFQILFES 88
 
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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