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Conserved domains on  [gi|1082558936|gb|OFY92418|]
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phosphoribosylformylglycinamidine synthase I [Bacteroidetes bacterium RIFOXYA2_FULL_33_7]

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;
1-227 1.42e-141

phosphoribosylformylglycinamidine synthase subunit PurQ;


:

Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 394.48  E-value: 1.42e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   1 MKFGVVIFPGSNCDEDMIYVLESVMEQEVVRLWHKDTDLQHVDGIFLPGGFSFGDYLRSGAIAKFSPIMKSVIEFANKGG 80
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  81 FVFGVCNGFQVLCESGLLPGALLHNDNQKFICKNIFIKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVETLKNMRLN 160
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082558936 161 KQILFRYCNEdgsinlesNPNGSVENIAGVCNEKRNVYGMMPHPERASDDELGNTDGRIIFESILKS 227
Cdd:PRK03619  161 GQVVFRYCDE--------NPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-227 1.42e-141

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 394.48  E-value: 1.42e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   1 MKFGVVIFPGSNCDEDMIYVLESVMEQEVVRLWHKDTDLQHVDGIFLPGGFSFGDYLRSGAIAKFSPIMKSVIEFANKGG 80
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  81 FVFGVCNGFQVLCESGLLPGALLHNDNQKFICKNIFIKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVETLKNMRLN 160
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082558936 161 KQILFRYCNEdgsinlesNPNGSVENIAGVCNEKRNVYGMMPHPERASDDELGNTDGRIIFESILKS 227
Cdd:PRK03619  161 GQVVFRYCDE--------NPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-228 7.38e-128

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: 360.53  E-value: 7.38e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   1 MKFGVVIFPGSNCDEDMIYVLESVmEQEVVRLWHKD--TDLQHVDGIFLPGGFSFGDYLRSGAIAKFSPIMKSVIEFANK 78
Cdd:COG0047     1 PKVAILVFPGSNCDRDMAAAFERA-GAEAEDVWHSDlrTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  79 GGFVFGVCNGFQVLCESGLLPG---ALLHNDNQKFICKNIFIKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVETLK 155
Cdd:COG0047    80 GGLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082558936 156 NMRLNKQILFRYCNEDGSINLESNPNGSVENIAGVCNEKRNVYGMMPHPERASDDELG---NTDGRIIFESILKSF 228
Cdd:COG0047   160 ELEANGQVAFRYVDADGNVTYPANPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGpgeSTDGLRIFRSAVKYF 235
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-227 1.88e-118

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: 336.66  E-value: 1.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   1 MKFGVVIFPGSNCDEDMIYVLESvMEQEVVRLWHKDTDLQHVDGIFLPGGFSFGDYLRSGAIAKFSPIMKSVIEFANKGG 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALRL-LGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  81 FVFGVCNGFQVLCESGLLPGALLHNDNQKFICKNIFIKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVETLKNMRLN 160
Cdd:TIGR01737  80 PVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082558936 161 KQILFRYCNEDGSINLESNPNGSVENIAGVCNEKRNVYGMMPHPERASDDELGNTDGRIIFESILKS 227
Cdd:TIGR01737 160 DQVVFRYCDEDGDVAEEANPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVEW 226
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-225 6.53e-101

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: 292.60  E-value: 6.53e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   3 FGVVIFPGSNCDEDMIYVLESVMeQEVVRLWHKDT-----DLQHVDGIFLPGGFSFGDYLRSGAIAKFSP-IMKSVIEFA 76
Cdd:cd01740     1 VAVLRFPGSNCDRDMAYAFELAG-FEAEDVWHNDLlagrkDLDDYDGVVLPGGFSYGDYLRAGAIAAASPlLMEEVKEFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  77 NKGGFVFGVCNGFQVLCESGLLPGALLHNDNQKFICKNIF----IKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVE 152
Cdd:cd01740    80 ERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQNrfvtLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082558936 153 TLKNMRLNKQIL-FRYCNEDGSINLESNPNGSVENIAGVCNEKRNVYGMMPHPERASD-----DELGNTDGRIIFESIL 225
Cdd:cd01740   160 TLAELEENGQIAqYVDDDGNVTERYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEpwqweRLLGGSDGLKLFRNAV 238
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 5-209 7.86e-50

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: 163.44  E-value: 7.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   5 VVIFPGSNCDEDMIYVLESV-MEQEVV---RLWHKDTDLQHVDGIFLPGGFSFGDYLRSG-AIAKF----SPIMKSVIEF 75
Cdd:pfam13507   6 ILREPGTNGEYEMAAAFERAgFDAVDVhmsDLLSGRVSLDDFQGLAAPGGFSYGDVLGSGkGWAASilfnPKLRDAFEAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  76 -ANKGGFVFGVCNGFQVLCESGLLPG----------ALLHNDNQKFICK--NIFIKPDNNTSALTNLipekATLKIPIAH 142
Cdd:pfam13507  86 fNRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRwvNVKISEKSPSVFLRGM----DGSGLPVAH 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936 143 GEGR-YYADVETLKNMRLNKQILFRYCNEDGSINLES--NPNGSVENIAGVCNEKRNVYGMMPHPERASD 209
Cdd:pfam13507 162 GEGRfVFRSEEVLARLEANGQVALRYVDNAGNPTEEYpfNPNGSPLGIAGICSPDGRVLGLMPHPERVFR 231
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-227 1.42e-141

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 394.48  E-value: 1.42e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   1 MKFGVVIFPGSNCDEDMIYVLESVMEQEVVRLWHKDTDLQHVDGIFLPGGFSFGDYLRSGAIAKFSPIMKSVIEFANKGG 80
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  81 FVFGVCNGFQVLCESGLLPGALLHNDNQKFICKNIFIKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVETLKNMRLN 160
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082558936 161 KQILFRYCNEdgsinlesNPNGSVENIAGVCNEKRNVYGMMPHPERASDDELGNTDGRIIFESILKS 227
Cdd:PRK03619  161 GQVVFRYCDE--------NPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLKS 219
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-228 7.38e-128

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: 360.53  E-value: 7.38e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   1 MKFGVVIFPGSNCDEDMIYVLESVmEQEVVRLWHKD--TDLQHVDGIFLPGGFSFGDYLRSGAIAKFSPIMKSVIEFANK 78
Cdd:COG0047     1 PKVAILVFPGSNCDRDMAAAFERA-GAEAEDVWHSDlrTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  79 GGFVFGVCNGFQVLCESGLLPG---ALLHNDNQKFICKNIFIKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVETLK 155
Cdd:COG0047    80 GGLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082558936 156 NMRLNKQILFRYCNEDGSINLESNPNGSVENIAGVCNEKRNVYGMMPHPERASDDELG---NTDGRIIFESILKSF 228
Cdd:COG0047   160 ELEANGQVAFRYVDADGNVTYPANPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGpgeSTDGLRIFRSAVKYF 235
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-227 1.88e-118

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: 336.66  E-value: 1.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   1 MKFGVVIFPGSNCDEDMIYVLESvMEQEVVRLWHKDTDLQHVDGIFLPGGFSFGDYLRSGAIAKFSPIMKSVIEFANKGG 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALRL-LGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  81 FVFGVCNGFQVLCESGLLPGALLHNDNQKFICKNIFIKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVETLKNMRLN 160
Cdd:TIGR01737  80 PVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082558936 161 KQILFRYCNEDGSINLESNPNGSVENIAGVCNEKRNVYGMMPHPERASDDELGNTDGRIIFESILKS 227
Cdd:TIGR01737 160 DQVVFRYCDEDGDVAEEANPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVEW 226
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-225 6.53e-101

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: 292.60  E-value: 6.53e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   3 FGVVIFPGSNCDEDMIYVLESVMeQEVVRLWHKDT-----DLQHVDGIFLPGGFSFGDYLRSGAIAKFSP-IMKSVIEFA 76
Cdd:cd01740     1 VAVLRFPGSNCDRDMAYAFELAG-FEAEDVWHNDLlagrkDLDDYDGVVLPGGFSYGDYLRAGAIAAASPlLMEEVKEFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  77 NKGGFVFGVCNGFQVLCESGLLPGALLHNDNQKFICKNIF----IKPDNNTSALTNLIPEKATLKIPIAHGEGRYYADVE 152
Cdd:cd01740    80 ERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQNrfvtLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082558936 153 TLKNMRLNKQIL-FRYCNEDGSINLESNPNGSVENIAGVCNEKRNVYGMMPHPERASD-----DELGNTDGRIIFESIL 225
Cdd:cd01740   160 TLAELEENGQIAqYVDDDGNVTERYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEpwqweRLLGGSDGLKLFRNAV 238
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 1-227 8.50e-62

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 193.82  E-value: 8.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   1 MKFGVVIFPGSNCDEDMIYVL-ESVMEQEVVRLwhKDTD-----LQHVDGIFLPGGFSFGDYLRSGAI--AKFSPI-MKS 71
Cdd:PRK01175    4 IRVAVLRMEGTNCEDETVKAFrRLGVEPEYVHI--NDLAaerksVSDYDCLVIPGGFSAGDYIRAGAIfaARLKAVlRKD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  72 VIEFANKGGFVFGVCNGFQVLCESGLLPG----------ALLHNDNQKFICKNIFIKPDNNTSALTNLIpEKATLKIPIA 141
Cdd:PRK01175   82 IEEFIDEGYPIIGICNGFQVLVELGLLPGfdeiaekpemALTVNESNRFECRPTYLKKENRKCIFTKLL-KKDVFQVPVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936 142 HGEGR-YYADVETLKNMRLNKQILFRYCNEDGSI-NLESNPNGSVENIAGVCNEKRNVYGMMPHPERA--------SDDE 211
Cdd:PRK01175  161 HAEGRvVFSEEEILERLIENDQIVFRYVDENGNYaGYPWNPNGSIYNIAGITNEKGNVIGLMPHPERAfygyqhpyWEKE 240

                         250
                  ....*....|....*.
gi 1082558936 212 LGNTDGRIIFESILKS 227
Cdd:PRK01175  241 EDYGDGKIFFDSLINY 256
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 5-209 7.86e-50

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: 163.44  E-value: 7.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   5 VVIFPGSNCDEDMIYVLESV-MEQEVV---RLWHKDTDLQHVDGIFLPGGFSFGDYLRSG-AIAKF----SPIMKSVIEF 75
Cdd:pfam13507   6 ILREPGTNGEYEMAAAFERAgFDAVDVhmsDLLSGRVSLDDFQGLAAPGGFSYGDVLGSGkGWAASilfnPKLRDAFEAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  76 -ANKGGFVFGVCNGFQVLCESGLLPG----------ALLHNDNQKFICK--NIFIKPDNNTSALTNLipekATLKIPIAH 142
Cdd:pfam13507  86 fNRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRwvNVKISEKSPSVFLRGM----DGSGLPVAH 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936 143 GEGR-YYADVETLKNMRLNKQILFRYCNEDGSINLES--NPNGSVENIAGVCNEKRNVYGMMPHPERASD 209
Cdd:pfam13507 162 GEGRfVFRSEEVLARLEANGQVALRYVDNAGNPTEEYpfNPNGSPLGIAGICSPDGRVLGLMPHPERVFR 231
FGAM_synt TIGR01735
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ...
 36-207 6.21e-26

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: 105.25  E-value: 6.21e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   36 DTDLQHVDGIFLPGGFSFGDYLRSG----AIAKFSPIMKSVIE--FANKGGFVFGVCNGFQVLCE-SGLLPG-----ALL 103
Cdd:TIGR01735 1095 RVHLDEFRGLAACGGFSYGDVLGAGkgwaKSILFNPRLRDQFQafFKRPDTFSLGVCNGCQMLSNlLEWIPGtenwpHFV 1174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  104 HNDNQKFICKNIFIKPDNNTSALTNLIpEKATLKIPIAHGEGR-YYADVETLKNMRLNKQILFRYCNEDGSIN--LESNP 180
Cdd:TIGR01735 1175 RNNSERFEARVASVRVGESPSIMLRGM-AGSRLPVAVAHGEGYaAFSSPELQAQADASGLAALRYIDDDGNPTeaYPLNP 1253

                          170       180
                   ....*....|....*....|....*..
gi 1082558936  181 NGSVENIAGVCNEKRNVYGMMPHPERA 207
Cdd:TIGR01735 1254 NGSPGGIAGITSCDGRVTIMMPHPERV 1280
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
 10-207 2.69e-25

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 103.69  E-value: 2.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   10 GSNCDEDMI-YVLESVMEQ---EVVRLWHKDTDLQHVDGIFLPGGFSFGDYLRSG----AIAKFS-PIMKSVIEFAN-KG 79
Cdd:PLN03206  1047 GSNGDREMAaAFYAAGFEPwdvTMSDLLNGRISLDDFRGIVFVGGFSYADVLDSAkgwaGSIRFNePLLQQFQEFYNrPD 1126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   80 GFVFGVCNGFQVLCESGLLPGA----------------LLHNDNQKFICKNIFIKPDNNTSALTNLIpEKATLKIPIAHG 143
Cdd:PLN03206  1127 TFSLGVCNGCQLMALLGWVPGPqvggglgaggdpsqprFVHNESGRFECRFTSVTIEDSPAIMLKGM-EGSTLGVWAAHG 1205

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082558936  144 EGR-YYADVETLKNMRLNKQILFRYCNEDGSINLE--SNPNGSVENIAGVCNEKRNVYGMMPHPERA 207
Cdd:PLN03206  1206 EGRaYFPDESVLDEVLKSNLAPVRYCDDDGEPTEQypFNPNGSPLGIAALCSPDGRHLAMMPHPERC 1272
PRK05297 PRK05297
phosphoribosylformylglycinamidine synthase; Provisional
 38-206 1.41e-22

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 235394 [Multi-domain]  Cd Length: 1290  Bit Score: 95.64  E-value: 1.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   38 DLQHVDGIFLPGGFSFGDYLRSG-----AIaKFSPIMKSVIE--FANKGGFVFGVCNGFQVLCE-SGLLPGA-----LLH 104
Cdd:PRK05297  1077 TLEDFKGLVACGGFSYGDVLGAGegwakSI-LFNPRLRDQFEafFARPDTFALGVCNGCQMMSNlKEIIPGAehwprFVR 1155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  105 NDNQKFICKNIFIK-PDNNTSALTNLipEKATLKIPIAHGEGRYYADVETLKNMRLNKQILFRYCNEDGSI--NLESNPN 181
Cdd:PRK05297  1156 NRSEQFEARFSLVEvQESPSIFLQGM--AGSRLPIAVAHGEGRAEFPDAHLAALEAKGLVALRYVDNHGQVteTYPANPN 1233

                          170       180
                   ....*....|....*....|....*
gi 1082558936  182 GSVENIAGVCNEKRNVYGMMPHPER 206
Cdd:PRK05297  1234 GSPNGITGLTTADGRVTIMMPHPER 1258
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-92 2.57e-09

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 53.37  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   4 GVVIFPGSNCDEdmIYVLESVMEQ---EVVRLWHK------DTDLQHVDGIFLPGGFSFGDYLRSGAiakfsPIMKSVIE 74
Cdd:cd01653     2 AVLLFPGFEELE--LASPLDALREagaEVDVVSPDggpvesDVDLDDYDGLILPGGPGTPDDLARDE-----ALLALLRE 74

                          90
                  ....*....|....*...
gi 1082558936  75 FANKGGFVFGVCNGFQVL 92
Cdd:cd01653    75 AAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-92 6.75e-09

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 51.43  E-value: 6.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936   4 GVVIFPGSNCDEdmIYVLESVMEQ---EVVRLWHKD------TDLQHVDGIFLPGGFSFGDYLRSGAiakfsPIMKSVIE 74
Cdd:cd03128     2 AVLLFGGSEELE--LASPLDALREagaEVDVVSPDGgpvesdVDLDDYDGLILPGGPGTPDDLAWDE-----ALLALLRE 74

                          90
                  ....*....|....*...
gi 1082558936  75 FANKGGFVFGVCNGFQVL 92
Cdd:cd03128    75 AAAAGKPVLGICLGAQLL 92
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
11-95 4.08e-08

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 51.47  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  11 SNCDEDMIYVLESVMEQEVVRLWHKDTDLQ-HVDGIFLPGGFsfgDYLRSGAIAKFSPIMKSVIEFANKGGFVFGVCNGF 89
Cdd:pfam07685  11 SNYTDDNLDPLRYEPAVRVRFVPLPDESLGpDADLIILPGGK---PTIQDLALLRNSGMDEAIKEAAEDGGPVLGICGGY 87


                  ....*.
gi 1082558936  90 QVLCES 95
Cdd:pfam07685  88 QMLGET 93
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 35-101 1.86e-06

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: 46.82  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  35 KDTDLQHVDGIFLPGGF--SFGDylrsgAIAKFSPIMKSVIEFANKGGFVFGVCNGFQVLCES------------GLLPG 100
Cdd:cd03130    34 KDEELPDADGLYLGGGYpeLFAE-----ELSANQSMRESIRAFAESGGPIYAECGGLMYLGESlddeegqsypmaGVLPG 108


                  .
gi 1082558936 101 A 101
Cdd:cd03130   109 D 109
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 35-100 3.05e-06

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: 45.71  E-value: 3.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082558936  35 KDTDLQHVDGIFLPGGFSFGDYLRSGAIAkfspiMKSVIEFANKGGFVFGVCNGFQVLCESGLLPG 100
Cdd:pfam01965  55 DDVKPDDYDALVLPGGRAGPERLRDNEKL-----VEFVKDFYEKGKPVAAICHGPQVLAAAGVLKG 115
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 35-100 9.38e-06

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: 44.32  E-value: 9.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082558936  35 KDTDLQHVDGIFLPGGFSFGDYLRSgaiakfSPIMKSVI-EFANKGGFVFGVCNGFQVLCESGLLPG 100
Cdd:COG0693    58 DDVDPDDYDALVLPGGHGAPDDLRE------DPDVVALVrEFYEAGKPVAAICHGPAVLAAAGLLKG 118
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 30-95 1.28e-05

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: 44.54  E-value: 1.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082558936  30 VRLWHKDTDLQHVDGIFLPGGFS-FGD--YLRSGAIAKfspimkSVIEFANKGGFVFGVCNGFQVLCES 95
Cdd:cd01750    26 VRYVEVPEGLGDADLIILPGSKDtIQDlaWLRKRGLAE------AIKNYARAGGPVLGICGGYQMLGKY 88
PRK00784 PRK00784
cobyric acid synthase;
30-95 6.41e-05

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 43.15  E-value: 6.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082558936  30 VRLWHKDTDLQHVDGIFLPGgfS---FGD--YLRSGAIAKfspimkSVIEFANKGGFVFGVCNGFQVLCES 95
Cdd:PRK00784  279 VRYVRPGEPLPDADLVILPG--SkntIADlaWLRESGWDE------AIRAHARRGGPVLGICGGYQMLGRR 341
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 18-124 8.95e-05

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: 41.39  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  18 IYVLESVMEQEVVRLWH----------KDTDLQHVDGIFLPGGFSFGDYLRSgaiakfSPIMKSVI-EFANKGGFVFGVC 86
Cdd:cd03135    27 EVTTASLEKKLAVGSSHgikvkadktlSDVNLDDYDAIVIPGGLPGAQNLAD------NEKLIKLLkEFNAKGKLIAAIC 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1082558936  87 NGFQVLCESGLLPGALL---HNDNQKFICKNIFIKP---DNN--TS 124
Cdd:cd03135   101 AAPAVLAKAGLLKGKKAtcyPGFEDKLGGANYVDEPvvvDGNiiTS 146
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
35-100 1.40e-04

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 42.04  E-value: 1.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082558936  35 KDTDLQHVDGIFLPGGFSfgdYLRSGAIAKFSPIMKSVIEFANKGGFVFGVCNGFQVLCES------------GLLPG 100
Cdd:PRK01077  281 ADEALPDCDGLYLGGGYP---ELFAAELAANTSMRASIRAAAAAGKPIYAECGGLMYLGESledadgerhpmvGLLPG 355
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 34-100 2.14e-04

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


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 40.94  E-value: 2.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082558936  34 HKDTDLQHVDGIFLPGGFSFGDylrsgAIAKF--SPIMKSVIEFANKGGFVFGVCNGFQVLCES----------GLLPG 100
Cdd:cd01748    29 SDPEEILSADKLILPGVGAFGD-----AMANLreRGLIEALKEAIASGKPFLGICLGMQLLFESseegggtkglGLIPG 102
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 43-230 2.62e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 40.50  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  43 DGIFLPGGFSFGD---YLRSGAIAKFspimksVIEFANKGGFVFGVCNGFQVLCES----------GLLPGAllhndnqk 109
Cdd:PRK13141   39 DGVILPGVGAFPDamaNLRERGLDEV------IKEAVASGKPLLGICLGMQLLFESseefgeteglGLLPGR-------- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936 110 fICKnifikpdnntsaltnlIPEKATLKIPiaH-GegryYADVETLKNMRLNKQIlfrycnEDG-------SINLESNPN 181
Cdd:PRK13141  105 -VRR----------------FPPEEGLKVP--HmG----WNQLELKKESPLLKGI------PDGayvyfvhSYYADPCDE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1082558936 182 gsvENIAGVCN---------EKRNVYGMMPHPERASDDELgntdgriifeSILKSFIG 230
Cdd:PRK13141  156 ---EYVAATTDygvefpaavGKDNVFGAQFHPEKSGDVGL----------KILKNFVE 200
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 43-100 3.08e-04

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: 39.84  E-value: 3.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082558936  43 DGIFLPGGFSfGDYLR--SGAIAkFspimksVIEFANKGGFVFGVCNGFQVLCESGLLPG 100
Cdd:cd03134    64 DALVIPGGTN-PDKLRrdPDAVA-F------VRAFAEAGKPVAAICHGPWVLISAGVVRG 115
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 30-95 1.02e-03

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: 39.66  E-value: 1.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082558936  30 VRLWHKDTDLQHVDGIFLPGgfS---FGD--YLRSGAIAKfspimkSVIEFANKGGFVFGVCNGFQVLCES 95
Cdd:COG1492   279 LRYVRPPEELGDADLVILPG--SkntIADlaWLRESGLDD------AIRAHARRGGPVLGICGGYQMLGRR 341
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 38-100 1.97e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 37.93  E-value: 1.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082558936  38 DLQHVDGIFLPGGFSFGDylrsgAIAKFSPIMKSVIEFANKGGFVFGVCNGFQVLCES----------GLLPG 100
Cdd:PRK13143   35 EILDADGIVLPGVGAFGA-----AMENLSPLRDVILEAARSGKPFLGICLGMQLLFESseegggvrglGLFPG 102
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 36-100 2.45e-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: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 37.63  E-value: 2.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082558936  36 DTDLQHVDGIFLPGGfSFGDYLRsgaiakfspIMKSVIE----FANKGGFVFGVCNGFQVLCESGLLPG 100
Cdd:cd03169    71 EVDPDDYDALVIPGG-RAPEYLR---------LDEKVLAivrhFAEANKPVAAICHGPQILAAAGVLKG 129
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 38-100 5.16e-03

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: 36.55  E-value: 5.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082558936  38 DLQHVDGIFLPG-GfSFGD---YLRSgaiakfSPIMKSVIEFANKGGFVFGVCNGFQVLCES----------GLLPG 100
Cdd:COG0118    35 EIRAADRLVLPGvG-AFGDameNLRE------RGLDEAIREAVAGGKPVLGICLGMQLLFERseengdteglGLIPG 104
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 28-88 6.80e-03

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: 36.35  E-value: 6.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082558936  28 EVVRLWHKDtDLQHVDGIFLPGGfsfgdylRSGAIAKF---SPIMKSVIEFANKGGFVFGVCNG 88
Cdd:cd01749    23 EVIEVRTPE-DLEGIDGLIIPGG-------ESTTIGKLlrrTGLLDPLREFIRAGKPVFGTCAG 78
 
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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