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Conserved domains on  [gi|985671755|gb|KXB02542|]
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glutamine amidotransferase [candidate division MSBL1 archaeon SCGC-AAA261F17]

Protein Classification

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT( domain architecture ID 10014275)

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-197 4.37e-106

glutamine amidotransferase subunit PdxT; Provisional


:

Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 302.96  E-value: 4.37e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHTEIINKAMRELDLEGKAFWLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPI 80
Cdd:PRK13527   1 MKIGVLALQGDVEEHIDALKRALDELGIDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKEKIEEGLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  81 LGTCAGLILLAKE-GDEEVEKTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGErPFRCVFIRAPAIEEVWSTVGVL 159
Cdd:PRK13527  81 LGTCAGLILLAKEvGDDRVTKTEQPLLGLMDVTVKRNAFGRQRDSFEAEIDLSGLDG-PFHAVFIRAPAITKVGGDVEVL 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 985671755 160 AGYRGKIVAAKQENLVALAFHPELTDDTRAHKYFLNLC 197
Cdd:PRK13527 160 AKLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKV 197
 
Name Accession Description Interval E-value
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-197 4.37e-106

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 302.96  E-value: 4.37e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHTEIINKAMRELDLEGKAFWLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPI 80
Cdd:PRK13527   1 MKIGVLALQGDVEEHIDALKRALDELGIDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKEKIEEGLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  81 LGTCAGLILLAKE-GDEEVEKTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGErPFRCVFIRAPAIEEVWSTVGVL 159
Cdd:PRK13527  81 LGTCAGLILLAKEvGDDRVTKTEQPLLGLMDVTVKRNAFGRQRDSFEAEIDLSGLDG-PFHAVFIRAPAITKVGGDVEVL 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 985671755 160 AGYRGKIVAAKQENLVALAFHPELTDDTRAHKYFLNLC 197
Cdd:PRK13527 160 AKLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKV 197
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 1-201 8.84e-103

Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440080 [Multi-domain]  Cd Length: 191  Bit Score: 294.28  E-value: 8.84e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHTEIINKAMreldleGKAFWLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPI 80
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLG------AEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  81 LGTCAGLILLAKEgdeeVEKTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGERPFRCVFIRAPAIEEVWSTVGVLA 160
Cdd:COG0311   75 FGTCAGLILLAKE----IEDPDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGPFPAVFIRAPYIEEVGPGVEVLA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 985671755 161 GYRGKIVAAKQENLVALAFHPELTDDTRAHKYFLNLCAASK 201
Cdd:COG0311  151 TVDGRIVAVRQGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 3-194 7.25e-95

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: 274.02  E-value: 7.25e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   3 IGVIGLQGAVSEHTEIInkamRELDLEGKAfwLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPILG 82
Cdd:cd01749    1 IGVLALQGDFREHIRAL----ERLGVEVIE--VRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  83 TCAGLILLAKEGDEEvekTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGERPFRCVFIRAPAIEEVWSTVGVLAGY 162
Cdd:cd01749   75 TCAGLILLAKEVEDQ---GGQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLGPFPAVFIRAPVIEEVGPGVEVLAEY 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 985671755 163 RGKIVAAKQENLVALAFHPELTDDTRAHKYFL 194
Cdd:cd01749  152 DGKIVAVRQGNVLATSFHPELTDDTRIHEYFL 183
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 2-195 1.70e-75

pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 274792 [Multi-domain]  Cd Length: 184  Bit Score: 225.00  E-value: 1.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755    2 KIGVIGLQGAVSEHTeiinKAMRELDLEGKAfwLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPIL 81
Cdd:TIGR03800   1 KIGVLALQGAVREHA----RALEALGVEGVE--VKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   82 GTCAGLILLAKEGDEEVEktGQplLNLMDMRITRNAFGRQRESFEVNLDIPAFGERPFRCVFIRAPAIEEVWSTVGVLAG 161
Cdd:TIGR03800  75 GTCAGLIMLAKEIIGQKE--GQ--LGLLDMTVERNAYGRQVDSFEAEVDIKGVGDDPITGVFIRAPKIVSVGNGVEILAK 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 985671755  162 YRGKIVAAKQENLVALAFHPELTDDTRAHKYFLN 195
Cdd:TIGR03800 151 VGNRIVAVRQGNILVSSFHPELTDDHRVHEYFLE 184
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 5-197 1.03e-54

SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680.


Pssm-ID: 334414 [Multi-domain]  Cd Length: 188  Bit Score: 172.33  E-value: 1.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755    5 VIGLQGAVSEHTEIINKAMREldlegkAFWLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRG-MPILGT 83
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAE------NKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   84 CAGLILLAKEGDEEVEKTgqplLNLMDMRITRNAFGRQRESFEVNLDIPAFGErPFRCVFIRAPAIEEVWS--TVGVLAG 161
Cdd:pfam01174  75 CAGLILLSKQLGNELVKT----LGLLKVTVKRNAFGRQVDSFEKECDFKNLIP-KFPGVFIRAPVIEEILDpeVVVVLYE 149

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 985671755  162 YRGKIVAAKQENLVALAFHPELT-DDTRAHKYFLNLC 197
Cdd:pfam01174 150 LDGKIVVAKQGNILATSFHPELAeDDYRVHDWFVENF 186
 
Name Accession Description Interval E-value
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-197 4.37e-106

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 302.96  E-value: 4.37e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHTEIINKAMRELDLEGKAFWLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPI 80
Cdd:PRK13527   1 MKIGVLALQGDVEEHIDALKRALDELGIDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKEKIEEGLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  81 LGTCAGLILLAKE-GDEEVEKTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGErPFRCVFIRAPAIEEVWSTVGVL 159
Cdd:PRK13527  81 LGTCAGLILLAKEvGDDRVTKTEQPLLGLMDVTVKRNAFGRQRDSFEAEIDLSGLDG-PFHAVFIRAPAITKVGGDVEVL 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 985671755 160 AGYRGKIVAAKQENLVALAFHPELTDDTRAHKYFLNLC 197
Cdd:PRK13527 160 AKLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKV 197
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 1-201 8.84e-103

Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440080 [Multi-domain]  Cd Length: 191  Bit Score: 294.28  E-value: 8.84e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHTEIINKAMreldleGKAFWLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPI 80
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLG------AEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  81 LGTCAGLILLAKEgdeeVEKTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGERPFRCVFIRAPAIEEVWSTVGVLA 160
Cdd:COG0311   75 FGTCAGLILLAKE----IEDPDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGPFPAVFIRAPYIEEVGPGVEVLA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 985671755 161 GYRGKIVAAKQENLVALAFHPELTDDTRAHKYFLNLCAASK 201
Cdd:COG0311  151 TVDGRIVAVRQGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 3-194 7.25e-95

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: 274.02  E-value: 7.25e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   3 IGVIGLQGAVSEHTEIInkamRELDLEGKAfwLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPILG 82
Cdd:cd01749    1 IGVLALQGDFREHIRAL----ERLGVEVIE--VRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  83 TCAGLILLAKEGDEEvekTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGERPFRCVFIRAPAIEEVWSTVGVLAGY 162
Cdd:cd01749   75 TCAGLILLAKEVEDQ---GGQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLGPFPAVFIRAPVIEEVGPGVEVLAEY 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 985671755 163 RGKIVAAKQENLVALAFHPELTDDTRAHKYFL 194
Cdd:cd01749  152 DGKIVAVRQGNVLATSFHPELTDDTRIHEYFL 183
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-199 3.67e-89

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 259.71  E-value: 3.67e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHTEIInkamRELDLEGKAfwLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPI 80
Cdd:PRK13525   2 MKIGVLALQGAVREHLAAL----EALGAEAVE--VRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  81 LGTCAGLILLAKEgdeeVEKTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGErPFRCVFIRAPAIEEVWSTVGVLA 160
Cdd:PRK13525  76 FGTCAGMILLAKE----IEGYEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGE-PFPAVFIRAPYIEEVGPGVEVLA 150

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 985671755 161 GYRGKIVAAKQENLVALAFHPELTDDTRAHKYFLNLCAA 199
Cdd:PRK13525 151 TVGGRIVAVRQGNILATSFHPELTDDTRVHRYFLEMVKE 189
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 2-195 1.70e-75

pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 274792 [Multi-domain]  Cd Length: 184  Bit Score: 225.00  E-value: 1.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755    2 KIGVIGLQGAVSEHTeiinKAMRELDLEGKAfwLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPIL 81
Cdd:TIGR03800   1 KIGVLALQGAVREHA----RALEALGVEGVE--VKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   82 GTCAGLILLAKEGDEEVEktGQplLNLMDMRITRNAFGRQRESFEVNLDIPAFGERPFRCVFIRAPAIEEVWSTVGVLAG 161
Cdd:TIGR03800  75 GTCAGLIMLAKEIIGQKE--GQ--LGLLDMTVERNAYGRQVDSFEAEVDIKGVGDDPITGVFIRAPKIVSVGNGVEILAK 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 985671755  162 YRGKIVAAKQENLVALAFHPELTDDTRAHKYFLN 195
Cdd:TIGR03800 151 VGNRIVAVRQGNILVSSFHPELTDDHRVHEYFLE 184
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 1-201 2.48e-61

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 191.08  E-value: 2.48e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHTEIINKamreldLEGKAFWLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGMPI 80
Cdd:PLN02832   2 MAIGVLALQGSFNEHIAALRR------LGVEAVEVRKPEQLEGVSGLIIPGGESTTMAKLAERHNLFPALREFVKSGKPV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  81 LGTCAGLILLAkEGDEEVEKTGQPLLNLMDMRITRNAFGRQRESFEVNLDIPAFGER-----PFRCVFIRAPAIEEVWST 155
Cdd:PLN02832  76 WGTCAGLIFLA-ERAVGQKEGGQELLGGLDCTVHRNFFGSQINSFETELPVPELAASeggpeTFRAVFIRAPAILSVGPG 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985671755 156 VGVLAGY------------------RGKIVAAKQENLVALAFHPELTDDTRAHKYFLNLCAASK 201
Cdd:PLN02832 155 VEVLAEYplpsekalyssstdaegrDKVIVAVKQGNLLATAFHPELTADTRWHSYFVKMVSESE 218
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 5-197 1.03e-54

SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680.


Pssm-ID: 334414 [Multi-domain]  Cd Length: 188  Bit Score: 172.33  E-value: 1.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755    5 VIGLQGAVSEHTEIINKAMREldlegkAFWLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRG-MPILGT 83
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAE------NKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   84 CAGLILLAKEGDEEVEKTgqplLNLMDMRITRNAFGRQRESFEVNLDIPAFGErPFRCVFIRAPAIEEVWS--TVGVLAG 161
Cdd:pfam01174  75 CAGLILLSKQLGNELVKT----LGLLKVTVKRNAFGRQVDSFEKECDFKNLIP-KFPGVFIRAPVIEEILDpeVVVVLYE 149

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 985671755  162 YRGKIVAAKQENLVALAFHPELT-DDTRAHKYFLNLC 197
Cdd:pfam01174 150 LDGKIVVAKQGNILATSFHPELAeDDYRVHDWFVENF 186
PRK13526 PRK13526
glutamine amidotransferase subunit PdxT; Provisional
 1-196 3.87e-41

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 184113 [Multi-domain]  Cd Length: 179  Bit Score: 137.39  E-value: 3.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHTEIINKAMRELDLegkafwLQEASQLSEVNGIIIPGGESTTIGRLMSTSGIFEKVKEMGRRGmPI 80
Cdd:PRK13526   3 QKVGVLAIQGGYQKHADMFKSLGVEVKL------VKFNNDFDSIDRLVIPGGESTTLLNLLNKHQIFDKLYNFCSSK-PV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  81 LGTCAGLILLAKegdeevektGQPLLNLMDMRITRNAFGRQRESFEVNLdipAFGERPFRCVFIRAPAIEEVWSTVGVLA 160
Cdd:PRK13526  76 FGTCAGSIILSK---------GEGYLNLLDLEVQRNAYGRQVDSFVADI---SFNDKNITGVFIRAPKFIVVGNQVDILS 143

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 985671755 161 GYRGKIVAAKQENLVALAFHPELTDDTRAHKYFLNL 196
Cdd:PRK13526 144 KYQNSPVLLRQANILVSSFHPELTQDPTVHEYFLAM 179
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-90 7.76e-08

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 48.35  E-value: 7.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   3 IGVIGLQGAVSEHTEIINKAMRELDLEGKAFWLQE-----ASQLSEVNGIIIPGGESTtIGRLMSTSGIFEKVKEMGRRG 77
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGT-PDDLAWDEALLALLREAAAAG 79

                         90
                 ....*....|...
gi 985671755  78 MPILGTCAGLILL 90
Cdd:cd03128   80 KPVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-90 8.85e-08

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 48.75  E-value: 8.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   3 IGVIGLQGAVSEHTEIINKAMRELDLEGKAFWLQE-----ASQLSEVNGIIIPGGESTtIGRLMSTSGIFEKVKEMGRRG 77
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGT-PDDLARDEALLALLREAAAAG 79

                         90
                 ....*....|...
gi 985671755  78 MPILGTCAGLILL 90
Cdd:cd01653   80 KPILGICLGAQLL 92
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 34-117 6.23e-07

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: 47.63  E-value: 6.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  34 WLQEASQLSEVNGIIIPGGESTtIGRL--MSTSGIFEKVKEMGRRGMPILGTCAGLILLAK--------EGDEEVEktGq 103
Cdd:cd01750   28 YVEVPEGLGDADLIILPGSKDT-IQDLawLRKRGLAEAIKNYARAGGPVLGICGGYQMLGKyivdpegvEGPGEIE--G- 103

                         90
                 ....*....|....
gi 985671755 104 plLNLMDMRITRNA 117
Cdd:cd01750  104 --LGLLDVETEFGP 115
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
35-120 7.74e-07

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 47.23  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   35 LQEASQLSEVNGIIIPGGESTtIGRL--MSTSGIFEKVKEMGRRGMPILGTCAGLILLAKEgDEEVEKTGQPLLNLMDM- 111
Cdd:pfam07685  34 LPDESLGPDADLIILPGGKPT-IQDLalLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGET-IEDPEGVRIEGLGLLDIe 111

                          90
                  ....*....|....*
gi 985671755  112 ------RITRNAFGR 120
Cdd:pfam07685 112 tvfqkeKLTGQVVGY 126
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-90 1.17e-04

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 41.25  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVSEHtEIINKAMRELDLEGKAFWLQEASqLSEVNGIIIPGGES-------TTIGRLmstSGIFEKVKEM 73
Cdd:PRK03619   1 MKVAVIVFPGSNCDR-DMARALRDLLGAEPEYVWHKETD-LDGVDAVVLPGGFSygdylrcGAIAAF---SPIMKAVKEF 75

                         90
                 ....*....|....*...
gi 985671755  74 GRRGMPILGTCAGL-ILL 90
Cdd:PRK03619  76 AEKGKPVLGICNGFqILT 93
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 39-137 1.30e-04

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: 41.04  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  39 SQLSEVNGIIIPGG--ESTTiGRLMSTSGIFEKVKEMGRRGMPILGTCAGLILLAKEGDEEVEKTGqPLLNLMDMRIT-- 114
Cdd:cd03130   36 EELPDADGLYLGGGypELFA-EELSANQSMRESIRAFAESGGPIYAECGGLMYLGESLDDEEGQSY-PMAGVLPGDARmt 113

                         90       100
                 ....*....|....*....|....*
gi 985671755 115 -RNAFG-RQRESFEVNLdIPAFGER 137
Cdd:cd03130  114 kRLGLGyREAEALGDTL-LGKKGTT 137
PRK06278 PRK06278
cobyrinic acid a,c-diamide synthase; Validated
 1-95 8.65e-04

cobyrinic acid a,c-diamide synthase; Validated


Pssm-ID: 180505 [Multi-domain]  Cd Length: 476  Bit Score: 39.25  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755   1 MKIGVIGLQGAVS--EH-----TEIIN----KAMRELDlegkafwlqeasqlsevnGIIIPGGestTIGRLMSTSGIFEK 69
Cdd:PRK06278   1 MEIGLLDIKGSLPcfENfgnlpTKIIDenniKEIKDLD------------------GLIIPGG---SLVESGSLTDELKK 59

                         90       100
                 ....*....|....*....|....*.
gi 985671755  70 vkEMGRRGMPILGTCAGLILLAKEGD 95
Cdd:PRK06278  60 --EILNFDGYIIGICSGFQILSEKID 83
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 38-115 1.11e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 38.31  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  38 ASQLSEVNGIIIPG-GE-STTIGRLMStSGIFEKVKEMGRRGMPILGTCAGLILLAKEGDEEVEKTgqplLNLMDMRITR 115
Cdd:PRK13181  32 PEEIAGADKVILPGvGAfGQAMRSLRE-SGLDEALKEHVEKKQPVLGICLGMQLLFESSEEGNVKG----LGLIPGDVKR 106
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
 42-93 3.09e-03

Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441402 [Multi-domain]  Cd Length: 459  Bit Score: 37.78  E-value: 3.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 985671755  42 SEVNGIIIPGG--EsTTIGRLMSTSGIFEKVKEMGRRGMPILGTCAGLILLAKE 93
Cdd:COG1797  290 EDVDGLYLGGGfpE-LFAEELSANRSMRESIREAAEAGMPIYAECGGLMYLCRS 342
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 28-182 3.80e-03

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: 36.71  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  28 LEGKAFWLQEASQLSEVNGIIIPG-GE-STTIGRLmSTSGIFEKVKEMGRRGMPILGTCAGLILLAKEGDEEVEKTGqpl 105
Cdd:cd01748   21 LGAEVIITSDPEEILSADKLILPGvGAfGDAMANL-RERGLIEALKEAIASGKPFLGICLGMQLLFESSEEGGGTKG--- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755 106 LNLMDMRITRnaFGRQRE---------SFEVNLDIPAF--GERPFRCVFI---RAPAIEEVWsTVGVlAGYRGKIVAA-K 170
Cdd:cd01748   97 LGLIPGKVVR--FPASEGlkvphmgwnQLEITKESPLFkgIPDGSYFYFVhsyYAPPDDPDY-ILAT-TDYGGKFPAAvE 172

                        170
                 ....*....|..
gi 985671755 171 QENLVALAFHPE 182
Cdd:cd01748  173 KDNIFGTQFHPE 184
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 41-94 4.40e-03

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


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 36.43  E-value: 4.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 985671755  41 LSEVNGIIIPGGESTTIGRlmsTSGIFEKVKEMGRRGMPILGTCAGLILLAKEG 94
Cdd:cd03140   58 PEDYDLLILPGGDSWDNPE---APDLAGLVRQALKQGKPVAAICGATLALARAG 108
PRK00784 PRK00784
cobyric acid synthase;
34-114 7.29e-03

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 36.60  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985671755  34 WLQEASQLSEVNGIIIPGGESTtIGRL--MSTSGIFEKVKEMGRRGMPILGTCAGLILLAK--------EGDEEVEKtGq 103
Cdd:PRK00784 281 YVRPGEPLPDADLVILPGSKNT-IADLawLRESGWDEAIRAHARRGGPVLGICGGYQMLGRriadpdgvEGAPGSVE-G- 357

                         90
                 ....*....|.
gi 985671755 104 plLNLMDMRIT 114
Cdd:PRK00784 358 --LGLLDVETV 366
 
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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