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Conserved domains on  [gi|1230362738|gb|OYJ38497|]
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imidazole glycerol phosphate synthase subunit HisH [Klebsiella pneumoniae subsp. pneumoniae]

Protein Classification

imidazole glycerol phosphate synthase subunit HisH( domain architecture ID 10014130)

imidazole glycerol phosphate synthase subunit HisH catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR

CATH:  3.40.50.880
EC:  4.3.2.10|3.5.1.2
Gene Ontology:  GO:0004359|GO:0000107|GO:0016829
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 1.83e-159

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 437.37  E-value: 1.83e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   1 MNVVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQPVLGICLGM 80
Cdd:PRK13170    1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  81 QLLGKRSEENNGVDLLGIIEQEVPKMTDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVNPYTIAQCNYG 160
Cdd:PRK13170   81 QLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEYTIAQCNYG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1230362738 161 EAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:PRK13170  161 EPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
 
Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 1.83e-159

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 437.37  E-value: 1.83e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   1 MNVVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQPVLGICLGM 80
Cdd:PRK13170    1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  81 QLLGKRSEENNGVDLLGIIEQEVPKMTDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVNPYTIAQCNYG 160
Cdd:PRK13170   81 QLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEYTIAQCNYG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1230362738 161 EAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:PRK13170  161 EPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-191 2.03e-107

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: 305.81  E-value: 2.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   1 MNVVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIK---ACTQPVLGIC 77
Cdd:COG0118     1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIReavAGGKPVLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  78 LGMQLLGKRSEENNGVDLLGIIEQEVPKMTDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVN--PYTIA 155
Cdd:COG0118    81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDdpEDVVA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1230362738 156 QCNYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLK 191
Cdd:COG0118   161 TTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 3-196 2.45e-101

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: 290.77  E-value: 2.45e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRE---LIDLIKACTQPVLGICLG 79
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGldlFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNGVDLLGIIEQEVPKMTDHglPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVNP-YTIAQCN 158
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR--KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEeAVLAYAD 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1230362738 159 YGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:TIGR01855 159 YGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 3-194 2.70e-101

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: 290.55  E-value: 2.70e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQ---PVLGICLG 79
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIAsgkPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNGVDLLGIIEQEVPKMTDH-GLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVNP--YTIAQ 156
Cdd:cd01748    81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASeGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDpdYILAT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1230362738 157 CNYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFL 194
Cdd:cd01748   161 TDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
GATase pfam00117
Glutamine amidotransferase class-I;
4-194 1.28e-18

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 79.20  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   4 VILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADK------LFLPGVGTAQAAmdqlrdRELIDLIKACTQ---PVL 74
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEenpdgiILSGGPGSPGAA------GGAIEAIREARElkiPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  75 GICLGMQLLGKRSEENngvdllgiieqevpkmTDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAmpVNPYTI 154
Cdd:pfam00117  75 GICLGHQLLALAFGGK----------------VVKAKKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYA--VDPDTL 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1230362738 155 -------AQCNYGEAFTAAVQKDN-FFGVQFHPE-RSGSAGAQLLKNFL 194
Cdd:pfam00117 137 pdglevtATSENDGTIMGIRHKKLpIFGVQFHPEsILTPHGPEILFNFF 185
 
Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 1.83e-159

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 437.37  E-value: 1.83e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   1 MNVVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQPVLGICLGM 80
Cdd:PRK13170    1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  81 QLLGKRSEENNGVDLLGIIEQEVPKMTDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVNPYTIAQCNYG 160
Cdd:PRK13170   81 QLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEYTIAQCNYG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1230362738 161 EAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:PRK13170  161 EPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-191 2.03e-107

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: 305.81  E-value: 2.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   1 MNVVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIK---ACTQPVLGIC 77
Cdd:COG0118     1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIReavAGGKPVLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  78 LGMQLLGKRSEENNGVDLLGIIEQEVPKMTDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVN--PYTIA 155
Cdd:COG0118    81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDdpEDVVA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1230362738 156 QCNYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLK 191
Cdd:COG0118   161 TTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 3-196 2.45e-101

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: 290.77  E-value: 2.45e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRE---LIDLIKACTQPVLGICLG 79
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGldlFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNGVDLLGIIEQEVPKMTDHglPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVNP-YTIAQCN 158
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR--KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEeAVLAYAD 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1230362738 159 YGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:TIGR01855 159 YGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 3-194 2.70e-101

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: 290.55  E-value: 2.70e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQ---PVLGICLG 79
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIAsgkPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNGVDLLGIIEQEVPKMTDH-GLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVNP--YTIAQ 156
Cdd:cd01748    81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASeGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDpdYILAT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1230362738 157 CNYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFL 194
Cdd:cd01748   161 TDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-196 6.91e-93

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 269.31  E-value: 6.91e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIK---ACTQPVLGICLG 79
Cdd:PRK13141    2 IAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKeavASGKPLLGICLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNGVDLLGIIEQEVPKMTDH-GLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSY-AMPVNP-YTIAQ 156
Cdd:PRK13141   82 MQLLFESSEEFGETEGLGLLPGRVRRFPPEeGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYyADPCDEeYVAAT 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1230362738 157 CNYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:PRK13141  162 TDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEM 201
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-196 3.67e-88

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 257.49  E-value: 3.67e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACT---QPVLGICLG 79
Cdd:PRK13181    2 IAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVekkQPVLGICLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNgVDLLGIIEQEVPKMTDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVNP--YTIAQC 157
Cdd:PRK13181   82 MQLLFESSEEGN-VKGLGLIPGDVKRFRSEPLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHSYYVPCEDpeDVLATT 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1230362738 158 NYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:PRK13181  161 EYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAEL 199
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-195 1.30e-77

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 230.82  E-value: 1.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   1 MNVVILDTGCANLNSVKSAIGR--HGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQ----PVL 74
Cdd:PRK13146    2 MTVAIIDYGSGNLRSAAKALERagAGADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAVLaagrPFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  75 GICLGMQLLGKRSEENNGVDLLGIIEQEVPKMTDHG--LPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYA-MPVNP 151
Cdd:PRK13146   82 GICVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDGpaLKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVHSYYaQPANP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1230362738 152 -YTIAQCNYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLE 195
Cdd:PRK13146  162 aDVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLA 206
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 8.01e-73

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 218.58  E-value: 8.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   1 MNVVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRD-RELIDLIKACTQPVLGICLG 79
Cdd:PRK13143    1 MMIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLSPlRDVILEAARSGKPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNGVDLLGIIEQEVPKMtDHGLPLPHMGWNRVYAKAGDRLFRGIEeGAYFYFVHSY-AMPVNP-YTIAQC 157
Cdd:PRK13143   81 MQLLFESSEEGGGVRGLGLFPGRVVRF-PAGVKVPHMGWNTVKVVKDCPLFEGID-GEYVYFVHSYyAYPDDEdYVVATT 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1230362738 158 NYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:PRK13143  159 DYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVEL 197
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 3-195 1.86e-56

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 186.46  E-value: 1.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQ---PVLGICLG 79
Cdd:PLN02617    9 VTLLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQndrPFLGICLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNGVDLLGIIEQEVPKM-TDHGLPLPHMGWNRVYAKAGDRLFRGIEeGAYFYFVHSY-AMPVNP---YTI 154
Cdd:PLN02617   89 LQLLFESSEENGPVEGLGVIPGVVGRFdSSNGLRVPHIGWNALQITKDSELLDGVG-GRHVYFVHSYrATPSDEnkdWVL 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1230362738 155 AQCNYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLE 195
Cdd:PLN02617  168 ATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRFLE 208
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-196 9.73e-54

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 170.02  E-value: 9.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACT----QPVLGICL 78
Cdd:PRK13152    2 IALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVlvqkKPILGICL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  79 GMQLLGKRSEENNGVDLLGIIEQEVPKM-TDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAMPVN-PYTIAQ 156
Cdd:PRK13152   82 GMQLFLERGYEGGVCEGLGFIEGEVVKFeEDLNLKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSFYVKCKdEFVSAK 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1230362738 157 CNYGEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:PRK13152  162 AQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL 201
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-195 1.86e-46

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 151.13  E-value: 1.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACT-QPVLGICLGMQ 81
Cdd:PRK13142    2 IVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNTdKKMIGICLGMQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  82 LLGKRSEENNgVDLLGIIEQE-VPKMTDHglPLPHMGWNRVYAKAgDRLFRGIeegayfYFVHSYAMPVNPYTIAQCNYG 160
Cdd:PRK13142   82 LMYEHSDEGD-ASGLGFIPGNiSRIQTEY--PVPHLGWNNLVSKH-PMLNQDV------YFVHSYQAPMSENVIAYAQYG 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1230362738 161 EAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLE 195
Cdd:PRK13142  152 ADIPAIVQFNNYIGIQFHPEKSGTYGLQILRQAIQ 186
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 1-195 2.44e-46

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 151.58  E-value: 2.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   1 MNVVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQ---PVLGIC 77
Cdd:CHL00188    2 MKIGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAegnPFIGIC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  78 LGMQLLGKRSEENNGvDLLGIIEQEVPKMTDHGL-PLPHMGWNRVYAKAGD------RLFRGIEEGAYFYFVHSY-AMPV 149
Cdd:CHL00188   82 LGLHLLFETSEEGKE-EGLGIYKGQVKRLKHSPVkVIPHMGWNRLECQNSEcqnsewVNWKAWPLNPWAYFVHSYgVMPK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1230362738 150 NPYTI-AQCNYG-EAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLE 195
Cdd:CHL00188  161 SQACAtTTTFYGkQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFMK 208
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-196 3.78e-43

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 143.51  E-value: 3.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRD---RELIDLIKACTQPVLGICLG 79
Cdd:PRK14004    2 IAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNStglRSTIDKHVESGKPLFGICIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  80 MQLLGKRSEENNG------VDLLGIIEQEVPKMTDHGLPLPHMGWNRVYAKAGDR--LFRGIEEGAYFYFVHSYaMPV-- 149
Cdd:PRK14004   82 FQILFESSEETNQgtkkeqIEGLGYIKGKIKKFEGKDFKVPHIGWNRLQIRRKDKskLLKGIGDQSFFYFIHSY-RPTga 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1230362738 150 --NPYTiAQCNY-GEAFTAAVQKDNFFGVQFHPERSGSAGAQLLKNFLEM 196
Cdd:PRK14004  161 egNAIT-GLCDYyQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFIEF 209
GATase pfam00117
Glutamine amidotransferase class-I;
4-194 1.28e-18

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 79.20  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   4 VILDTGCANLNSVKSAIGRHGYEPVVSRDPEVVLRADK------LFLPGVGTAQAAmdqlrdRELIDLIKACTQ---PVL 74
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEenpdgiILSGGPGSPGAA------GGAIEAIREARElkiPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  75 GICLGMQLLGKRSEENngvdllgiieqevpkmTDHGLPLPHMGWNRVYAKAGDRLFRGIEEGAYFYFVHSYAmpVNPYTI 154
Cdd:pfam00117  75 GICLGHQLLALAFGGK----------------VVKAKKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYA--VDPDTL 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1230362738 155 -------AQCNYGEAFTAAVQKDN-FFGVQFHPE-RSGSAGAQLLKNFL 194
Cdd:pfam00117 137 pdglevtATSENDGTIMGIRHKKLpIFGVQFHPEsILTPHGPEILFNFF 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 20-194 7.84e-13

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: 63.71  E-value: 7.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  20 IGRHGYEPVVSR------DPEVVLRADKLFL-PGVGT-AQAAMDqlrdrelIDLIKACTQ--PVLGICLGMQLLGkrsEE 89
Cdd:cd01743    18 LRELGAEVVVVRndeitlEELELLNPDAIVIsPGPGHpEDAGIS-------LEIIRALAGkvPILGVCLGHQAIA---EA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  90 NNGVdllgIIEQEVPKmtdHGL--PLPHmgwnrvyakAGDRLFRGIEEG--AYFYfvHSYA---MPVNPY--TIAQCNYG 160
Cdd:cd01743    88 FGGK----VVRAPEPM---HGKtsEIHH---------DGSGLFKGLPQPftVGRY--HSLVvdpDPLPDLleVTASTEDG 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1230362738 161 EAFTAAVQKDNFFGVQFHPERSGSA-GAQLLKNFL 194
Cdd:cd01743   150 VIMALRHRDLPIYGVQFHPESILTEyGLRLLENFL 184
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 20-196 3.70e-11

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: 59.28  E-value: 3.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  20 IGRHGYEPVVSR----DPEVV--LRADKLFL-PGVGTAQAAmdqlrdRELIDLIKAC--TQPVLGICLGMQLLGkrseen 90
Cdd:COG0512    18 LGELGAEVVVVRndeiTLEEIeaLAPDGIVLsPGPGTPEEA------GISLEVIRAFagKIPILGVCLGHQAIG------ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  91 ngvdllgiieqEVpkmtdHGLPLPHMGwnRVY-AKA------GDRLFRGIEEGayFYFV--HSYAmpVNPYTI------- 154
Cdd:COG0512    86 -----------EA-----FGGKVVRAP--EPMhGKTspithdGSGLFAGLPNP--FTATryHSLV--VDRETLpdelevt 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1230362738 155 AQCNYGEafTAAVQ--KDNFFGVQFHPERSGS-AGAQLLKNFLEM 196
Cdd:COG0512   144 AWTEDGE--IMGIRhrELPIEGVQFHPESILTeHGHQLLANFLEL 186
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 59-194 4.35e-09

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 53.31  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  59 DRELIDLIKactqPVLGICLGMQLLGKrseENNGvdllgiieqEVPKmtdhglplphmGWNRVYAKA------GDRLFRG 132
Cdd:cd01742    63 DPEIFELGV----PVLGICYGMQLIAK---ALGG---------KVER-----------GDKREYGKAeieiddSSPLFEG 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1230362738 133 IEEGAYFYFVHS---YAMPVNPYTIA---QCNYgeaftAAVQ--KDNFFGVQFHPERSGSA-GAQLLKNFL 194
Cdd:cd01742   116 LPDEQTVWMSHGdevVKLPEGFKVIAssdNCPV-----AAIAneEKKIYGVQFHPEVTHTEkGKEILKNFL 181
guaA PRK00074
GMP synthase; Reviewed
 72-194 6.44e-09

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 54.67  E-value: 6.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  72 PVLGICLGMQLLGKrseenngvDLLGIIEQevpkmTDHGlplpHMGWNRVYAKAGDRLFRGIEEGAYFYFVHS---YAMP 148
Cdd:PRK00074   77 PVLGICYGMQLMAH--------QLGGKVER-----AGKR----EYGRAELEVDNDSPLFKGLPEEQDVWMSHGdkvTELP 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1230362738 149 VNPYTIAQ---CNYgeaftAAVQKD--NFFGVQFHPERSGSA-GAQLLKNFL 194
Cdd:PRK00074  140 EGFKVIAStenCPI-----AAIANEerKFYGVQFHPEVTHTPqGKKLLENFV 186
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 60-194 7.99e-09

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: 53.02  E-value: 7.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  60 RELIDLIKACTQ---PVLGICLGMQLLGKrseenngvdLLGiieQEVpkmtdhgLPLPH---MGWNRVY---AKAGDRLF 130
Cdd:cd01741    68 KKLKELIRQALAagkPVLGICLGHQLLAR---------ALG---GKV-------GRNPKgweIGWFPVTlteAGKADPLF 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738 131 RGIEEGAYFYFVHSYAMPVNP------YTIAQCNYgEAFTAavqKDNFFGVQFHPERsgsagaQLLKNFL 194
Cdd:cd01741   129 AGLPDEFPVFHWHGDTVVELPpgavllASSEACPN-QAFRY---GDRALGLQFHPEE------RLLRNFL 188
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 60-180 1.33e-07

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: 49.94  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  60 RELIDLIKACTQ---PVLGICLGMQLLGKrseenngvdLLGiieQEVPKMtdhglPLPHMGWNRVYAKAGDRLFRGIEEG 136
Cdd:COG0518    69 EDEPALIREAFElgkPVLGICYGAQLLAH---------ALG---GKVEPG-----PGREIGWAPVELTEADPLFAGLPDE 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1230362738 137 AYFYFVHSY---AMPVNPYTIA---QCNYgeaftAAVQ-KDNFFGVQFHPE 180
Cdd:COG0518   132 FTVWMSHGDtvtELPEGAEVLAssdNCPN-----QAFRyGRRVYGVQFHPE 177
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-83 1.77e-07

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: 47.98  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKS---AIGRHGYEPVV-------SRDPEVVLRADKLFLPGVGtaQAAMDQLRDRELIDLIKACTQ- 71
Cdd:cd01653     1 VAVLLFPGFEELELASpldALREAGAEVDVvspdggpVESDVDLDDYDGLILPGGP--GTPDDLARDEALLALLREAAAa 78

                          90
                  ....*....|....
gi 1230362738  72 --PVLGICLGMQLL 83
Cdd:cd01653    79 gkPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-83 3.76e-07

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: 46.42  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGCANLNSVKS---AIGRHGYEPVV-------SRDPEVVLRADKLFLPGVGtaQAAMDQLRDRELIDLIKACTQ- 71
Cdd:cd03128     1 VAVLLFGGSEELELASpldALREAGAEVDVvspdggpVESDVDLDDYDGLILPGGP--GTPDDLAWDEALLALLREAAAa 78

                          90
                  ....*....|....
gi 1230362738  72 --PVLGICLGMQLL 83
Cdd:cd03128    79 gkPVLGICLGAQLL 92
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 20-196 7.97e-07

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 47.43  E-value: 7.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  20 IGRHGYEPVVSRDPEVV------LRADKLFL-PGVGT-AQAAMdqlrdreLIDLIK--ACTQPVLGICLGMQLLGkrseE 89
Cdd:PRK05670   19 LGELGAEVVVYRNDEITleeieaLNPDAIVLsPGPGTpAEAGI-------SLELIRefAGKVPILGVCLGHQAIG----E 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  90 NNGvdllGIIEQEVPKMtdHGlplphmgwnrvyaKA------GDRLFRGIEE----GAYfyfvHSYAmpVNPYTIAQCny 159
Cdd:PRK05670   88 AFG----GKVVRAKEIM--HG-------------KTspiehdGSGIFAGLPNpftvTRY----HSLV--VDRESLPDC-- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1230362738 160 geaF--TA--------AVQ--KDNFFGVQFHPERSGSA-GAQLLKNFLEM 196
Cdd:PRK05670  141 ---LevTAwtddgeimGVRhkELPIYGVQFHPESILTEhGHKLLENFLEL 187
PRK13566 PRK13566
anthranilate synthase component I;
22-196 1.66e-06

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 47.60  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  22 RHGYEPVVSR---DPEVV--LRADKLFL-PGVGTAQ-----AAMDQLRDRELidlikactqPVLGICLGMQLLGkrsEEN 90
Cdd:PRK13566  548 QTGAEVTTVRygfAEEMLdrVNPDLVVLsPGPGRPSdfdckATIDAALARNL---------PIFGVCLGLQAIV---EAF 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  91 NGVdlLGIIEQEVpkmtdHGLPlphmgwNRVYAKAGDRLFRGIEE----GAYfyfvHS-YAMPVNpytiaqcnYGEAFTA 165
Cdd:PRK13566  616 GGE--LGQLAYPM-----HGKP------SRIRVRGPGRLFSGLPEeftvGRY----HSlFADPET--------LPDELLV 670

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1230362738 166 -AVQKDN-----------FFGVQFHPER----SGSAGAQLLKNFLEM 196
Cdd:PRK13566  671 tAETEDGvimaiehktlpVAAVQFHPESimtlGGDVGLRIIENVVRL 717
PLN02347 PLN02347
GMP synthetase
 61-194 2.31e-06

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 46.99  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  61 ELIDLIKACTQPVLGICLGMQLLGKRseenngvdLLGIIE----QEVPKMTdhglplphmgwnrVYAKAGDRLFRGIEEG 136
Cdd:PLN02347   77 GFFDYCRERGVPVLGICYGMQLIVQK--------LGGEVKpgekQEYGRME-------------IRVVCGSQLFGDLPSG 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1230362738 137 AYFYFVHSY-----AMPVNPYTIAQCNYGEafTAAVQ--KDNFFGVQFHPERSGSA-GAQLLKNFL 194
Cdd:PLN02347  136 ETQTVWMSHgdeavKLPEGFEVVAKSVQGA--VVAIEnrERRIYGLQYHPEVTHSPkGMETLRHFL 199
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 53-180 2.63e-05

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: 43.40  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  53 AMDQLRDRELIDLIKACTQ---PVLGICLGMQLLgkrseennGVDLLGIIEQEVPKMTDHGLPLPHmgwnRVYAKAGDRL 129
Cdd:pfam07722  85 PYDPARDAYELALIRAALArgkPILGICRGFQLL--------NVALGGTLYQDIQEQPGFTDHREH----CQVAPYAPSH 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1230362738 130 FRGIEEGAYFYFVHSYAMP-VNPY-------------TIAQCNYG--EAFTAAVQKDNFFGVQFHPE 180
Cdd:pfam07722 153 AVNVEPGSLLASLLGSEEFrVNSLhhqaidrlapglrVEAVAPDGtiEAIESPNAKGFALGVQWHPE 219
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 23-100 3.36e-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: 42.62  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  23 HGYEPVVSRDPEVVLRADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQ---PVLGICLGMQLLGKRSEENNGVDLLGII 99
Cdd:cd01750    22 PGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARaggPVLGICGGYQMLGKYIVDPEGVEGPGEI 101


                  .
gi 1230362738 100 E 100
Cdd:cd01750   102 E 102
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 20-195 5.33e-05

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 42.08  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  20 IGRHGYEPVVSRDPEVV------LRADKLFL-PGVGT-AQAAMDqlrdrelIDLIK--ACTQPVLGICLGMQLLGkrseE 89
Cdd:TIGR00566  19 FCELGAEVVVKRNDSLTlqeieaLLPLLIVIsPGPCTpNEAGIS-------LEAIRhfAGKLPILGVCLGHQAMG----Q 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  90 NNGVDllgIIEQEVPKmtdHG--LPLPHMGWNRVyakAGdrLFRGIEEGAYfyfvHSyaMPVNPYTIAQC-------NYG 160
Cdd:TIGR00566  88 AFGGD---VVRANTVM---HGktSEIEHNGAGIF---RG--LFNPLTATRY----HS--LVVEPETLPTCfpvtaweEEN 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1230362738 161 EAFTAAVQKD-NFFGVQFHPERSGSA-GAQLLKNFLE 195
Cdd:TIGR00566 151 IEIMAIRHRDlPLEGVQFHPESILSEqGHQLLANFLH 187
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 19-83 8.12e-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: 41.69  E-value: 8.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  19 AIGRHGYEPVV-------SRDPEVVLRADKLFLPG------------VGTAQAAMDQLRDR-ELiDLIKACTQ---PVLG 75
Cdd:COG2071    23 AVRAAGGLPVLlppvgdeEDLDELLDRLDGLVLTGgadvdpalygeePHPELGPIDPERDAfEL-ALIRAALErgkPVLG 101


                  ....*...
gi 1230362738  76 ICLGMQLL 83
Cdd:COG2071   102 ICRGMQLL 109
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 19-181 9.02e-05

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 41.41  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  19 AIGRHGYEPVV-------SRDPEVVLRADKLFLPGVG------------TAQAAMDQLRDRELIDLIKACTQ---PVLGI 76
Cdd:cd01745    27 AVRKAGGLPVLlppvddeEDLEQYLELLDGLLLTGGGdvdpplygeephPELGPIDPERDAFELALLRAALErgkPILGI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  77 CLGMQLL-----GK-------RSEENNGVDLLGiieqevpkmtdHGLplphmgwnRVYAKAGDRLFRGIEegayfyfvhs 144
Cdd:cd01745   107 CRGMQLLnvalgGTlyqdirvNSLHHQAIKRLA-----------DGL--------RVEARAPDGVIEAIE---------- 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1230362738 145 yampvnpytiaqcNYGEAFtaavqkdnFFGVQFHPER 181
Cdd:cd01745   158 -------------SPDRPF--------VLGVQWHPEW 173
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
72-194 1.25e-04

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 42.01  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  72 PVLGICLGMQLLGKRSEENngvdllgIIEQEVPKmtdHGL--PLPHmgwnrvyakAGDRLFRGIEEGAYFYFVHSYampv 149
Cdd:PRK14607   75 PILGVCLGHQAIGYAFGGK-------IVHAKRIL---HGKtsPIDH---------NGKGLFRGIPNPTVATRYHSL---- 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1230362738 150 npyTIAQCNYGEAFTAAVQKDN------------FFGVQFHPERSGSA-GAQLLKNFL 194
Cdd:PRK14607  132 ---VVEEASLPECLEVTAKSDDgeimgirhkehpIFGVQFHPESILTEeGKRILKNFL 186
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
26-84 3.28e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 40.03  E-value: 3.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1230362738  26 EPVVSRDPEVVLRADKLFL-PGVGTAQAAmdqlrdRELIDLIKACTQ---PVLGICLGMQLLG 84
Cdd:PRK07765   34 DPRLADEAAVAAQFDGVLLsPGPGTPERA------GASIDMVRACAAagtPLLGVCLGHQAIG 90
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 19-99 4.77e-04

Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 39.43  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  19 AIGRHGYEPVVSRDPEVVLRADKLFLPGvGTAQAAMDQLRDRELIDLIK---ACTQPVLGICLGMQLLGKRSEENNGVDL 95
Cdd:cd01749    16 ALERLGVEVIEVRTPEDLEGIDGLIIPG-GESTTIGKLLRRTGLLDPLRefiRAGKPVFGTCAGLILLAKEVEDQGGQPL 94


                  ....
gi 1230362738  96 LGII 99
Cdd:cd01749    95 LGLL 98
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 3-186 5.05e-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: 39.02  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738   3 VVILDTGcanlnsVKSAIGR----HGYEPVV---SRDPEVVL--RADKLFLP-GVGTAQAAmdqlrdRELIDLIKAC--- 69
Cdd:cd01744     1 VVVIDFG------VKHNILRellkRGCEVTVvpyNTDAEEILklDPDGIFLSnGPGDPALL------DEAIKTVRKLlgk 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  70 TQPVLGICLGMQLLG--------KRSEENNG-----VDLL-GIIEqevpkMT--DHGlplphmgwnrvYAKAGDRLfrgi 133
Cdd:cd01744    69 KIPIFGICLGHQLLAlalgaktyKMKFGHRGsnhpvKDLItGRVY-----ITsqNHG-----------YAVDPDSL---- 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1230362738 134 EEGAYFYFVHsyampVNPYTIAQCNYgeaftaavQKDNFFGVQFHPErsGSAG 186
Cdd:cd01744   129 PGGLEVTHVN-----LNDGTVEGIRH--------KDLPVFSVQFHPE--ASPG 166
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
39-99 5.85e-04

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 39.15  E-value: 5.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1230362738  39 ADKLFLPG----VGTAQAAMDQLRDRELIDLIKACTqPVLGICLGMQLLGKRSEENNGV--DLLGII 99
Cdd:pfam07685  43 ADLIILPGgkptIQDLALLRNSGMDEAIKEAAEDGG-PVLGICGGYQMLGETIEDPEGVriEGLGLL 108
PRK00758 PRK00758
GMP synthase subunit A; Validated
 72-196 1.05e-03

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 38.29  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  72 PVLGICLGMQLLGK------RSEENNGvdlLGIIEQEVpkmTDH-----GLPlPHMgwnRVYAKAGD---RLFRGIEEGA 137
Cdd:PRK00758   69 PILGICLGHQLIAKafggevGRGEYGE---YALVEVEI---LDEddilkGLP-PEI---RVWASHADevkELPDGFEILA 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1230362738 138 yfyfvHSYAMPVnpytiaqcnygEAFtaaVQKDN-FFGVQFHPERSGSA-GAQLLKNFLEM 196
Cdd:PRK00758  139 -----RSDICEV-----------EAM---KHKEKpIYGVQFHPEVAHTEyGEEIFKNFLEI 180
PRK00784 PRK00784
cobyric acid synthase;
31-93 2.09e-03

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 38.14  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1230362738  31 RDPEVVLR----------ADKLFLPGVGTAQAAMDQLRDRELIDLIKACTQ---PVLGICLGMQLLGKRSEENNGV 93
Cdd:PRK00784  273 AEPGVDVRyvrpgeplpdADLVILPGSKNTIADLAWLRESGWDEAIRAHARrggPVLGICGGYQMLGRRIADPDGV 348
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 22-99 4.02e-03

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


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 37.08  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  22 RHGYEPVVSR----DPEVVLRADKLFLPGvGT--AQA-AMDQLRDR--ELIDLIKACTqPVLGICLGMQLLGKRSEENNG 92
Cdd:COG3442    30 WRGIDVEVVEvnpgDDLPFDDVDIVFIGG-GQdrEQEiVADDLLRIkdALRAAIEDGV-PVLAICGGYQLLGHYYETADG 107


                  ....*....
gi 1230362738  93 VDL--LGII 99
Cdd:COG3442   108 ERIpgLGIL 116
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
72-194 5.41e-03

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 36.43  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  72 PVLGICLGMQLLGKRseenngvdLLGIIEQEVPKMTDHGLPLPHmgwnrvyakAGDRLFRGIEEGAYFYFVHSyaMPVNP 151
Cdd:PRK08007   74 PILGVCLGHQAMAQA--------FGGKVVRAAKVMHGKTSPITH---------NGEGVFRGLANPLTVTRYHS--LVVEP 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1230362738 152 YTIAQCNYGEAFTAAVQ-------KDNFFGVQFHPERSGS-AGAQLLKNFL 194
Cdd:PRK08007  135 DSLPACFEVTAWSETREimgirhrQWDLEGVQFHPESILSeQGHQLLANFL 185
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 15-103 5.57e-03

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 36.40  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230362738  15 SVKSAIGRHG--YEPVVSRDPEVVLRADKLFLPGvGTAqAAMDQLRDRE-LIDLIKACTQ---PVLGICLGMQLLGKRSE 88
Cdd:PRK13527   18 ALKRALDELGidGEVVEVRRPGDLPDCDALIIPG-GES-TTIGRLMKREgILDEIKEKIEeglPILGTCAGLILLAKEVG 95

                          90
                  ....*....|....*....
gi 1230362738  89 ----ENNGVDLLGIIEQEV 103
Cdd:PRK13527   96 ddrvTKTEQPLLGLMDVTV 114
 
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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