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Conserved domains on  [gi|1067578658|emb|SBN12633|]
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imidazole glycerol phosphate synthase subunit HisH [Neisseria gonorrhoeae]

Protein Classification

imidazole glycerol phosphate synthase subunit HisH( domain architecture ID 10014122)

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 PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-212 8.02e-125

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 351.01  E-value: 8.02e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   1 MQTAIIDYGMGNLHSVLKSVRTAGQlagkNTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDA--LKN 78
Cdd:PRK13146    2 MTVAIIDYGSGNLRSAAKALERAGA----GADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAvlAAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  79 KPFFGICVGAQLLFDHSEE-GNTDGLGWFGGKVRRFardlrDPQGCRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVH 157
Cdd:PRK13146   78 RPFLGICVGMQLLFERGLEhGDTPGLGLIPGEVVRF-----QPDGPALKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVH 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1067578658 158 SYYFAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW 212
Cdd:PRK13146  153 SYYAQPANPADVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLAW 207
 
Name Accession Description Interval E-value
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-212 8.02e-125

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 351.01  E-value: 8.02e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   1 MQTAIIDYGMGNLHSVLKSVRTAGQlagkNTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDA--LKN 78
Cdd:PRK13146    2 MTVAIIDYGSGNLRSAAKALERAGA----GADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAvlAAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  79 KPFFGICVGAQLLFDHSEE-GNTDGLGWFGGKVRRFardlrDPQGCRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVH 157
Cdd:PRK13146   78 RPFLGICVGMQLLFERGLEhGDTPGLGLIPGEVVRF-----QPDGPALKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVH 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1067578658 158 SYYFAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW 212
Cdd:PRK13146  153 SYYAQPANPADVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLAW 207
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-207 1.59e-115

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: 327.00  E-value: 1.59e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   1 MQTAIIDYGMGNLHSVLKSVRTAGqlagknTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDAL-KNK 79
Cdd:COG0118     1 MMIAIIDYGMGNLRSVAKALERLG------AEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVaGGK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  80 PFFGICVGAQLLFDHSEE-GNTDGLGWFGGKVRRFARDlrdpqgcRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHS 158
Cdd:COG0118    75 PVLGICLGMQLLFERSEEnGDTEGLGLIPGEVVRFPAS-------DLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHS 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1067578658 159 YYFAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLK 207
Cdd:COG0118   148 YYVPPDDPEDVVATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 4-210 6.89e-108

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: 307.89  E-value: 6.89e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGNLHSVLKSVRTAGQlagkntKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDALKN-KPFF 82
Cdd:cd01748     2 AIIDYGMGNLRSVANALERLGA------EVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASgKPFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  83 GICVGAQLLFDHSEEGN-TDGLGWFGGKVRRFardlrdPQGCRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYYF 161
Cdd:cd01748    76 GICLGMQLLFESSEEGGgTKGLGLIPGKVVRF------PASEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1067578658 162 APENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFL 210
Cdd:cd01748   150 PPDDPDYILATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 3-212 4.25e-78

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: 232.60  E-value: 4.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   3 TAIIDYGMGNLHSVLKSVRTAGqlagknTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDALKN-KPF 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVG------AEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLgKPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  82 FGICVGAQLLFDHSEEGN-TDGLGWFGGKVRRFARDlrdpqgcrlKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYY 160
Cdd:TIGR01855  75 LGICLGMQLLFERSEEGGgVPGLGLIKGNVVKLEAR---------KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYY 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1067578658 161 fAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW 212
Cdd:TIGR01855 146 -AVCEEEAVLAYADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase pfam00117
Glutamine amidotransferase class-I;
4-210 1.18e-19

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 82.29  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGNLHSVLKSVRTAGQlagkNTKIFLSGDPDRVSRADK----VIFPGQGAmPDcmaalTRGGLDEAVKDALKNK 79
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGV----EVTVVPNDTPAEEILEENpdgiILSGGPGS-PG-----AAGGAIEAIREARELK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  80 -PFFGICVGAQLLFDHseegntdglgwFGGKVRRfardlrdpqgcRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHS 158
Cdd:pfam00117  71 iPILGICLGHQLLALA-----------FGGKVVK-----------AKKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHS 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578658 159 YYFAPEN-PE--TILGESDYPSPFACIVGKDN-VFATQFHTEKSH-DAGLTMLKNFL 210
Cdd:pfam00117 129 YAVDPDTlPDglEVTATSENDGTIMGIRHKKLpIFGVQFHPESILtPHGPEILFNFF 185
 
Name Accession Description Interval E-value
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-212 8.02e-125

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 351.01  E-value: 8.02e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   1 MQTAIIDYGMGNLHSVLKSVRTAGQlagkNTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDA--LKN 78
Cdd:PRK13146    2 MTVAIIDYGSGNLRSAAKALERAGA----GADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAvlAAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  79 KPFFGICVGAQLLFDHSEE-GNTDGLGWFGGKVRRFardlrDPQGCRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVH 157
Cdd:PRK13146   78 RPFLGICVGMQLLFERGLEhGDTPGLGLIPGEVVRF-----QPDGPALKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVH 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1067578658 158 SYYFAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW 212
Cdd:PRK13146  153 SYYAQPANPADVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLAW 207
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-207 1.59e-115

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: 327.00  E-value: 1.59e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   1 MQTAIIDYGMGNLHSVLKSVRTAGqlagknTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDAL-KNK 79
Cdd:COG0118     1 MMIAIIDYGMGNLRSVAKALERLG------AEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVaGGK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  80 PFFGICVGAQLLFDHSEE-GNTDGLGWFGGKVRRFARDlrdpqgcRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHS 158
Cdd:COG0118    75 PVLGICLGMQLLFERSEEnGDTEGLGLIPGEVVRFPAS-------DLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHS 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1067578658 159 YYFAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLK 207
Cdd:COG0118   148 YYVPPDDPEDVVATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 4-210 6.89e-108

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: 307.89  E-value: 6.89e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGNLHSVLKSVRTAGQlagkntKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDALKN-KPFF 82
Cdd:cd01748     2 AIIDYGMGNLRSVANALERLGA------EVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASgKPFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  83 GICVGAQLLFDHSEEGN-TDGLGWFGGKVRRFardlrdPQGCRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYYF 161
Cdd:cd01748    76 GICLGMQLLFESSEEGGgTKGLGLIPGKVVRF------PASEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1067578658 162 APENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFL 210
Cdd:cd01748   150 PPDDPDYILATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 4-212 4.14e-106

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 303.59  E-value: 4.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGNLHSVLKSVRTAGQlagkntKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDALKN-KPFF 82
Cdd:PRK13141    3 AIIDYGMGNLRSVEKALERLGA------EAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASgKPLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  83 GICVGAQLLFDHSEE-GNTDGLGWFGGKVRRFardlrdPQGCRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYYF 161
Cdd:PRK13141   77 GICLGMQLLFESSEEfGETEGLGLLPGRVRRF------PPEEGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1067578658 162 APENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW 212
Cdd:PRK13141  151 DPCDEEYVAATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEM 201
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-210 1.56e-98

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 284.07  E-value: 1.56e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   3 TAIIDYGMGNLHSVLKSVRTAGqlagknTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDALKNK-PF 81
Cdd:PRK13181    2 IAIIDYGAGNLRSVANALKRLG------VEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKqPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  82 FGICVGAQLLFDHSEEGNTDGLGWFGGKVRRFARDlrdpqgcRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYYF 161
Cdd:PRK13181   76 LGICLGMQLLFESSEEGNVKGLGLIPGDVKRFRSE-------PLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHSYYV 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1067578658 162 APENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFL 210
Cdd:PRK13181  149 PCEDPEDVLATTEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFA 197
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-212 3.51e-83

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 245.55  E-value: 3.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   1 MQTAIIDYGMGNLHSVLKSVRtagqLAGKNTKIflSGDPDRVSRADKVIFPGQGAMPDCMAALtrGGLDEAVKDAL-KNK 79
Cdd:PRK13143    1 MMIVIIDYGVGNLRSVSKALE----RAGAEVVI--TSDPEEILDADGIVLPGVGAFGAAMENL--SPLRDVILEAArSGK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  80 PFFGICVGAQLLFDHSEEG-NTDGLGWFGGKVRRFARDLrdpqgcrlKVPHMGWNTVRQTQNHPLFQGIpQNTRFYFVHS 158
Cdd:PRK13143   73 PFLGICLGMQLLFESSEEGgGVRGLGLFPGRVVRFPAGV--------KVPHMGWNTVKVVKDCPLFEGI-DGEYVYFVHS 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1067578658 159 YYFAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW 212
Cdd:PRK13143  144 YYAYPDDEDYVVATTDYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVEL 197
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 3-212 4.25e-78

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: 232.60  E-value: 4.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   3 TAIIDYGMGNLHSVLKSVRTAGqlagknTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDALKN-KPF 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVG------AEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLgKPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  82 FGICVGAQLLFDHSEEGN-TDGLGWFGGKVRRFARDlrdpqgcrlKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYY 160
Cdd:TIGR01855  75 LGICLGMQLLFERSEEGGgVPGLGLIKGNVVKLEAR---------KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYY 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1067578658 161 fAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW 212
Cdd:TIGR01855 146 -AVCEEEAVLAYADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-211 2.08e-60

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 187.37  E-value: 2.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   1 MQTAIIDYGMGNLHSVlksvRTAGQLAGKNTKIflSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDAlkNKP 80
Cdd:PRK13170    1 MNVVIIDTGCANLSSV----KFAIERLGYEPVV--SRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKAC--TQP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  81 FFGICVGAQLLFDHSEEGN-TDGLGWFGGKVRRFARdlrdpqgCRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSY 159
Cdd:PRK13170   73 VLGICLGMQLLGERSEESGgVDCLGIIDGPVKKMTD-------FGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSY 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1067578658 160 YfAPENPETIlGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLN 211
Cdd:PRK13170  146 A-MPVNEYTI-AQCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLE 195
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 4-212 7.43e-60

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 186.20  E-value: 7.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGNLHSVLKSVRTAGQlagkntKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDAL--KNKPF 81
Cdd:PRK13152    3 ALIDYKAGNLNSVAKAFEKIGA------INFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVlvQKKPI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  82 FGICVGAQLLFDHSEE-GNTDGLGWFGGKVRRFARDLRdpqgcrLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYY 160
Cdd:PRK13152   77 LGICLGMQLFLERGYEgGVCEGLGFIEGEVVKFEEDLN------LKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSFY 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1067578658 161 FAPeNPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW 212
Cdd:PRK13152  151 VKC-KDEFVSAKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL 201
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 5-210 2.40e-55

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 184.14  E-value: 2.40e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   5 IIDYGMGNLhsvlKSVRTAGQLAGknTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDALKN-KPFFG 83
Cdd:PLN02617   11 LLDYGAGNV----RSVRNAIRHLG--FTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNdRPFLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  84 ICVGAQLLFDHSEE-GNTDGLGWFGGKVRRFARdlrdpqGCRLKVPHMGWNTVRQTQNHPLFQGIPqNTRFYFVHSYYFA 162
Cdd:PLN02617   85 ICLGLQLLFESSEEnGPVEGLGVIPGVVGRFDS------SNGLRVPHIGWNALQITKDSELLDGVG-GRHVYFVHSYRAT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1067578658 163 P--ENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFL 210
Cdd:PLN02617  158 PsdENKDWVLATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRFL 207
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 4-210 1.17e-51

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 165.85  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGNLHSVLKSVRTAgqlagknTKIFL-SGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDAL-KNKPF 81
Cdd:PRK14004    3 AILDYGMGNIHSCLKAVSLY-------TKDFVfTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVeSGKPL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  82 FGICVGAQLLFDHSEEGNT-------DGLGWFGGKVRRFardlrdpQGCRLKVPHMGWNT--VRQTQNHPLFQGIPQNTR 152
Cdd:PRK14004   76 FGICIGFQILFESSEETNQgtkkeqiEGLGYIKGKIKKF-------EGKDFKVPHIGWNRlqIRRKDKSKLLKGIGDQSF 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578658 153 FYFVHSYYFAPENPETILGESDY-PSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFL 210
Cdd:PRK14004  149 FYFIHSYRPTGAEGNAITGLCDYyQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFI 207
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 1-210 2.11e-50

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 162.36  E-value: 2.11e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   1 MQTAIIDYGMGNLHSVLKSVRTAGQlagkNTKIFLSGDpdRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDAL-KNK 79
Cdd:CHL00188    2 MKIGIIDYSMGNLHSVSRAIQQAGQ----QPCIINSES--ELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIaEGN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  80 PFFGICVGAQLLFDHSEEGNTDGLGWFGGKVRRFARDLrdpqgcRLKVPHMGWNTVR----QTQNH--PLFQGIPQNTRF 153
Cdd:CHL00188   76 PFIGICLGLHLLFETSEEGKEEGLGIYKGQVKRLKHSP------VKVIPHMGWNRLEcqnsECQNSewVNWKAWPLNPWA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578658 154 YFVHSYYFAPENPETILGESDYPS-PFACIVGKDNVFATQFHTEKSHDAGLTMLKNFL 210
Cdd:CHL00188  150 YFVHSYGVMPKSQACATTTTFYGKqQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFM 207
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 4-210 9.65e-44

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 144.97  E-value: 9.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGNLHSVLKSVRTAGQlagkntKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDaLKNKPFFG 83
Cdd:PRK13142    3 VIVDYGLGNISNVKRAIEHLGY------EVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAK-NTDKKMIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  84 ICVGAQLLFDHSEEGNTDGLGWFGGKVRRFARDlrdpqgcrLKVPHMGWNTVRQTqnHPLFqgipqNTRFYFVHSYYfaP 163
Cdd:PRK13142   76 ICLGMQLMYEHSDEGDASGLGFIPGNISRIQTE--------YPVPHLGWNNLVSK--HPML-----NQDVYFVHSYQ--A 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1067578658 164 ENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFL 210
Cdd:PRK13142  139 PMSENVIAYAQYGADIPAIVQFNNYIGIQFHPEKSGTYGLQILRQAI 185
GATase pfam00117
Glutamine amidotransferase class-I;
4-210 1.18e-19

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 82.29  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGNLHSVLKSVRTAGQlagkNTKIFLSGDPDRVSRADK----VIFPGQGAmPDcmaalTRGGLDEAVKDALKNK 79
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGV----EVTVVPNDTPAEEILEENpdgiILSGGPGS-PG-----AAGGAIEAIREARELK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  80 -PFFGICVGAQLLFDHseegntdglgwFGGKVRRfardlrdpqgcRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHS 158
Cdd:pfam00117  71 iPILGICLGHQLLALA-----------FGGKVVK-----------AKKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHS 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578658 159 YYFAPEN-PE--TILGESDYPSPFACIVGKDN-VFATQFHTEKSH-DAGLTMLKNFL 210
Cdd:pfam00117 129 YAVDPDTlPDglEVTATSENDGTIMGIRHKKLpIFGVQFHPESILtPHGPEILFNFF 185
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 68-200 4.19e-14

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: 68.43  E-value: 4.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  68 LDEAVKDAlkNKPFFGICVGAQLLFDHseegntdglgwFGGKVRrfardlrdpqgcRLKVPHMGWNTVRQTQNHPLFQGI 147
Cdd:COG0518    74 LIREAFEL--GKPVLGICYGAQLLAHA-----------LGGKVE------------PGPGREIGWAPVELTEADPLFAGL 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1067578658 148 PQNTRFYFVHSYYFApENPE--TILGESDYpSPFACIVGKDNVFATQFHTEKSHD 200
Cdd:COG0518   129 PDEFTVWMSHGDTVT-ELPEgaEVLASSDN-CPNQAFRYGRRVYGVQFHPEVTHT 181
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 38-210 1.86e-11

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: 60.24  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  38 DPDRVsradkVIFPGQGAmPDcmaalTRGGLDEAVKDALKNKPFFGICVGAQLLFDHseegntdglgwFGGKVRrfardl 117
Cdd:cd01743    42 NPDAI-----VISPGPGH-PE-----DAGISLEIIRALAGKVPILGVCLGHQAIAEA-----------FGGKVV------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658 118 rdpqgcRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYYFAPENPETILGESDYPS---PFACIVGKDNVFATQFH 194
Cdd:cd01743    94 ------RAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLEVTASTEdgvIMALRHRDLPIYGVQFH 167

                         170       180
                  ....*....|....*....|.
gi 1067578658 195 -----TEKshdaGLTMLKNFL 210
Cdd:cd01743   168 pesilTEY----GLRLLENFL 184
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 68-210 7.06e-11

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: 58.80  E-value: 7.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  68 LDEAVKDALK-NKPFFGICVGAQLLFDHseegntdglgwFGGKVRrfardlRDPQGcrlkvPHMGWNTVRQT---QNHPL 143
Cdd:cd01741    70 LKELIRQALAaGKPVLGICLGHQLLARA-----------LGGKVG------RNPKG-----WEIGWFPVTLTeagKADPL 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578658 144 FQGIPQNTRFYFVHSYYFApENPE--TILGESDYpSPFACIVGKDNVFATQFHTEKshdaglTMLKNFL 210
Cdd:cd01741   128 FAGLPDEFPVFHWHGDTVV-ELPPgaVLLASSEA-CPNQAFRYGDRALGLQFHPEE------RLLRNFL 188
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 33-210 3.05e-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: 54.08  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  33 IFLSGDPDRVsRADKVifpgqgampdcmaaltrGGLDEAVKDAlkNKPFFGICVGAQLLFDHseegntdglgwFGGKVRr 112
Cdd:cd01742    45 IILSGGPSSV-YEEDA-----------------PRVDPEIFEL--GVPVLGICYGMQLIAKA-----------LGGKVE- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658 113 fardlrdpqgcRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYYF--APENPETIlGESDyPSPFACIVGKD-NVF 189
Cdd:cd01742    93 -----------RGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVvkLPEGFKVI-ASSD-NCPVAAIANEEkKIY 159

                         170       180
                  ....*....|....*....|..
gi 1067578658 190 ATQFHTEKSH-DAGLTMLKNFL 210
Cdd:cd01742   160 GVQFHPEVTHtEKGKEILKNFL 181
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 38-212 5.68e-07

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 47.82  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  38 DPDRVsradkVIFPGQGAmPD---CMAALtrggldeaVKDALKNKPFFGICVGAQLLFDHseegntdglgwFGGKVRRfA 114
Cdd:PRK05670   43 NPDAI-----VLSPGPGT-PAeagISLEL--------IREFAGKVPILGVCLGHQAIGEA-----------FGGKVVR-A 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658 115 RdlrdpqgcrlKVPHmGWNTVRQTQNHPLFQGIPQN---TRFyfvHSYYFAPEN-PE--TILGESDYPSPFACIVGKDNV 188
Cdd:PRK05670   97 K----------EIMH-GKTSPIEHDGSGIFAGLPNPftvTRY---HSLVVDRESlPDclEVTAWTDDGEIMGVRHKELPI 162

                         170       180
                  ....*....|....*....|....*..
gi 1067578658 189 FATQFHTEK---SHdaGLTMLKNFLNW 212
Cdd:PRK05670  163 YGVQFHPESiltEH--GHKLLENFLEL 187
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-92 5.87e-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: 46.82  E-value: 5.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGN---LHSVLKSVRTAG---QLAGKNTKIFLSGDpdRVSRADKVIFPGQGAMPDCMAALTRggLDEAVKDALK 77
Cdd:cd01653     2 AVLLFPGFEeleLASPLDALREAGaevDVVSPDGGPVESDV--DLDDYDGLILPGGPGTPDDLARDEA--LLALLREAAA 77

                          90
                  ....*....|....*.
gi 1067578658  78 N-KPFFGICVGAQLLF 92
Cdd:cd01653    78 AgKPILGICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-91 1.25e-06

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: 45.27  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYGMGN---LHSVLKSVRTAG---QLAGKNTKIFLSGDpdRVSRADKVIFPGQGAMPDCMAALTRggLDEAVKDALK 77
Cdd:cd03128     2 AVLLFGGSEeleLASPLDALREAGaevDVVSPDGGPVESDV--DLDDYDGLILPGGPGTPDDLAWDEA--LLALLREAAA 77

                          90
                  ....*....|....*
gi 1067578658  78 N-KPFFGICVGAQLL 91
Cdd:cd03128    78 AgKPVLGICLGAQLL 92
PRK13566 PRK13566
anthranilate synthase component I;
38-208 1.35e-06

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 47.99  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  38 DPDRVsradkVIFPGQGAMPDCMAALTrggLDEAVKdalKNKPFFGICVGAQLLFDHseegntdglgwFGGKVRrfardl 117
Cdd:PRK13566  569 NPDLV-----VLSPGPGRPSDFDCKAT---IDAALA---RNLPIFGVCLGLQAIVEA-----------FGGELG------ 620

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658 118 rdpqgcRLKVP-HMGWNTVRQTQNHPLFQGIPQNTRFYFVHSYYFAPEN-PE--TILGESDYPSPFAcIVGKDN-VFATQ 192
Cdd:PRK13566  621 ------QLAYPmHGKPSRIRVRGPGRLFSGLPEEFTVGRYHSLFADPETlPDelLVTAETEDGVIMA-IEHKTLpVAAVQ 693

                         170       180
                  ....*....|....*....|
gi 1067578658 193 FHTEK----SHDAGLTMLKN 208
Cdd:PRK13566  694 FHPESimtlGGDVGLRIIEN 713
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 4-104 3.86e-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: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658   4 AIIDYG-MGNlHSVLKSVRTAgqlagKNTKIFLSGDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKD-ALKNKPF 81
Cdd:cd01750     2 AVIRYPdISN-FTDLDPLARE-----PGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNyARAGGPV 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1067578658  82 FGICVGAQLLF------DHSE-EGNTDGLG 104
Cdd:cd01750    76 LGICGGYQMLGkyivdpEGVEgPGEIEGLG 105
PRK00784 PRK00784
cobyric acid synthase;
37-106 1.44e-04

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 41.99  E-value: 1.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578658  37 GDPDRVSRADKVIFPGQGAMPDCMAALTRGGLDEAVKDALKN-KPFFGICVGAQLL------FDHSE--EGNTDGLGWF 106
Cdd:PRK00784  283 RPGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRAHARRgGPVLGICGGYQMLgrriadPDGVEgaPGSVEGLGLL 361
PRK00758 PRK00758
GMP synthase subunit A; Validated
 78-210 2.23e-04

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 40.61  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  78 NKPFFGICVGAQLLFDHseegntdglgwFGGKVRrfardlrdpqgcRLKVPHMGWNTVRQTQNHPLFQGIPQNTRFYFVH 157
Cdd:PRK00758   67 DVPILGICLGHQLIAKA-----------FGGEVG------------RGEYGEYALVEVEILDEDDILKGLPPEIRVWASH 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658 158 syyfAPE---NPE--TILGESDYpSPFACIVGKDN-VFATQFHTEKSH-DAGLTMLKNFL 210
Cdd:PRK00758  124 ----ADEvkeLPDgfEILARSDI-CEVEAMKHKEKpIYGVQFHPEVAHtEYGEEIFKNFL 178
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 78-199 1.96e-03

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 38.02  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  78 NKPFFGICVGAQLLFDHseegntdglgwFGGKVRrfardlRDPQGcrlKVpHMGWNTVRQTQNHPLFQGIPQNTrfYFVH 157
Cdd:PRK06490   86 NKPFLGICLGAQMLARH-----------LGARVA------PHPDG---RV-EIGYYPLRPTEAGRALMHWPEMV--YHWH 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1067578658 158 SYYFA-PENPETILGESDYPSPfACIVGkDNVFATQFHTEKSH 199
Cdd:PRK06490  143 REGFDlPAGAELLATGDDFPNQ-AFRYG-DNAWGLQFHPEVTR 183
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 33-91 3.29e-03

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 37.69  E-value: 3.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578658  33 IFLS---GDPdrvSRADKVIfpgqgampdcmaaltrggldEAVKDAL-KNKPFFGICVGAQLL 91
Cdd:COG0505   221 VFLSngpGDP---AALDYAI--------------------ETIRELLgKGIPIFGICLGHQLL 260
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 46-94 6.03e-03

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 36.08  E-value: 6.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1067578658  46 DKVIFPGQGAMPDCMAALTRggLDEAVKDAL-KNKPFFGICVGAQLLFDH 94
Cdd:pfam01965  63 DALVLPGGRAGPERLRDNEK--LVEFVKDFYeKGKPVAAICHGPQVLAAA 110
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 68-200 8.61e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 36.09  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578658  68 LDEAVKDALknkPFFGICVGAQLLfDHSeegntdglgwFGGKVrrfardlrdpqGCRLKVPHMGWNTVRQT---QNHPLF 144
Cdd:PRK09065   81 LRQAAAAGM---PLLGICYGHQLL-AHA----------LGGEV-----------GYNPAGRESGTVTVELHpaaADDPLF 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578658 145 QGIPQNTRFYFVH--SYYFAPENpETILGESDYPSPFACIVGkDNVFATQFHTEKSHD 200
Cdd:PRK09065  136 AGLPAQFPAHLTHlqSVLRLPPG-AVVLARSAQDPHQAFRYG-PHAWGVQFHPEFTAH 191
 
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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