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Conserved domains on  [gi|1473345100|ref|WP_117812052|]
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imidazole glycerol phosphate synthase subunit HisH [Faecalibacillus faecis]

Protein Classification

imidazole glycerol phosphate synthase subunit HisH( domain architecture ID 10793738)

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 PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 1.17e-111

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 317.07  E-value: 1.17e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICL 80
Cdd:PRK13141    1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEKGYEVEETKGLGFIPGYVSYMDIDE--KIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDEN-LAA 157
Cdd:PRK13141   81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEglKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADPCDEEyVAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1473345100 158 YSDYGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEMVEC 202
Cdd:PRK13141  161 TTDYG-VEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEE 204
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 1.17e-111

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 317.07  E-value: 1.17e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICL 80
Cdd:PRK13141    1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEKGYEVEETKGLGFIPGYVSYMDIDE--KIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDEN-LAA 157
Cdd:PRK13141   81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEglKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADPCDEEyVAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1473345100 158 YSDYGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEMVEC 202
Cdd:PRK13141  161 TTDYG-VEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEE 204
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-194 4.06e-104

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: 297.72  E-value: 4.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICL 80
Cdd:COG0118     2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEKGYEVEETKGLGFIPGYVSYMDIDE-KIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSD-ENLAAY 158
Cdd:COG0118    82 GMQLLFERSEENGDTEGLGLIPGEVVRFPASDlKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDDpEDVVAT 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1473345100 159 SDYGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILR 194
Cdd:COG0118   162 TDYG-VPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-196 2.22e-99

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: 285.93  E-value: 2.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICLG 81
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  82 MQILFEKGYEVEETKGLGFIPGYVSYMD--IDEKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDEN-LAAY 158
Cdd:cd01748    81 MQLLFESSEEGGGTKGLGLIPGKVVRFPasEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDPDyILAT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1473345100 159 SDYGStKVTALVQNGNVMGCQFHPEKSGKVGQNILRAF 196
Cdd:cd01748   161 TDYGG-KFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNF 197
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-199 9.23e-85

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: 248.78  E-value: 9.23e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICLG 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  82 MQILFEKGYEVEETKGLGFIPGYVSYMDiDEKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDENLAAYSDY 161
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLE-ARKVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEEAVLAYADY 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1473345100 162 GsTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEM 199
Cdd:TIGR01855 160 G-EKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase pfam00117
Glutamine amidotransferase class-I;
3-196 3.60e-22

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 88.83  E-value: 3.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   3 VIIDYNVGNLKSVTGAFKRIGLEAVV-----SRDEKVIREAKGIVL-PGVGTfPTAMKNLerfhlVELLKERKEAGIPIL 76
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVvpndtPAEEILEENPDGIILsGGPGS-PGAAGGA-----IEAIREARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  77 GICLGMQILFEK-GYEVEETKglgfipgyvsymdideKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDEN- 154
Cdd:pfam00117  75 GICLGHQLLALAfGGKVVKAK----------------KFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPd 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1473345100 155 ---LAAYSDYGSTkVTALVQNGN-VMGCQFHPEKSGKV-GQNILRAF 196
Cdd:pfam00117 139 gleVTATSENDGT-IMGIRHKKLpIFGVQFHPESILTPhGPEILFNF 184
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 1.17e-111

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 317.07  E-value: 1.17e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICL 80
Cdd:PRK13141    1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEKGYEVEETKGLGFIPGYVSYMDIDE--KIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDEN-LAA 157
Cdd:PRK13141   81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEglKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADPCDEEyVAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1473345100 158 YSDYGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEMVEC 202
Cdd:PRK13141  161 TTDYG-VEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEE 204
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-194 4.06e-104

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: 297.72  E-value: 4.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICL 80
Cdd:COG0118     2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEKGYEVEETKGLGFIPGYVSYMDIDE-KIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSD-ENLAAY 158
Cdd:COG0118    82 GMQLLFERSEENGDTEGLGLIPGEVVRFPASDlKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDDpEDVVAT 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1473345100 159 SDYGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILR 194
Cdd:COG0118   162 TDYG-VPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-196 2.22e-99

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: 285.93  E-value: 2.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICLG 81
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  82 MQILFEKGYEVEETKGLGFIPGYVSYMD--IDEKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDEN-LAAY 158
Cdd:cd01748    81 MQLLFESSEEGGGTKGLGLIPGKVVRFPasEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDPDyILAT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1473345100 159 SDYGStKVTALVQNGNVMGCQFHPEKSGKVGQNILRAF 196
Cdd:cd01748   161 TDYGG-KFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNF 197
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-200 4.74e-86

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 252.10  E-value: 4.74e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFhlVELLKERKEAGIPILGICL 80
Cdd:PRK13143    2 MIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLSPL--RDVILEAARSGKPFLGICL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEKGYEVEETKGLGFIPGYVSYMDIDEKIPHMGWNQLHKTQDHLLLKYVhENEDVYFVHSYMAHVSD-ENLAAYS 159
Cdd:PRK13143   80 GMQLLFESSEEGGGVRGLGLFPGRVVRFPAGVKVPHMGWNTVKVVKDCPLFEGI-DGEYVYFVHSYYAYPDDeDYVVATT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1473345100 160 DYGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEMV 200
Cdd:PRK13143  159 DYG-IEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVELI 198
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-199 9.23e-85

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: 248.78  E-value: 9.23e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICLG 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  82 MQILFEKGYEVEETKGLGFIPGYVSYMDiDEKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDENLAAYSDY 161
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLE-ARKVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEEAVLAYADY 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1473345100 162 GsTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEM 199
Cdd:TIGR01855 160 G-EKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-196 5.86e-81

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 239.68  E-value: 5.86e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTGAFKRIGLEA--VVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKE-RKEAGIPILGI 78
Cdd:PRK13146    4 VAIIDYGSGNLRSAAKALERAGAGAdvVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEaVLAAGRPFLGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  79 CLGMQILFEKGYEVEETKGLGFIPGYVSYMDIDE---KIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDEN- 154
Cdd:PRK13146   84 CVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDGpalKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVHSYYAQPANPAd 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1473345100 155 LAAYSDYGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAF 196
Cdd:PRK13146  164 VVAWTDYG-GPFTAAVARDNLFATQFHPEKSQDAGLALLRNF 204
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-199 5.04e-79

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 234.37  E-value: 5.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICL 80
Cdd:PRK13181    1 MIAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKQPVLGICL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEkgyEVEE--TKGLGFIPGYV-SYMDIDEKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSD-ENLA 156
Cdd:PRK13181   81 GMQLLFE---SSEEgnVKGLGLIPGDVkRFRSEPLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHSYYVPCEDpEDVL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1473345100 157 AYSDYGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEM 199
Cdd:PRK13181  158 ATTEYG-VPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAEL 199
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-199 2.58e-68

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 207.02  E-value: 2.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEagiPILGICL 80
Cdd:PRK13170    2 NVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQ---PVLGICL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEKGYEVEETKGLGFIPGYVSYMDI-DEKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDENLaAYS 159
Cdd:PRK13170   79 GMQLLGERSEESGGVDCLGIIDGPVKKMTDfGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEYTI-AQC 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1473345100 160 DYGSTkVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEM 199
Cdd:PRK13170  158 NYGEP-FSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 7.37e-61

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 188.51  E-value: 7.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERK-EAGIPILGIC 79
Cdd:PRK13152    1 MIALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVlVQKKPILGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  80 LGMQILFEKGYEVEETKGLGFIPGYVSYMDID--EKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDENLAA 157
Cdd:PRK13152   81 LGMQLFLERGYEGGVCEGLGFIEGEVVKFEEDlnLKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSFYVKCKDEFVSA 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1473345100 158 YSDYGStKVTALVQNGNVMGCQFHPEKSGKVGQNILRAF 196
Cdd:PRK13152  161 KAQYGH-KFVASLQKDNIFATQFHPEKSQNLGLKLLENF 198
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-194 9.37e-61

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 187.72  E-value: 9.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAgiPILGICL 80
Cdd:PRK13142    1 MIVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNTDK--KMIGICL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFEKGYEvEETKGLGFIPGYVSYMDIDEKIPHMGWNQLHKTqdHLLLkyvheNEDVYFVHSYMAHVSdENLAAYSD 160
Cdd:PRK13142   79 GMQLMYEHSDE-GDASGLGFIPGNISRIQTEYPVPHLGWNNLVSK--HPML-----NQDVYFVHSYQAPMS-ENVIAYAQ 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1473345100 161 YGsTKVTALVQNGNVMGCQFHPEKSGKVGQNILR 194
Cdd:PRK13142  150 YG-ADIPAIVQFNNYIGIQFHPEKSGTYGLQILR 182
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-196 5.06e-60

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 196.09  E-value: 5.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICLG 81
Cdd:PLN02617    9 VTLLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRPFLGICLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  82 MQILFEKGYEVEETKGLGFIPGYVSYMDIDE--KIPHMGWNQLHKTQDHLLLKYVhENEDVYFVHSYMAHVSDEN---LA 156
Cdd:PLN02617   89 LQLLFESSEENGPVEGLGVIPGVVGRFDSSNglRVPHIGWNALQITKDSELLDGV-GGRHVYFVHSYRATPSDENkdwVL 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1473345100 157 AYSDYGSTKVTAlVQNGNVMGCQFHPEKSGKVGQNILRAF 196
Cdd:PLN02617  168 ATCNYGGEFIAS-VRKGNVHAVQFHPEKSGATGLSILRRF 206
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 2-196 2.51e-52

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 166.98  E-value: 2.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICLG 81
Cdd:CHL00188    4 IGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAEGNPFIGICLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  82 MQILFEKGYEVEETkGLGFIPGYVSYM--DIDEKIPHMGWNQLH----KTQDHLLLKYVH--ENEDVYFVHSYMAHVSDE 153
Cdd:CHL00188   84 LHLLFETSEEGKEE-GLGIYKGQVKRLkhSPVKVIPHMGWNRLEcqnsECQNSEWVNWKAwpLNPWAYFVHSYGVMPKSQ 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1473345100 154 N-LAAYSDYGSTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAF 196
Cdd:CHL00188  163 AcATTTTFYGKQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREF 206
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-200 5.29e-42

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 140.81  E-value: 5.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIIDYNVGNLKSVTGAFKRIGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICL 80
Cdd:PRK14004    1 MIAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVESGKPLFGICI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  81 GMQILFE------KGYEVEETKGLGFIPGYV-SYMDIDEKIPHMGWNQLH--KTQDHLLLKYVHENEDVYFVHSYMAHVS 151
Cdd:PRK14004   81 GFQILFEsseetnQGTKKEQIEGLGYIKGKIkKFEGKDFKVPHIGWNRLQirRKDKSKLLKGIGDQSFFYFIHSYRPTGA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1473345100 152 DEN-LAAYSDYGSTKVTALVQNGNVMGCQFHPEKSGKVGQNILRAFKEMV 200
Cdd:PRK14004  161 EGNaITGLCDYYQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFIEFV 210
GATase pfam00117
Glutamine amidotransferase class-I;
3-196 3.60e-22

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 88.83  E-value: 3.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   3 VIIDYNVGNLKSVTGAFKRIGLEAVV-----SRDEKVIREAKGIVL-PGVGTfPTAMKNLerfhlVELLKERKEAGIPIL 76
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVvpndtPAEEILEENPDGIILsGGPGS-PGAAGGA-----IEAIREARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  77 GICLGMQILFEK-GYEVEETKglgfipgyvsymdideKIPHMGWNQLHKTQDHLLLKYVHENEDVYFVHSYMAHVSDEN- 154
Cdd:pfam00117  75 GICLGHQLLALAfGGKVVKAK----------------KFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPd 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1473345100 155 ---LAAYSDYGSTkVTALVQNGN-VMGCQFHPEKSGKV-GQNILRAF 196
Cdd:pfam00117 139 gleVTATSENDGT-IMGIRHKKLpIFGVQFHPESILTPhGPEILFNF 184
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-86 8.11e-12

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: 59.53  E-value: 8.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTG---AFKRIGLEAVV-------SRDEKVIREAKGIVLPGVGTFPTAMKNLERfhLVELLKERKEA 71
Cdd:cd01653     1 VAVLLFPGFEELELASpldALREAGAEVDVvspdggpVESDVDLDDYDGLILPGGPGTPDDLARDEA--LLALLREAAAA 78

                          90
                  ....*....|....*
gi 1473345100  72 GIPILGICLGMQILF 86
Cdd:cd01653    79 GKPILGICLGAQLLV 93
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 63-183 1.87e-11

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: 60.73  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  63 ELLKERKEAGIPILGICLGMQILfekgyeveeTKGLGfipGYVSYMDIDEkiphMGWNQLHKTQDHLLLKYVHENEDVYf 142
Cdd:COG0518    73 ALIREAFELGKPVLGICYGAQLL---------AHALG---GKVEPGPGRE----IGWAPVELTEADPLFAGLPDEFTVW- 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1473345100 143 vHSYMAHVSD-----ENLaAYSDygSTKVTALVQNGNVMGCQFHPE 183
Cdd:COG0518   136 -MSHGDTVTElpegaEVL-ASSD--NCPNQAFRYGRRVYGVQFHPE 177
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 2.92e-11

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: 57.60  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNLKSVTG---AFKRIGLEAVV-------SRDEKVIREAKGIVLPGVGTFPTAMKNLERfhLVELLKERKEA 71
Cdd:cd03128     1 VAVLLFGGSEELELASpldALREAGAEVDVvspdggpVESDVDLDDYDGLILPGGPGTPDDLAWDEA--LLALLREAAAA 78

                          90
                  ....*....|....
gi 1473345100  72 GIPILGICLGMQIL 85
Cdd:cd03128    79 GKPVLGICLGAQLL 92
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 60-196 3.13e-10

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: 56.87  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  60 HLVELLKERKEAGIPILGICLGMQILfekgyeveeTKGLGfipGYVSYMdidEKIPHMGWNQLHKTQD---HLLLKYVHE 136
Cdd:cd01741    69 KLKELIRQALAAGKPVLGICLGHQLL---------ARALG---GKVGRN---PKGWEIGWFPVTLTEAgkaDPLFAGLPD 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1473345100 137 NEDVYFVHSYMAHVSDEN--LAAYSDYgsTKVTALVQNGNVMGCQFHPEKSgkvgqnILRAF 196
Cdd:cd01741   134 EFPVFHWHGDTVVELPPGavLLASSEA--CPNQAFRYGDRALGLQFHPEER------LLRNF 187
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 2-183 2.08e-09

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: 54.46  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYN---VGNLKSVtgaFKRIGLEAVVSR------DEKVIREAKGIVL-PGVGTfPTAMKNleRFHLVELLKERkea 71
Cdd:cd01743     1 ILLIDNYdsfTYNLVQY---LRELGAEVVVVRndeitlEELELLNPDAIVIsPGPGH-PEDAGI--SLEIIRALAGK--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  72 gIPILGICLGMQILFEK-GYEVEETKglgfipgyvsymdideKIPHMGWNQLHkTQDHLLLKYVHENEDVYFVHSYMAHV 150
Cdd:cd01743    72 -VPILGVCLGHQAIAEAfGGKVVRAP----------------EPMHGKTSEIH-HDGSGLFKGLPQPFTVGRYHSLVVDP 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1473345100 151 SDENLaaysdygSTKVTALVQNGNVM----------GCQFHPE 183
Cdd:cd01743   134 DPLPD-------LLEVTASTEDGVIMalrhrdlpiyGVQFHPE 169
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 18-183 5.55e-08

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: 50.60  E-value: 5.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  18 AFKRIGLEAVVSRDEKVIREAKGIVLPGVGTfpTAM-KNLERFHLVELLKERKEAGIPILGICLGMQILFEKGYEVEETK 96
Cdd:cd01749    16 ALERLGVEVIEVRTPEDLEGIDGLIIPGGES--TTIgKLLRRTGLLDPLREFIRAGKPVFGTCAGLILLAKEVEDQGGQP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  97 GLGFipgyvsyMDI-DEKiphmgwN----QLHKTQDHLLLKYVHENE-DVYFVHS-YMAHV-SDENLAAYSDygstKVTA 168
Cdd:cd01749    94 LLGL-------LDItVRR------NafgrQVDSFEADLDIPGLGLGPfPAVFIRApVIEEVgPGVEVLAEYD----GKIV 156

                         170
                  ....*....|....*
gi 1473345100 169 LVQNGNVMGCQFHPE 183
Cdd:cd01749   157 AVRQGNVLATSFHPE 171
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
18-201 9.05e-08

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 50.16  E-value: 9.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  18 AFKRIGLEAVVSRDEKVIREAKGIVLPGvGTfPTAM-KNLERFHLVELLKERKEAGIPILGICLGMqILFEKGYEVEETK 96
Cdd:PRK13525   19 ALEALGAEAVEVRRPEDLDEIDGLILPG-GE-STTMgKLLRDFGLLEPLREFIASGLPVFGTCAGM-ILLAKEIEGYEQE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  97 GLGFipgyvsyMDIDEKIPHMGwNQLHKTQDHLLLKYVHENEDVYFVHS-YMAHVSD--ENLAAYSDygstKVTAlVQNG 173
Cdd:PRK13525   96 HLGL-------LDITVRRNAFG-RQVDSFEAELDIKGLGEPFPAVFIRApYIEEVGPgvEVLATVGG----RIVA-VRQG 162

                         170       180
                  ....*....|....*....|....*...
gi 1473345100 174 NVMGCQFHPEKSGKVgqNILRAFKEMVE 201
Cdd:PRK13525  163 NILATSFHPELTDDT--RVHRYFLEMVK 188
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 22-141 1.38e-06

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: 46.86  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  22 IGLEAVVSRDEKVIREAKGIVLPGVGTFPTAMKNLERFHLVELLKERKEAGIPILGICLGMQILFEK---GYEVE---ET 95
Cdd:cd01750    22 PGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGICGGYQMLGKYivdPEGVEgpgEI 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1473345100  96 KGLGFIPGYVSYMD-------------IDEKIP------HMGWNQLHKTQDHLLLKYVHENEDVY 141
Cdd:cd01750   102 EGLGLLDVETEFGPekttrrvtgrldeEGEGGEvtgyeiHSGRTTLGDGARPLGKGYGNNGEDGT 166
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 2-183 3.73e-06

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: 45.41  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIID------YNVGNLksvtgaFKRIGLEAVVSRDEKV----IREAK--GIVL-PGVGTfPTAMKNLerfhlVELLKER 68
Cdd:COG0512     1 ILLIDnydsftYNLVQY------LGELGAEVVVVRNDEItleeIEALApdGIVLsPGPGT-PEEAGIS-----LEVIRAF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  69 KeAGIPILGICLGMQILFE-KGYEVEETKGLgfIPGYVSYMDIDekiphmgwnqlhktqDHLLLKYVHENEDV--YfvHS 145
Cdd:COG0512    69 A-GKIPILGVCLGHQAIGEaFGGKVVRAPEP--MHGKTSPITHD---------------GSGLFAGLPNPFTAtrY--HS 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1473345100 146 YMahVSDENLAAysdygSTKVTALVQNGNVM----------GCQFHPE 183
Cdd:COG0512   129 LV--VDRETLPD-----ELEVTAWTEDGEIMgirhrelpieGVQFHPE 169
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
27-105 4.76e-06

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 45.31  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  27 VVSRDEKVIREAKGIVLPGvgTFPT-AMKNLERFH-LVELLKERKEAGIPILGICLGMQILFEK--GYEVEETKGLGFIP 102
Cdd:pfam07685  32 VPLPDESLGPDADLIILPG--GKPTiQDLALLRNSgMDEAIKEAAEDGGPVLGICGGYQMLGETieDPEGVRIEGLGLLD 109


                  ...
gi 1473345100 103 GYV 105
Cdd:pfam07685 110 IET 112
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 18-96 5.06e-06

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 45.26  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  18 AFKR------IGLEAVVSRDEKVIREAKGIVLPGvGTFPTAMKNLERFHLVELLKERKEAGIPILGICLGMqILFEKGY- 90
Cdd:PRK13527   18 ALKRaldelgIDGEVVEVRRPGDLPDCDALIIPG-GESTTIGRLMKREGILDEIKEKIEEGLPILGTCAGL-ILLAKEVg 95


                  ....*...
gi 1473345100  91 --EVEETK 96
Cdd:PRK13527   96 ddRVTKTE 103
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 18-89 6.52e-05

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 42.39  E-value: 6.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1473345100  18 AFKRIGLEAVVSRDEKVIREAKGIVLPGVGTfpTAMKNL-ERFHLVELLKERKEAGIPILGICLGMQILFEKG 89
Cdd:PLN02832   19 ALRRLGVEAVEVRKPEQLEGVSGLIIPGGES--TTMAKLaERHNLFPALREFVKSGKPVWGTCAGLIFLAERA 89
guaA PRK00074
GMP synthase; Reviewed
 70-196 1.28e-04

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 41.96  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  70 EAGIPILGICLGMQILfekgyeveeTKGLGfipGYVSYMDIDEkiphMGWNQLHKTQDHLLLKYVHENEDVyfvhsYMAH 149
Cdd:PRK00074   73 ELGVPVLGICYGMQLM---------AHQLG---GKVERAGKRE----YGRAELEVDNDSPLFKGLPEEQDV-----WMSH 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1473345100 150 vSDENLAAYSDY---GSTKVT--ALVQN--GNVMGCQFHPEksgkV-----GQNILRAF 196
Cdd:PRK00074  132 -GDKVTELPEGFkviASTENCpiAAIANeeRKFYGVQFHPE----VthtpqGKKLLENF 185
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 63-85 1.52e-04

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 41.02  E-value: 1.52e-04
                          10        20
                  ....*....|....*....|...
gi 1473345100  63 ELLKERKEAGIPILGICLGMQIL 85
Cdd:cd01745    91 ALLRAALERGKPILGICRGMQLL 113
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 36-196 1.84e-04

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 40.76  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  36 REAKGIVLPGvGTFPTAMKNLERfhlveLLKERKEAGIPILGICLGMQILfekgyeveeTKGLGfipGYVSYMDIDEkip 115
Cdd:TIGR00888  40 KNPKGIILSG-GPSSVYAENAPR-----ADEKIFELGVPVLGICYGMQLM---------AKQLG---GEVGRAEKRE--- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100 116 hMGWNQLHKTQDHLLLKYVHENEDVyfvhsYMAHvSDENLA--------AYSDygSTKVTALVQNGN-VMGCQFHPE-KS 185
Cdd:TIGR00888  99 -YGKAELEILDEDDLFRGLPDESTV-----WMSH-GDKVKElpegfkvlATSD--NCPVAAMAHEEKpIYGVQFHPEvTH 169

                         170
                  ....*....|.
gi 1473345100 186 GKVGQNILRAF 196
Cdd:TIGR00888 170 TEYGNELLENF 180
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 63-85 2.63e-04

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: 40.54  E-value: 2.63e-04
                          10        20
                  ....*....|....*....|...
gi 1473345100  63 ELLKERKEAGIPILGICLGMQIL 85
Cdd:COG2071    87 ALIRAALERGKPVLGICRGMQLL 109
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
60-85 4.25e-04

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 40.06  E-value: 4.25e-04
                          10        20
                  ....*....|....*....|....*.
gi 1473345100  60 HLVELLKERKEAGIPILGICLGMQIL 85
Cdd:PRK12564  236 YAIEMIRELLEKKIPIFGICLGHQLL 261
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 18-103 4.28e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 39.91  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  18 AFKRIGLEA--VVSRD----EKVIREAKGIVLPGvGtF---------------PTAMKNLERFHlvellkerkEAGIPIL 76
Cdd:cd01740    18 AFELAGFEAedVWHNDllagRKDLDDYDGVVLPG-G-FsygdylragaiaaasPLLMEEVKEFA---------ERGGLVL 86

                          90       100
                  ....*....|....*....|....*..
gi 1473345100  77 GICLGMQILFEkgyeveetkgLGFIPG 103
Cdd:cd01740    87 GICNGFQILVE----------LGLLPG 103
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 18-103 5.09e-04

Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439817 [Multi-domain]  Cd Length: 236  Bit Score: 39.66  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  18 AFKRIGLEAV---VSRDEKVIREAKGIVLPGvG-------------TFPTAMKNLERFhlvellkerKEAGIPILGICLG 81
Cdd:COG0047    20 AFERAGAEAEdvwHSDLRTDLDDFDGLVLPG-GfsygdylragaiaAFSPIMDAVREF---------ARRGGLVLGICNG 89

                          90       100
                  ....*....|....*....|..
gi 1473345100  82 MQILFEkgyeveetkgLGFIPG 103
Cdd:COG0047    90 FQILTE----------LGLLPG 101
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 62-85 6.22e-04

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: 39.62  E-value: 6.22e-04
                          10        20
                  ....*....|....*....|....
gi 1473345100  62 VELLKERKEAGIPILGICLGMQIL 85
Cdd:COG0505   237 IETIRELLGKGIPIFGICLGHQLL 260
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 64-85 1.07e-03

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: 38.78  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|..
gi 1473345100  64 LLKERKEAGIPILGICLGMQIL 85
Cdd:pfam07722  97 LIRAALARGKPILGICRGFQLL 118
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 30-102 1.46e-03

Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441101 [Multi-domain]  Cd Length: 493  Bit Score: 38.89  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  30 RDEKVIREAKGIVLPGVgtfptamKN----LERFH---LVELLKERKEAGIPILGICLGMQILFEK-----GYE--VEET 95
Cdd:COG1492   283 RPPEELGDADLVILPGS-------KNtiadLAWLResgLDDAIRAHARRGGPVLGICGGYQMLGRRiadpdGVEggAGEV 355


                  ....*..
gi 1473345100  96 KGLGFIP 102
Cdd:COG1492   356 PGLGLLP 362
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 1-85 1.58e-03

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 37.80  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIID------YN----VGNLksvtgafkriGLEAVVSR-DEKVIREAK-----GIVL-PGVGTfPTAMKNLerfhlVE 63
Cdd:PRK05670    1 MILLIDnydsftYNlvqyLGEL----------GAEVVVYRnDEITLEEIEalnpdAIVLsPGPGT-PAEAGIS-----LE 64

                          90       100
                  ....*....|....*....|..
gi 1473345100  64 LLKERKEaGIPILGICLGMQIL 85
Cdd:PRK05670   65 LIREFAG-KVPILGVCLGHQAI 85
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 52-104 1.75e-03

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


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 38.23  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1473345100  52 AMKNLERFHlvELLKERKEAGIPILGICLGMQiLFEKGYEV---EETKGLGFIPGY 104
Cdd:COG3442    67 VADDLLRIK--DALRAAIEDGVPVLAICGGYQ-LLGHYYETadgERIPGLGILDVY 119
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 65-183 2.88e-03

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 37.25  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  65 LKERKeagiPILGICLGMQILfekgyeveeTKGLGfipGYVSymdidekiPH------MGWNQLHKT-QDHLLLkyvHEN 137
Cdd:PRK06490   83 LKENK----PFLGICLGAQML---------ARHLG---ARVA--------PHpdgrveIGYYPLRPTeAGRALM---HWP 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1473345100 138 EDVYFVHS--YMAHVSDENLAAYSDYgstKVTALVQNGNVMGCQFHPE 183
Cdd:PRK06490  136 EMVYHWHRegFDLPAGAELLATGDDF---PNQAFRYGDNAWGLQFHPE 180
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 2-85 3.17e-03

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: 37.09  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIIDYNVGNlkSVTGAFKRIGLEAVV-----SRDEKVIREAKGIVLP-GVGTfPTAMKnlerfHLVELLKERKEAGIPI 75
Cdd:cd01744     1 VVVIDFGVKH--NILRELLKRGCEVTVvpyntDAEEILKLDPDGIFLSnGPGD-PALLD-----EAIKTVRKLLGKKIPI 72

                          90
                  ....*....|
gi 1473345100  76 LGICLGMQIL 85
Cdd:cd01744    73 FGICLGHQLL 82
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 61-84 3.17e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 37.23  E-value: 3.17e-03
                          10        20
                  ....*....|....*....|....
gi 1473345100  61 LVELLKERKEAGIPILGICLGMQI 84
Cdd:PRK07053   72 EIALLRQRLAAGLPTLGICLGAQL 95
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
2-83 3.26e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 37.34  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   2 IVIID-YN--VGNLKSVTGafkRIGLEAVVSR--------DEKVIREAKGIVL-PGVGTfPtamknlERFHL-VELLKER 68
Cdd:PRK07765    3 ILVVDnYDsfVFNLVQYLG---QLGVEAEVWRnddprladEAAVAAQFDGVLLsPGPGT-P------ERAGAsIDMVRAC 72

                          90
                  ....*....|....*
gi 1473345100  69 KEAGIPILGICLGMQ 83
Cdd:PRK07765   73 AAAGTPLLGVCLGHQ 87
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-85 3.38e-03

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 36.75  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100   1 MIVIID----YNVGNLKSVtgafKRIGLEA-VVSRD---EKVIREAKGIVLPGvGtfPTamknLERF-HLVELLKErkeA 71
Cdd:PRK00758    1 KIVVVDnggqYNHLIHRTL----RYLGVDAkIIPNTtpvEEIKAFEDGLILSG-G--PD----IERAgNCPEYLKE---L 66

                          90
                  ....*....|....
gi 1473345100  72 GIPILGICLGMQIL 85
Cdd:PRK00758   67 DVPILGICLGHQLI 80
PRK00784 PRK00784
cobyric acid synthase;
65-102 4.15e-03

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 37.37  E-value: 4.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1473345100  65 LKERKEAGIPILGICLGMQILFEK---GYEVE----ETKGLGFIP 102
Cdd:PRK00784  318 IRAHARRGGPVLGICGGYQMLGRRiadPDGVEgapgSVEGLGLLD 362
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 31-84 6.00e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 36.38  E-value: 6.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1473345100  31 DEKVIREAKGIVLPGvGtFPtaMKNLErfHLVELLKERKEAGIPILGICLGMQI 84
Cdd:cd01746    49 AEEALKGADGILVPG-G-FG--IRGVE--GKILAIKYARENNIPFLGICLGMQL 96
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 70-85 6.22e-03

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: 35.97  E-value: 6.22e-03
                          10
                  ....*....|....*.
gi 1473345100  70 EAGIPILGICLGMQIL 85
Cdd:cd01742    68 ELGVPVLGICYGMQLI 83
PRK13566 PRK13566
anthranilate synthase component I;
19-87 7.06e-03

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 36.82  E-value: 7.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1473345100  19 FKRIGLEAVVSR---DEKVIREAKG--IVL-PGVGTfPtamknlERFHLVELLKERKEAGIPILGICLGMQILFE 87
Cdd:PRK13566  546 FRQTGAEVTTVRygfAEEMLDRVNPdlVVLsPGPGR-P------SDFDCKATIDAALARNLPIFGVCLGLQAIVE 613
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 18-90 7.08e-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: 35.70  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  18 AFKRIGLEA-VVSRDEKVIREAKG-------------------IVLPGVGTFPTAMKNLERfhLVELLKERKEAGIPILG 77
Cdd:pfam01965  22 VLRRAGIKVtVVSVDGGEVKGSRGvkvtvdaslddvkpddydaLVLPGGRAGPERLRDNEK--LVEFVKDFYEKGKPVAA 99

                          90
                  ....*....|...
gi 1473345100  78 ICLGMQILFEKGY 90
Cdd:pfam01965 100 ICHGPQVLAAAGV 112
pyrG PRK05380
CTP synthetase; Validated
 70-84 8.71e-03

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 36.54  E-value: 8.71e-03
                          10
                  ....*....|....*
gi 1473345100  70 EAGIPILGICLGMQI 84
Cdd:PRK05380  370 ENNIPFLGICLGMQL 384
PepE COG3340
Peptidase E [Amino acid transport and metabolism];
18-103 9.58e-03

Peptidase E [Amino acid transport and metabolism];


Pssm-ID: 442569 [Multi-domain]  Cd Length: 212  Bit Score: 35.56  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473345100  18 AFKRIGLEAVV--------SRDEKVIREAKGIVLPGVGTFpTAMKNLERFHLVELLKERKEAGIPILGICLGMQILFEKG 89
Cdd:COG3340    54 AFSKLGVKVSVlhlfsptfEDPVEALLEADVIFVGGGNTF-NLLALWREHGLDDILREAVEAGTVYAGVSAGSNCWFPTI 132

                          90       100
                  ....*....|....*....|.
gi 1473345100  90 -------YEVEETKGLGFIPG 103
Cdd:COG3340   133 rttndgpPPLRSFDGLGLVPF 153
 
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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