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Conserved domains on  [gi|1934263381|ref|WP_195478408|]
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imidazole glycerol phosphate synthase subunit HisH [Ruminococcus sp. D55t1_190419_H1]

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
 1-205 9.42e-129

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 360.60  E-value: 9.42e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICL 80
Cdd:PRK13141    1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDETPGVEGLGLLKGKIVKIPPAQGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIVKA 160
Cdd:PRK13141   81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADPCDEEYVAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKLGKEA 205
Cdd:PRK13141  161 TTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-205 9.42e-129

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 360.60  E-value: 9.42e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICL 80
Cdd:PRK13141    1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDETPGVEGLGLLKGKIVKIPPAQGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIVKA 160
Cdd:PRK13141   81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADPCDEEYVAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKLGKEA 205
Cdd:PRK13141  161 TTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-196 9.75e-120

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: 337.40  E-value: 9.75e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICL 80
Cdd:COG0118     2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDETPGVEGLGLLKGKIVKIPPAqGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIVKA 160
Cdd:COG0118    82 GMQLLFERSEENGDTEGLGLIPGEVVRFPAS-DLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDDPEDVVA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILE 196
Cdd:COG0118   161 TTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-198 2.76e-117

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: 331.38  E-value: 2.76e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLG 81
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  82 LQLLFESSDETPGVEGLGLLKGKIVKIPPAQGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIVKAT 161
Cdd:cd01748    81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDPDYILAT 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1934263381 162 TQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENF 198
Cdd:cd01748   161 TDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNF 197
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-201 5.82e-91

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: 264.57  E-value: 5.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLG 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  82 LQLLFESSDETPGVEGLGLLKGKIVKIPPAqglKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEElEIVKAT 161
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR---KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEE-EAVLAY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1934263381 162 TQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKL 201
Cdd:TIGR01855 157 ADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase pfam00117
Glutamine amidotransferase class-I;
4-198 4.84e-32

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 114.26  E-value: 4.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   4 IIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADK------VILPGVGSFGDAmnnlnkFGLVPVIKEITDKGTPFLG 77
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEenpdgiILSGGPGSPGAA------GGAIEAIREARELKIPILG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  78 ICLGLQLLFESsdetpgvegLGllkGKIVKIPpaqglKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELE- 156
Cdd:pfam00117  76 ICLGHQLLALA---------FG---GKVVKAK-----KFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPd 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1934263381 157 --IVKATTQYGVTIHASVEKDN-IFACQFHPEKSSK-YGLKILENF 198
Cdd:pfam00117 139 glEVTATSENDGTIMGIRHKKLpIFGVQFHPESILTpHGPEILFNF 184
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-205 9.42e-129

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 360.60  E-value: 9.42e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICL 80
Cdd:PRK13141    1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDETPGVEGLGLLKGKIVKIPPAQGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIVKA 160
Cdd:PRK13141   81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYYADPCDEEYVAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKLGKEA 205
Cdd:PRK13141  161 TTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-196 9.75e-120

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: 337.40  E-value: 9.75e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICL 80
Cdd:COG0118     2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDETPGVEGLGLLKGKIVKIPPAqGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIVKA 160
Cdd:COG0118    82 GMQLLFERSEENGDTEGLGLIPGEVVRFPAS-DLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDDPEDVVA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILE 196
Cdd:COG0118   161 TTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-198 2.76e-117

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: 331.38  E-value: 2.76e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLG 81
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  82 LQLLFESSDETPGVEGLGLLKGKIVKIPPAQGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIVKAT 161
Cdd:cd01748    81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDPDYILAT 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1934263381 162 TQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENF 198
Cdd:cd01748   161 TDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNF 197
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-201 1.03e-105

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 302.17  E-value: 1.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICL 80
Cdd:PRK13181    1 MIAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKQPVLGICL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDEtPGVEGLGLLKGKIVKIPPAqGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIVKA 160
Cdd:PRK13181   81 GMQLLFESSEE-GNVKGLGLIPGDVKRFRSE-PLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHSYYVPCEDPEDVLA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKL 201
Cdd:PRK13181  159 TTEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAEL 199
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-204 1.89e-95

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 276.36  E-value: 1.89e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFglVPVIKEITDKGTPFLGICL 80
Cdd:PRK13143    2 MIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLSPL--RDVILEAARSGKPFLGICL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDETPGVEGLGLLKGKIVKIPPaqGLKIPHMGWNSLHLQNDGRLFKGIpEETYVYFVHSYYLQAEELEIVKA 160
Cdd:PRK13143   80 GMQLLFESSEEGGGVRGLGLFPGRVVRFPA--GVKVPHMGWNTVKVVKDCPLFEGI-DGEYVYFVHSYYAYPDDEDYVVA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKLGKE 204
Cdd:PRK13143  157 TTDYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVELIKR 200
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-198 3.30e-94

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 273.20  E-value: 3.30e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAGNIKSVEKALHYLG--EETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEI-TDKGTPFLGI 78
Cdd:PRK13146    4 VAIIDYGSGNLRSAAKALERAGagADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAvLAAGRPFLGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  79 CLGLQLLFESSDETPGVEGLGLLKGKIVKIPPA-QGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEI 157
Cdd:PRK13146   84 CVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDgPALKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVHSYYAQPANPAD 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934263381 158 VKATTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENF 198
Cdd:PRK13146  164 VVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNF 204
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-201 5.82e-91

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: 264.57  E-value: 5.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLG 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  82 LQLLFESSDETPGVEGLGLLKGKIVKIPPAqglKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEElEIVKAT 161
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR---KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEE-EAVLAY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1934263381 162 TQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKL 201
Cdd:TIGR01855 157 ADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-198 1.37e-79

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 235.91  E-value: 1.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDkgtPFLGICL 80
Cdd:PRK13170    2 NVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQ---PVLGICL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDETPGVEGLGLLKGKIVKIpPAQGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELEIvkA 160
Cdd:PRK13170   79 GMQLLGERSEESGGVDCLGIIDGPVKKM-TDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEYTI--A 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENF 198
Cdd:PRK13170  156 QCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNF 193
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 4-198 1.35e-73

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 231.52  E-value: 1.35e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   4 IIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLGLQ 83
Cdd:PLN02617   11 LLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRPFLGICLGLQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  84 LLFESSDETPGVEGLGLLKGKIVKIPPAQGLKIPHMGWNSLHLQNDGRLFKGIPEEtYVYFVHSYY--LQAEELEIVKAT 161
Cdd:PLN02617   91 LLFESSEENGPVEGLGVIPGVVGRFDSSNGLRVPHIGWNALQITKDSELLDGVGGR-HVYFVHSYRatPSDENKDWVLAT 169

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1934263381 162 TQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENF 198
Cdd:PLN02617  170 CNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRF 206
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-201 5.08e-73

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 219.33  E-value: 5.08e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKE-ITDKGTPFLGIC 79
Cdd:PRK13152    1 MIALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEqVLVQKKPILGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  80 LGLQLLFESSDETPGVEGLGLLKGKIVKIPPAQGLKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEElEIVK 159
Cdd:PRK13152   81 LGMQLFLERGYEGGVCEGLGFIEGEVVKFEEDLNLKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSFYVKCKD-EFVS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1934263381 160 ATTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKL 201
Cdd:PRK13152  160 AKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL 201
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 2-200 3.87e-61

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 189.71  E-value: 3.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLG 81
Cdd:CHL00188    4 IGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAEGNPFIGICLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  82 LQLLFESSDEtpGVE-GLGLLKGKIVKIPPAQGLKIPHMGWNSLHLQN------DGRLFKGIPEETYVYFVHSYYLQAEE 154
Cdd:CHL00188   84 LHLLFETSEE--GKEeGLGIYKGQVKRLKHSPVKVIPHMGWNRLECQNsecqnsEWVNWKAWPLNPWAYFVHSYGVMPKS 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1934263381 155 LEIVKATTQYG-VTIHASVEKDNIFACQFHPEKSSKYGLKILENFAK 200
Cdd:CHL00188  162 QACATTTTFYGkQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFMK 208
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-198 6.18e-61

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 188.96  E-value: 6.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICL 80
Cdd:PRK14004    1 MIAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVESGKPLFGICI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDET----PG--VEGLGLLKGKIVKIpPAQGLKIPHMGWNSLHL--QNDGRLFKGIPEETYVYFVHSYY-LQ 151
Cdd:PRK14004   81 GFQILFESSEETnqgtKKeqIEGLGYIKGKIKKF-EGKDFKVPHIGWNRLQIrrKDKSKLLKGIGDQSFFYFIHSYRpTG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1934263381 152 AEELEIVKATTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENF 198
Cdd:PRK14004  160 AEGNAITGLCDYYQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENF 206
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 2.63e-59

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 184.26  E-value: 2.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKgtPFLGICL 80
Cdd:PRK13142    1 MIVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNTDK--KMIGICL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  81 GLQLLFESSDETpGVEGLGLLKGKIVKIPPAQglKIPHMGWNSLH-----LQNDgrlfkgipeetyVYFVHSYylQAEEL 155
Cdd:PRK13142   79 GMQLMYEHSDEG-DASGLGFIPGNISRIQTEY--PVPHLGWNNLVskhpmLNQD------------VYFVHSY--QAPMS 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1934263381 156 EIVKATTQYGVTIHASVEKDNIFACQFHPEKSSKYGLKILENFAKLG 202
Cdd:PRK13142  142 ENVIAYAQYGADIPAIVQFNNYIGIQFHPEKSGTYGLQILRQAIQGG 188
GATase pfam00117
Glutamine amidotransferase class-I;
4-198 4.84e-32

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 114.26  E-value: 4.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   4 IIDYDAGNIKSVEKALHYLGEETVVSRDPQVLLNADK------VILPGVGSFGDAmnnlnkFGLVPVIKEITDKGTPFLG 77
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEenpdgiILSGGPGSPGAA------GGAIEAIREARELKIPILG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  78 ICLGLQLLFESsdetpgvegLGllkGKIVKIPpaqglKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEELE- 156
Cdd:pfam00117  76 ICLGHQLLALA---------FG---GKVVKAK-----KFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLPd 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1934263381 157 --IVKATTQYGVTIHASVEKDN-IFACQFHPEKSSK-YGLKILENF 198
Cdd:pfam00117 139 glEVTATSENDGTIMGIRHKKLpIFGVQFHPESILTpHGPEILFNF 184
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 4-198 1.27e-19

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: 82.20  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   4 IID-YDA--GNIKSVekaLHYLGEETVVSR------DPQVLLNADKVIL-PGVGSFGDAMNnlnkfgLVPVIKEITdKGT 73
Cdd:cd01743     3 LIDnYDSftYNLVQY---LRELGAEVVVVRndeitlEELELLNPDAIVIsPGPGHPEDAGI------SLEIIRALA-GKV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  74 PFLGICLGLQLLFESsdetpgvegLGllkGKIVKIPPaqglkiPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAE 153
Cdd:cd01743    73 PILGVCLGHQAIAEA---------FG---GKVVRAPE------PMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPD 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1934263381 154 ELE---IVKATTQYGVtIHA-SVEKDNIFACQFHPEkS--SKYGLKILENF 198
Cdd:cd01743   135 PLPdllEVTASTEDGV-IMAlRHRDLPIYGVQFHPE-SilTEYGLRLLENF 183
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 22-201 4.78e-14

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 67.46  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  22 LGEETVVSRDPQVL------LNADKVIL-PGVGSFGDAMNnlnkfgLVPVIKEITDKgTPFLGICLGLQLLfessdetpg 94
Cdd:PRK05670   22 LGAEVVVYRNDEITleeieaLNPDAIVLsPGPGTPAEAGI------SLELIREFAGK-VPILGVCLGHQAI--------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  95 VEGLGllkGKIVKIPpaqglKIPHmGWNSLHLQNDGRLFKGIPEETYV--YfvHSyyLQAEELEI-----VKATTQYGVT 167
Cdd:PRK05670   86 GEAFG---GKVVRAK-----EIMH-GKTSPIEHDGSGIFAGLPNPFTVtrY--HS--LVVDRESLpdcleVTAWTDDGEI 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1934263381 168 IHASVEKDNIFACQFHPEkS--SKYGLKILENFAKL 201
Cdd:PRK05670  153 MGVRHKELPIYGVQFHPE-SilTEHGHKLLENFLEL 187
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 20-204 1.70e-13

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: 65.83  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  20 HYLGE---ETVVSRDPQV------LLNADKVIL-PGVGSFGDAMNnlnkfgLVPVIKEITDKgTPFLGICLGLQLLfess 89
Cdd:COG0512    16 QYLGElgaEVVVVRNDEItleeieALAPDGIVLsPGPGTPEEAGI------SLEVIRAFAGK-IPILGVCLGHQAI---- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  90 detpgVEGLGllkGKIVKIPpaqglKIPHmGWNSLHLQNDGRLFKGIPEETYV--YfvHSYYLQAE----ELEIVkATTQ 163
Cdd:COG0512    85 -----GEAFG---GKVVRAP-----EPMH-GKTSPITHDGSGLFAGLPNPFTAtrY--HSLVVDREtlpdELEVT-AWTE 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1934263381 164 YGVtIHA-SVEKDNIFACQFHPEkS--SKYGLKILENFAKLGKE 204
Cdd:COG0512   148 DGE-IMGiRHRELPIEGVQFHPE-SilTEHGHQLLANFLELAGE 189
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 1-199 1.81e-12

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: 63.03  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGII----DYDAGNIKSVEKALHYLGEETVVSR--DPQVLLNADK----VILpgvGSFGDAMNNLNKF--GLVPVIKEI 68
Cdd:cd01741     1 RILILqhdtPEGPGLFEDLLREAGAETIEIDVVDvyAGELLPDLDDydglVIL---GGPMSVDEDDYPWlkKLKELIRQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  69 TDKGTPFLGICLGLQLLfessdetpgVEGLGllkGKIVKIPPAQGlkiphMGWNSLHLQNDGR---LFKGIPEETYVYFV 145
Cdd:cd01741    78 LAAGKPVLGICLGHQLL---------ARALG---GKVGRNPKGWE-----IGWFPVTLTEAGKadpLFAGLPDEFPVFHW 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934263381 146 HSyylqaeelEIVKATTQyGVTIHASVEK---------DNIFACQFHPEKsskyglKILENFA 199
Cdd:cd01741   141 HG--------DTVVELPP-GAVLLASSEAcpnqafrygDRALGLQFHPEE------RLLRNFL 188
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 64-185 1.28e-10

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: 58.42  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  64 VIKEITDKGTPFLGICLGLQLLfessdetpgVEGLGllkGKIVKIPpaqglkIPHMGWNSLHLQNDGRLFKGIPEETYVY 143
Cdd:COG0518    74 LIREAFELGKPVLGICYGAQLL---------AHALG---GKVEPGP------GREIGWAPVELTEADPLFAGLPDEFTVW 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1934263381 144 FVHSYylQAEEL----EIVkATTQyGVTIHASVEKDNIFACQFHPE 185
Cdd:COG0518   136 MSHGD--TVTELpegaEVL-ASSD-NCPNQAFRYGRRVYGVQFHPE 177
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-86 1.63e-09

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 53.37  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAGN---IKSVEKALHYLGEETVV-------SRDPQVLLNADKVILPGvgSFGDAMNNLNKFGLVPVIKEITDK 71
Cdd:cd01653     1 VAVLLFPGFEeleLASPLDALREAGAEVDVvspdggpVESDVDLDDYDGLILPG--GPGTPDDLARDEALLALLREAAAA 78

                          90
                  ....*....|....*
gi 1934263381  72 GTPFLGICLGLQLLF 86
Cdd:cd01653    79 GKPILGICLGAQLLV 93
PRK13566 PRK13566
anthranilate synthase component I;
22-197 1.94e-09

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 56.46  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  22 LGEETVVSR---DPQVL--LNADKVIL-PGVGSFGDamnnlnkFGLVPVIKEITDKGTPFLGICLGLQLLFESSDETPGV 95
Cdd:PRK13566  549 TGAEVTTVRygfAEEMLdrVNPDLVVLsPGPGRPSD-------FDCKATIDAALARNLPIFGVCLGLQAIVEAFGGELGQ 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  96 eglgllkgkivkippaqgLKIPHMGWNS-LHLQNDGRLFKGIPEETYVYFVHSYYLQAEELE---IVKATTQYGVTIHAS 171
Cdd:PRK13566  622 ------------------LAYPMHGKPSrIRVRGPGRLFSGLPEEFTVGRYHSLFADPETLPdelLVTAETEDGVIMAIE 683

                         170       180       190
                  ....*....|....*....|....*....|
gi 1934263381 172 VEKDNIFACQFHPEK----SSKYGLKILEN 197
Cdd:PRK13566  684 HKTLPVAAVQFHPESimtlGGDVGLRIIEN 713
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 2-101 2.35e-09

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: 54.56  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDY-DAGNIKSVEKALHYLGEETVVSRDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICL 80
Cdd:cd01750     1 IAVIRYpDISNFTDLDPLAREPGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGICG 80

                          90       100
                  ....*....|....*....|....*..
gi 1934263381  81 GLQLLFESSD-----ETPG-VEGLGLL 101
Cdd:cd01750    81 GYQMLGKYIVdpegvEGPGeIEGLGLL 107
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 7.14e-09

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 51.05  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAGN---IKSVEKALHYLGEETVV-------SRDPQVLLNADKVILPGVGSFGDAMNNLnkFGLVPVIKEITDK 71
Cdd:cd03128     1 VAVLLFGGSEeleLASPLDALREAGAEVDVvspdggpVESDVDLDDYDGLILPGGPGTPDDLAWD--EALLALLREAAAA 78

                          90
                  ....*....|....
gi 1934263381  72 GTPFLGICLGLQLL 85
Cdd:cd03128    79 GKPVLGICLGAQLL 92
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 18-185 2.29e-07

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: 49.06  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  18 ALHYLGEETVVSRDPQVLLNADKVILPGVGSfGDAMNNLNKFGLVPVIKEITDKGTPFLGICLGLQLLFESSDETPGVEG 97
Cdd:cd01749    16 ALERLGVEVIEVRTPEDLEGIDGLIIPGGES-TTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLILLAKEVEDQGGQPL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  98 LGLLKGKIVKippaqglkiphmgwNSLHLQND---GRL-FKGIPEETY-VYFVHSYYLQaEELEIVKATTQYGVTIHAsV 172
Cdd:cd01749    95 LGLLDITVRR--------------NAFGRQVDsfeADLdIPGLGLGPFpAVFIRAPVIE-EVGPGVEVLAEYDGKIVA-V 158

                         170
                  ....*....|...
gi 1934263381 173 EKDNIFACQFHPE 185
Cdd:cd01749   159 RQGNVLATSFHPE 171
trpG CHL00101
anthranilate synthase component 2
 1-198 2.81e-07

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 48.96  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGIID-YDAGNIKSVekalHYLGE---ETVVSRDPQV------LLNADKVIL-PGVGSFGDAMNNLnkfglvPVIKEIT 69
Cdd:CHL00101    1 MILIIDnYDSFTYNLV----QSLGElnsDVLVCRNDEIdlskikNLNIRHIIIsPGPGHPRDSGISL------DVISSYA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  70 DKgTPFLGICLGLQLLFEssdetpgveglgLLKGKIVKIPPaqglkiPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYY 149
Cdd:CHL00101   71 PY-IPILGVCLGHQSIGY------------LFGGKIIKAPK------PMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLI 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1934263381 150 LQAE----ELEIVkATTQYGVtIHASVEKDN--IFACQFHPEKS-SKYGLKILENF 198
Cdd:CHL00101  132 IDPLnlpsPLEIT-AWTEDGL-IMACRHKKYkmLRGIQFHPESLlTTHGQQILRNF 185
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
36-205 5.66e-07

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 48.94  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  36 LNADKVIL-PGVGSFGDAMNNlnkfglVPVIKEITDKgTPFLGICLGLQLLFESsdetpgveglglLKGKIVKIPpaqgl 114
Cdd:PRK14607   43 LNPSHIVIsPGPGRPEEAGIS------VEVIRHFSGK-VPILGVCLGHQAIGYA------------FGGKIVHAK----- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381 115 KIPHMGWNSLHLQNDGrLFKGIPEETYVYFVHSYYLQAEELE---IVKATTQYGvTIHASVEKDN-IFACQFHPEK-SSK 189
Cdd:PRK14607   99 RILHGKTSPIDHNGKG-LFRGIPNPTVATRYHSLVVEEASLPeclEVTAKSDDG-EIMGIRHKEHpIFGVQFHPESiLTE 176

                         170
                  ....*....|....*.
gi 1934263381 190 YGLKILENFAKLGKEA 205
Cdd:PRK14607  177 EGKRILKNFLNYQREE 192
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 30-101 9.65e-07

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: 48.13  E-value: 9.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  30 RDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLGLQLL---------FESSDETpgVEGLGL 100
Cdd:COG1492   283 RPPEELGDADLVILPGSKNTIADLAWLRESGLDDAIRAHARRGGPVLGICGGYQMLgrriadpdgVEGGAGE--VPGLGL 360


                  .
gi 1934263381 101 L 101
Cdd:COG1492   361 L 361
PRK00784 PRK00784
cobyric acid synthase;
30-101 2.45e-05

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 43.92  E-value: 2.45e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934263381  30 RDPQVLLNADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLGLQLL-------FESSDETPGVEGLGLL 101
Cdd:PRK00784  283 RPGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRAHARRGGPVLGICGGYQMLgrriadpDGVEGAPGSVEGLGLL 361
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-103 3.68e-05

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 42.80  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   1 MIGII-------DYDagniksVEKAL-HYLGEETVV----SRDPQvllNADKVILPGVGSFGD-----AMNnlnkfGLVP 63
Cdd:PRK03619    2 KVAVIvfpgsncDRD------MARALrDLLGAEPEYvwhkETDLD---GVDAVVLPGGFSYGDylrcgAIA-----AFSP 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1934263381  64 VIKEI---TDKGTPFLGICLGLQLLFESsdetpgveglGLLKG 103
Cdd:PRK03619   68 IMKAVkefAEKGKPVLGICNGFQILTEA----------GLLPG 100
PRK06895 PRK06895
anthranilate synthase component II;
76-198 4.55e-05

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 42.42  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  76 LGICLGLQLLFEssdetpgveglgLLKGKIVKIPpaqglKIPHMGWNSLHLQNDGRLFKGIPEETYVYFVHSYYLQAEEL 155
Cdd:PRK06895   76 LGVCLGHQTLCE------------FFGGELYNLN-----NVRHGQQRPLKVRSNSPLFDGLPEEFNIGLYHSWAVSEENF 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1934263381 156 E---IVKATTQYGVTIHASVEKDNIFACQFHPEKS-SKYGLKILENF 198
Cdd:PRK06895  139 PtplEITAVCDENVVMAMQHKTLPIYGVQFHPESYiSEFGEQILRNW 185
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
18-106 6.73e-05

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 41.84  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  18 ALHYLGEETVV-SRDPQVLL--NADKVILPGVGSFGDAMNNLNKFGLVPVIKEITDKGTPFLGICLGLQLLFESSDETPG 94
Cdd:pfam07685  20 PLRYEPAVRVRfVPLPDESLgpDADLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGETIEDPEG 99

                          90
                  ....*....|....
gi 1934263381  95 V--EGLGLLKGKIV 106
Cdd:pfam07685 100 VriEGLGLLDIETV 113
PLN02347 PLN02347
GMP synthetase
 68-198 1.01e-04

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 42.36  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  68 ITDKGTPFLGICLGLQLLfessdetpgVEGLGllkGKIVkipPAQGLKIPHMgwnSLHLQNDGRLFKGIPEETY--VYFV 145
Cdd:PLN02347   82 CRERGVPVLGICYGMQLI---------VQKLG---GEVK---PGEKQEYGRM---EIRVVCGSQLFGDLPSGETqtVWMS 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1934263381 146 HSYYLQA--EELEIVKATTQYGVTIHASVEKdNIFACQFHPEKS-SKYGLKILENF 198
Cdd:PLN02347  144 HGDEAVKlpEGFEVVAKSVQGAVVAIENRER-RIYGLQYHPEVThSPKGMETLRHF 198
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 62-85 1.19e-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: 41.93  E-value: 1.19e-04
                          10        20
                  ....*....|....*....|....
gi 1934263381  62 VPVIKEITDKGTPFLGICLGLQLL 85
Cdd:COG0505   237 IETIRELLGKGIPIFGICLGHQLL 260
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
19-185 2.19e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 40.80  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  19 LHYLGEETVVSR--------DPQVLLNADKVIL-PGVGSFGDAmnnlnkfGL-VPVIKEITDKGTPFLGICLGLQLLFES 88
Cdd:PRK07765   20 LGQLGVEAEVWRnddprladEAAVAAQFDGVLLsPGPGTPERA-------GAsIDMVRACAAAGTPLLGVCLGHQAIGVA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  89 ----SDETPgveglGLLKGKIvkippaqglkiphmgwNSLHLQNDGrLFKGIPEETYVYFVHSYYLQAE----ELEiVKA 160
Cdd:PRK07765   93 fgatVDRAP-----ELLHGKT----------------SSVHHTGVG-VLAGLPDPFTATRYHSLTILPEtlpaELE-VTA 149

                         170       180
                  ....*....|....*....|....*
gi 1934263381 161 TTQYGVTIHASVEKDNIFACQFHPE 185
Cdd:PRK07765  150 RTDSGVIMAVRHRELPIHGVQFHPE 174
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 8-101 3.63e-04

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


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 40.16  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   8 DAGNIKSVEKALHYLGEETVVSR----DPQVLLNADKVILPGvGS---FGDAMNNLNKFGlvPVIKEITDKGTPFLGICL 80
Cdd:COG3442    17 DRGNVLALKRRAEWRGIDVEVVEvnpgDDLPFDDVDIVFIGG-GQdreQEIVADDLLRIK--DALRAAIEDGVPVLAICG 93

                          90       100
                  ....*....|....*....|....
gi 1934263381  81 GLQLL---FESSDETpGVEGLGLL 101
Cdd:COG3442    94 GYQLLghyYETADGE-RIPGLGIL 116
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 18-87 4.55e-04

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 40.08  E-value: 4.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934263381  18 ALHYLGEETVVSRDPQVLLNADKVILPGVGSfgDAMNNL-NKFGLVPVIKEITDKGTPFLGICLGLQLLFE 87
Cdd:PLN02832   19 ALRRLGVEAVEVRKPEQLEGVSGLIIPGGES--TTMAKLaERHNLFPALREFVKSGKPVWGTCAGLIFLAE 87
PLN02335 PLN02335
anthranilate synthase
 74-205 5.08e-04

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 39.78  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  74 PFLGICLGLQLLFESsdetpgveglglLKGKIVKIPPAqglkIPHMGWNSLHLQNDGR--LFKGIPEETYVYFVHSYYLQ 151
Cdd:PLN02335   93 PLFGVCMGLQCIGEA------------FGGKIVRSPFG----VMHGKSSPVHYDEKGEegLFSGLPNPFTAGRYHSLVIE 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934263381 152 -----AEELEIVkATTQYGVTIHASVEK-DNIFACQFHPEK-SSKYGLKILENFAKL--GKEA 205
Cdd:PLN02335  157 kdtfpSDELEVT-AWTEDGLIMAARHRKyKHIQGVQFHPESiITTEGKTIVRNFIKIieKKES 218
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 2-101 6.82e-04

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 39.10  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   2 IGIIDYDAG---NIKSVEKALHYLGE--ETVVSRDPQVLLNADKVILPG-----VGSFgdamnnLNKFGLVPVIKEITDK 71
Cdd:PRK13527    3 IGVLALQGDveeHIDALKRALDELGIdgEVVEVRRPGDLPDCDALIIPGgesttIGRL------MKREGILDEIKEKIEE 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1934263381  72 GTPFLGICLGLQLLF-ESSD---ETPGVEGLGLL 101
Cdd:PRK13527   77 GLPILGTCAGLILLAkEVGDdrvTKTEQPLLGLM 110
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
62-85 9.16e-04

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 39.29  E-value: 9.16e-04
                          10        20
                  ....*....|....*....|....
gi 1934263381  62 VPVIKEITDKGTPFLGICLGLQLL 85
Cdd:PRK12564  238 IEMIRELLEKKIPIFGICLGHQLL 261
PepE COG3340
Peptidase E [Amino acid transport and metabolism];
5-158 1.27e-03

Peptidase E [Amino acid transport and metabolism];


Pssm-ID: 442569 [Multi-domain]  Cd Length: 212  Bit Score: 38.26  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381   5 IDYDAgNIKSVEKALHYLGEETVV-------SRDPQ-VLLNADkVILpgVGSfGDAMNNLN---KFGLVPVIKEITDKGT 73
Cdd:COG3340    42 GDHDA-YTAKFYEAFSKLGVKVSVlhlfsptFEDPVeALLEAD-VIF--VGG-GNTFNLLAlwrEHGLDDILREAVEAGT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  74 PFLG-----ICLGLQLLfESSDETP---GVEGLGLLKGKIvkippaqglkIPH-----MGWNS------LHLQNDGRLFK 134
Cdd:COG3340   117 VYAGvsagsNCWFPTIR-TTNDGPPplrSFDGLGLVPFSI----------NPHyddedMGETRepriheFLASNPLPPVY 185

                         170       180
                  ....*....|....*....|....
gi 1934263381 135 GIPEETYVYFVHsyylqaEELEIV 158
Cdd:COG3340   186 ALDDGTALHVRG------GKLEVV 203
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 72-185 2.13e-03

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 38.02  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  72 GTPFLGICLGLQLLfessdetpgVEGLGllkGKIVkiPPAQGLKipHMGWNSLHLQNDGRLFKGIPEetYVYFVHS--YY 149
Cdd:PRK06490   86 NKPFLGICLGAQML---------ARHLG---ARVA--PHPDGRV--EIGYYPLRPTEAGRALMHWPE--MVYHWHRegFD 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1934263381 150 LQAEELEIVKATT------QYGvtihasvekDNIFACQFHPE 185
Cdd:PRK06490  148 LPAGAELLATGDDfpnqafRYG---------DNAWGLQFHPE 180
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 41-103 2.39e-03

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: 37.59  E-value: 2.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934263381  41 VILPGVGSFGDAMNNLNKFG----LVPVIKEITDKGTPFLGICLGLQLLFEssdetpgvegLGLLKG 103
Cdd:cd01740    47 VVLPGGFSYGDYLRAGAIAAasplLMEEVKEFAERGGLVLGICNGFQILVE----------LGLLPG 103
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 41-188 4.42e-03

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. 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. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 36.91  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381  41 VILPGVGSFgdamnnLNKFGLVPVIKEI-------TDKGTPF--LGICLGLQLLFESSDETPgveglgLLKGKIVKIPPA 111
Cdd:cd01747    58 ILFPGGAVD------IDTSGYARTAKIIynlalerNDAGDYFpvWGTCLGFELLTYLTSGET------LLLEATEATNSA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934263381 112 QGLKIPHMGWNSLHLQN-DGRLFKGIPEETYVYFVHSYYLQAEELEIVKATTQY-----------GVTIHASVE--KDNI 177
Cdd:cd01747   126 LPLNFTEDALQSRLFKRfPPDLLKSLATEPLTMNNHRYGISPENFTENGLLSDFfnvlttnddwnGVEFISTVEayKYPI 205

                         170
                  ....*....|.
gi 1934263381 178 FACQFHPEKSS 188
Cdd:cd01747   206 YGVQWHPEKNA 216
 
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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