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Conserved domains on  [gi|939707379|ref|WP_054943384|]
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imidazole glycerol phosphate synthase subunit HisH [Paenibacillus ihuae]

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
 2-206 2.65e-124

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 349.43  E-value: 2.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   2 TVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICL 81
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  82 GMQLLFSSSEEYGEHTGLDILPGSVVLFAPRVGYKVPHMGWNKLSFLQPqSPLLTNLTEG-HVYFVHSYHVQMGRESDLL 160
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEGLKVPHMGWNQLELKKE-SPLLKGIPDGaYVYFVHSYYADPCDEEYVA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 939707379 161 AVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQLKRER 206
Cdd:PRK13141 160 ATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-206 2.65e-124

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 349.43  E-value: 2.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   2 TVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICL 81
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  82 GMQLLFSSSEEYGEHTGLDILPGSVVLFAPRVGYKVPHMGWNKLSFLQPqSPLLTNLTEG-HVYFVHSYHVQMGRESDLL 160
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEGLKVPHMGWNQLELKKE-SPLLKGIPDGaYVYFVHSYYADPCDEEYVA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 939707379 161 AVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQLKRER 206
Cdd:PRK13141 160 ATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-196 8.39e-119

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: 335.08  E-value: 8.39e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   1 MTVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGIC 80
Cdd:COG0118    1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  81 LGMQLLFSSSEEYGEHTGLDILPGSVVLFAPRvGYKVPHMGWNKLSFLQPqSPLLTNLTEG-HVYFVHSYHVQMGRESDL 159
Cdd:COG0118   81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPAS-DLKVPHMGWNTVEIAKD-HPLFAGIPDGeYFYFVHSYYVPPDDPEDV 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 939707379 160 LAVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLL 196
Cdd:COG0118  159 VATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLL 195
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 3-200 2.70e-112

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: 318.67  E-value: 2.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICLG 82
Cdd:cd01748    1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  83 MQLLFSSSEEYGEHTGLDILPGSVVLFAPRVGYKVPHMGWNKLSFLQPqSPLLTNLTEG-HVYFVHSYHVQMGRESDLLA 161
Cdd:cd01748   81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASEGLKVPHMGWNQLEITKE-SPLFKGIPDGsYFYFVHSYYAPPDDPDYILA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 939707379 162 VTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFL 200
Cdd:cd01748  160 TTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 3-202 1.33e-89

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: 261.49  E-value: 1.33e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379    3 VAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICLG 82
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   83 MQLLFSSSEEYGEHTGLDILPGSVVLFAPRvgyKVPHMGWNKLSFLQpQSPLLTNLTEG-HVYFVHSYHVQMGrESDLLA 161
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR---KVPHMGWNEVHPVK-ESPLLNGIDEGaYFYFVHSYYAVCE-EEAVLA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 939707379  162 VTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQL 202
Cdd:TIGR01855 156 YADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase pfam00117
Glutamine amidotransferase class-I;
4-200 3.70e-24

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 94.23  E-value: 3.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379    4 AIVDYGMGNLHSVSKAVERLGYESLV---TGDPEEIFAA--DSVIL-PGVGAFGDAMDQLRssgldvIVKEAAAGGQPLL 77
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVvpnDTPAEEILEEnpDGIILsGGPGSPGAAGGAIE------AIREARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   78 GICLGMQLLFsssEEYGEHTGldilpgsvvlfaprVGYKVPHMGWNKLSFLQPQSPLLTNLTEGHVYFVHSYHVQMGRES 157
Cdd:pfam00117  75 GICLGHQLLA---LAFGGKVV--------------KAKKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLP 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 939707379  158 D---LLAVTDYGHPVTAVVGRDN-VFGMQFHPEK-SGELGMKLLGNFL 200
Cdd:pfam00117 138 DgleVTATSENDGTIMGIRHKKLpIFGVQFHPESiLTPHGPEILFNFF 185
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-206 2.65e-124

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 349.43  E-value: 2.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   2 TVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICL 81
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  82 GMQLLFSSSEEYGEHTGLDILPGSVVLFAPRVGYKVPHMGWNKLSFLQPqSPLLTNLTEG-HVYFVHSYHVQMGRESDLL 160
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEGLKVPHMGWNQLELKKE-SPLLKGIPDGaYVYFVHSYYADPCDEEYVA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 939707379 161 AVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQLKRER 206
Cdd:PRK13141 160 ATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-196 8.39e-119

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: 335.08  E-value: 8.39e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   1 MTVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGIC 80
Cdd:COG0118    1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  81 LGMQLLFSSSEEYGEHTGLDILPGSVVLFAPRvGYKVPHMGWNKLSFLQPqSPLLTNLTEG-HVYFVHSYHVQMGRESDL 159
Cdd:COG0118   81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPAS-DLKVPHMGWNTVEIAKD-HPLFAGIPDGeYFYFVHSYYVPPDDPEDV 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 939707379 160 LAVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLL 196
Cdd:COG0118  159 VATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLL 195
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 3-200 2.70e-112

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: 318.67  E-value: 2.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICLG 82
Cdd:cd01748    1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  83 MQLLFSSSEEYGEHTGLDILPGSVVLFAPRVGYKVPHMGWNKLSFLQPqSPLLTNLTEG-HVYFVHSYHVQMGRESDLLA 161
Cdd:cd01748   81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASEGLKVPHMGWNQLEITKE-SPLFKGIPDGsYFYFVHSYYAPPDDPDYILA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 939707379 162 VTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFL 200
Cdd:cd01748  160 TTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-200 4.11e-101

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 290.92  E-value: 4.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   1 MTVAIVDYGMGNLHSVSKAVERLG--YESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGL-DVIVKEAAAGGQPLL 77
Cdd:PRK13146   2 MTVAIIDYGSGNLRSAAKALERAGagADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLgEAVIEAVLAAGRPFL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  78 GICLGMQLLFSSSEEYGEHTGLDILPGSVVLFAPRV-GYKVPHMGWNKLSFLQPqSPLLTNLTEG-HVYFVHSYHVQMGR 155
Cdd:PRK13146  82 GICVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDGpALKVPHMGWNTVDQTRD-HPLFAGIPDGaRFYFVHSYYAQPAN 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 939707379 156 ESDLLAVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFL 200
Cdd:PRK13146 161 PADVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFL 205
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-202 1.62e-99

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 286.38  E-value: 1.62e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICLG 82
Cdd:PRK13181   2 IAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKQPVLGICLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  83 MQLLFSSSEEyGEHTGLDILPGSVVLFaPRVGYKVPHMGWNKLSFLQpQSPLLTNLTEG-HVYFVHSYHVQMGRESDLLA 161
Cdd:PRK13181  82 MQLLFESSEE-GNVKGLGLIPGDVKRF-RSEPLKVPQMGWNSVKPLK-ESPLFKGIEEGsYFYFVHSYYVPCEDPEDVLA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 939707379 162 VTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQL 202
Cdd:PRK13181 159 TTEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAEL 199
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-205 6.41e-94

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 272.51  E-value: 6.41e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   1 MTVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSsgLDVIVKEAAAGGQPLLGIC 80
Cdd:PRK13143   1 MMIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLSP--LRDVILEAARSGKPFLGIC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  81 LGMQLLFSSSEEYGEHTGLDILPGSVVLFapRVGYKVPHMGWNKLSFLQPqSPLLTNLTEGHVYFVHSYHVQMGRESDLL 160
Cdd:PRK13143  79 LGMQLLFESSEEGGGVRGLGLFPGRVVRF--PAGVKVPHMGWNTVKVVKD-CPLFEGIDGEYVYFVHSYYAYPDDEDYVV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 939707379 161 AVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQLKRE 205
Cdd:PRK13143 156 ATTDYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVELIKR 200
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 3-202 1.33e-89

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: 261.49  E-value: 1.33e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379    3 VAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICLG 82
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   83 MQLLFSSSEEYGEHTGLDILPGSVVLFAPRvgyKVPHMGWNKLSFLQpQSPLLTNLTEG-HVYFVHSYHVQMGrESDLLA 161
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR---KVPHMGWNEVHPVK-ESPLLNGIDEGaYFYFVHSYYAVCE-EEAVLA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 939707379  162 VTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQL 202
Cdd:TIGR01855 156 YADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 6.39e-77

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 229.36  E-value: 6.39e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   1 MTVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAaggQPLLGIC 80
Cdd:PRK13170   1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACT---QPVLGIC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  81 LGMQLLFSSSEEYGEHTGLDILPGSVVLFaPRVGYKVPHMGWNKLSFlQPQSPLLTNLTEG-HVYFVHSYHVQMGRESdl 159
Cdd:PRK13170  78 LGMQLLGERSEESGGVDCLGIIDGPVKKM-TDFGLPLPHMGWNQVTP-QAGHPLFQGIEDGsYFYFVHSYAMPVNEYT-- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 939707379 160 LAVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQL 202
Cdd:PRK13170 154 IAQCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-200 6.05e-67

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 214.19  E-value: 6.05e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   2 TVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICL 81
Cdd:PLN02617   8 EVTLLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRPFLGICL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  82 GMQLLFSSSEEYGEHTGLDILPGSVVLFAPRVGYKVPHMGWNKLSFLQpQSPLLTNLTEGHVYFVHSYHVQMGRESD--L 159
Cdd:PLN02617  88 GLQLLFESSEENGPVEGLGVIPGVVGRFDSSNGLRVPHIGWNALQITK-DSELLDGVGGRHVYFVHSYRATPSDENKdwV 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 939707379 160 LAVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFL 200
Cdd:PLN02617 167 LATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRFL 207
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-202 1.66e-64

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 197.75  E-value: 1.66e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAA-AGGQPLLGICL 81
Cdd:PRK13152   2 IALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVlVQKKPILGICL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  82 GMQLLFSSSEEYGEHTGLDILPGSVVLFAPRVGYKVPHMGWNKLSFLQpQSPLLTNLTEG-HVYFVHSYHVQMgRESDLL 160
Cdd:PRK13152  82 GMQLFLERGYEGGVCEGLGFIEGEVVKFEEDLNLKIPHMGWNELEILK-QSPLYQGIPEKsDFYFVHSFYVKC-KDEFVS 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 939707379 161 AVTDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQL 202
Cdd:PRK13152 160 AKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL 201
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 1-201 1.08e-61

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 191.25  E-value: 1.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   1 MTVAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGIC 80
Cdd:CHL00188   2 MKIGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAEGNPFIGIC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  81 LGMQLLFSSSEEyGEHTGLDILPGSVVLFAPRVGYKVPHMGWNKLSFLQPQS-----PLLTNLT-EGHVYFVHSYHVQMG 154
Cdd:CHL00188  82 LGLHLLFETSEE-GKEEGLGIYKGQVKRLKHSPVKVIPHMGWNRLECQNSECqnsewVNWKAWPlNPWAYFVHSYGVMPK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 939707379 155 RESDLLAVTDYG-HPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQ 201
Cdd:CHL00188 161 SQACATTTTFYGkQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFMK 208
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-201 1.78e-61

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 190.03  E-value: 1.78e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAagGQPLLGICLG 82
Cdd:PRK13142   2 IVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNT--DKKMIGICLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  83 MQLLFSSSEEyGEHTGLDILPGSVVLFapRVGYKVPHMGWNKlsfLQPQSPLLTNltegHVYFVHSYHVQMgrESDLLAV 162
Cdd:PRK13142  80 MQLMYEHSDE-GDASGLGFIPGNISRI--QTEYPVPHLGWNN---LVSKHPMLNQ----DVYFVHSYQAPM--SENVIAY 147

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 939707379 163 TDYGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQ 201
Cdd:PRK13142 148 AQYGADIPAIVQFNNYIGIQFHPEKSGTYGLQILRQAIQ 186
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-202 5.73e-52

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 166.23  E-value: 5.73e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGNLHSVSKAVERLGYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICLG 82
Cdd:PRK14004   2 IAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVESGKPLFGICIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  83 MQLLFSSSEEYGEHT------GLDILPGSVVLFAPRvGYKVPHMGWNKLSFL-QPQSPLLTNL-TEGHVYFVHSYHVQMG 154
Cdd:PRK14004  82 FQILFESSEETNQGTkkeqieGLGYIKGKIKKFEGK-DFKVPHIGWNRLQIRrKDKSKLLKGIgDQSFFYFIHSYRPTGA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 939707379 155 RESDLLAVTD-YGHPVTAVVGRDNVFGMQFHPEKSGELGMKLLGNFLQL 202
Cdd:PRK14004 161 EGNAITGLCDyYQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFIEF 209
GATase pfam00117
Glutamine amidotransferase class-I;
4-200 3.70e-24

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 94.23  E-value: 3.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379    4 AIVDYGMGNLHSVSKAVERLGYESLV---TGDPEEIFAA--DSVIL-PGVGAFGDAMDQLRssgldvIVKEAAAGGQPLL 77
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVvpnDTPAEEILEEnpDGIILsGGPGSPGAAGGAIE------AIREARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   78 GICLGMQLLFsssEEYGEHTGldilpgsvvlfaprVGYKVPHMGWNKLSFLQPQSPLLTNLTEGHVYFVHSYHVQMGRES 157
Cdd:pfam00117  75 GICLGHQLLA---LAFGGKVV--------------KAKKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPDTLP 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 939707379  158 D---LLAVTDYGHPVTAVVGRDN-VFGMQFHPEK-SGELGMKLLGNFL 200
Cdd:pfam00117 138 DgleVTATSENDGTIMGIRHKKLpIFGVQFHPESiLTPHGPEILFNFF 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 20-200 1.45e-11

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 60.63  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  20 VERLGYESLV------TGDPEEIFAADSVIL-PGVGAFGDAmdqlrssGLDVIVKEAAAGGQPLLGICLGMQLLFsssEE 92
Cdd:cd01743   18 LRELGAEVVVvrndeiTLEELELLNPDAIVIsPGPGHPEDA-------GISLEIIRALAGKVPILGVCLGHQAIA---EA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  93 YGehtgldilpGSVVlFAPRvgykvPHMGwnKLSFLQP-QSPLLTNLTEG-HVYFVHSYHVQMGRESDLLAVT---DYGH 167
Cdd:cd01743   88 FG---------GKVV-RAPE-----PMHG--KTSEIHHdGSGLFKGLPQPfTVGRYHSLVVDPDPLPDLLEVTastEDGV 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 939707379 168 pVTAVVGRD-NVFGMQFHPEkS--GELGMKLLGNFL 200
Cdd:cd01743  151 -IMALRHRDlPIYGVQFHPE-SilTEYGLRLLENFL 184
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 65-186 7.00e-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: 59.19  E-value: 7.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  65 IVKEAAAGGQPLLGICLGMQLLfssseeyGEHTGldilpGSVVlFAPRVGYkvphmGWNKLSfLQPQSPLLTNLTEG-HV 143
Cdd:COG0518   74 LIREAFELGKPVLGICYGAQLL-------AHALG-----GKVE-PGPGREI-----GWAPVE-LTEADPLFAGLPDEfTV 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 939707379 144 YFVHSYHV-QMGRESDLLAVTDYGhPVTAVVGRDNVFGMQFHPE 186
Cdd:COG0518  135 WMSHGDTVtELPEGAEVLASSDNC-PNQAFRYGRRVYGVQFHPE 177
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-87 7.22e-10

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: 54.53  E-value: 7.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGN---LHSVSKAVERLGYESLV---TGDPEEIFA----ADSVILPGVgaFGDAMDQLRSSGLDVIVKEAAAG 72
Cdd:cd01653    1 VAVLLFPGFEeleLASPLDALREAGAEVDVvspDGGPVESDVdlddYDGLILPGG--PGTPDDLARDEALLALLREAAAA 78

                         90
                 ....*....|....*
gi 939707379  73 GQPLLGICLGMQLLF 87
Cdd:cd01653   79 GKPILGICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-86 2.57e-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: 52.59  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGN---LHSVSKAVERLGYESLV---TGDPEEIFA----ADSVILPGVgaFGDAMDQLRSSGLDVIVKEAAAG 72
Cdd:cd03128    1 VAVLLFGGSEeleLASPLDALREAGAEVDVvspDGGPVESDVdlddYDGLILPGG--PGTPDDLAWDEALLALLREAAAA 78

                         90
                 ....*....|....
gi 939707379  73 GQPLLGICLGMQLL 86
Cdd:cd03128   79 GKPVLGICLGAQLL 92
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 3-103 2.69e-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: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYG-MGNlHSVSKAVERL-GYESLVTGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGIC 80
Cdd:cd01750    1 IAVIRYPdISN-FTDLDPLAREpGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGIC 79

                         90       100
                 ....*....|....*....|....*....
gi 939707379  81 LGMQLLFSS------SEEYGEHTGLDILP 103
Cdd:cd01750   80 GGYQMLGKYivdpegVEGPGEIEGLGLLD 108
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 3-200 3.13e-08

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: 51.38  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGNLHSVSKAVERLGYESLV---TGDPEEI--FAADSVILPGvgafGDAMDqlRSSGLDVIVKEAAAGGQPLL 77
Cdd:cd01742    1 ILILDFGSQYTHLIARRVRELGVYSEIlpnTTPLEEIklKNPKGIILSG----GPSSV--YEEDAPRVDPEIFELGVPVL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  78 GICLGMQLL---F------SSSEEYGeHTGLDILPGSvvlfaprvgykvphmgwnklsflqpqsPLLTNLTEG-HVYFVH 147
Cdd:cd01742   75 GICYGMQLIakaLggkverGDKREYG-KAEIEIDDSS---------------------------PLFEGLPDEqTVWMSH 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 939707379 148 SYHV-QMGRESDLLAVTDyGHPVTAVVGRD-NVFGMQFHPE-KSGELGMKLLGNFL 200
Cdd:cd01742  127 GDEVvKLPEGFKVIASSD-NCPVAAIANEEkKIYGVQFHPEvTHTEKGKEILKNFL 181
guaA PRK00074
GMP synthase; Reviewed
 73-200 3.61e-08

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 52.74  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  73 GQPLLGICLGMQLL---------FSSSEEYGeHTGLDILPGsvvlfaprvgykvphmgwnklsflqpqSPLLTNLTEGH- 142
Cdd:PRK00074  75 GVPVLGICYGMQLMahqlggkveRAGKREYG-RAELEVDND---------------------------SPLFKGLPEEQd 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939707379 143 VYFVHSYHV-QMGRESDLLAVTDyGHPVTAVVGRD-NVFGMQFHPE-KSGELGMKLLGNFL 200
Cdd:PRK00074 127 VWMSHGDKVtELPEGFKVIASTE-NCPIAAIANEErKFYGVQFHPEvTHTPQGKKLLENFV 186
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 62-205 5.30e-08

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: 50.81  E-value: 5.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  62 LDVIvkEAAAGGQPLLGICLGMQLLfssseeyGEHTGldilpGSVVLfAPRV--GykvphmgwnKLSFLQ-PQSPLLTNL 138
Cdd:COG0512   62 LEVI--RAFAGKIPILGVCLGHQAI-------GEAFG-----GKVVR-APEPmhG---------KTSPIThDGSGLFAGL 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939707379 139 TEGHV---YfvHSYHVqmgRESDL------LAVTDYGHpVTAVVGRD-NVFGMQFHPEkS--GELGMKLLGNFLQLKRE 205
Cdd:COG0512  118 PNPFTatrY--HSLVV---DRETLpdelevTAWTEDGE-IMGIRHRElPIEGVQFHPE-SilTEHGHQLLANFLELAGE 189
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 30-86 7.43e-08

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: 51.60  E-value: 7.43e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 939707379  30 TGDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICLGMQLL 86
Cdd:COG1492  282 VRPPEELGDADLVILPGSKNTIADLAWLRESGLDDAIRAHARRGGPVLGICGGYQML 338
PRK00784 PRK00784
cobyric acid synthase;
31-86 9.20e-08

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 51.24  E-value: 9.20e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 939707379  31 GDPEEIFAADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAGGQPLLGICLGMQLL 86
Cdd:PRK00784 283 RPGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRAHARRGGPVLGICGGYQML 338
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 66-200 1.31e-07

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: 49.55  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  66 VKEAAAGGQPLLGICLGMQLLfssseeyGEHTGldilpGSVvlfapRVGYKVPHMGWNKLSFLQ--PQSPLLTNL-TEGH 142
Cdd:cd01741   74 IRQALAAGKPVLGICLGHQLL-------ARALG-----GKV-----GRNPKGWEIGWFPVTLTEagKADPLFAGLpDEFP 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939707379 143 VYFVHSYHV-QMGRESDLLAVTDyGHPVTAVVGRDNVFGMQFHPEKsgelgmKLLGNFL 200
Cdd:cd01741  137 VFHWHGDTVvELPPGAVLLASSE-ACPNQAFRYGDRALGLQFHPEE------RLLRNFL 188
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 42-202 1.10e-06

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 47.05  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  42 VILPGVGAFGDAmdqlrssG--LDVIvkEAAAGGQPLLGICLGMQLLfssseeyGEHTGldilpGSVVLfAPRVGY---- 115
Cdd:PRK05670  48 VLSPGPGTPAEA-------GisLELI--REFAGKVPILGVCLGHQAI-------GEAFG-----GKVVR-AKEIMHgkts 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379 116 KVPHMGwnklsflqpqSPLLTNLTEGhvYFVHSYHVQMGRESDL------LAVTDYGHpVTAVVGRD-NVFGMQFHPEKS 188
Cdd:PRK05670 106 PIEHDG----------SGIFAGLPNP--FTVTRYHSLVVDRESLpdclevTAWTDDGE-IMGVRHKElPIYGVQFHPESI 172

                        170
                 ....*....|....*
gi 939707379 189 G-ELGMKLLGNFLQL 202
Cdd:PRK05670 173 LtEHGHKLLENFLEL 187
PLN02347 PLN02347
GMP synthetase
 2-200 4.51e-06

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 46.60  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   2 TVAIVDYGMGNLHSVSKAVERLGYESLV---TGDPEEIFA-----------ADSVILPGVGAFGDAmdqlrssgldvIVK 67
Cdd:PLN02347  12 VVLILDYGSQYTHLITRRVRELGVYSLLlsgTASLDRIASlnprvvilsggPHSVHVEGAPTVPEG-----------FFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  68 EAAAGGQPLLGICLGMQLLFSsseeygehtgldiLPGSVVLFAPRVGY-KVPHMgwnklsfLQPQSPLLTNLTEGHVYFV 146
Cdd:PLN02347  81 YCRERGVPVLGICYGMQLIVQ-------------KLGGEVKPGEKQEYgRMEIR-------VVCGSQLFGDLPSGETQTV 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379 147 HSYH----VQMGRESDLLAVTDYGhPVTAVVGRD-NVFGMQFHPEKS-GELGMKLLGNFL 200
Cdd:PLN02347 141 WMSHgdeaVKLPEGFEVVAKSVQG-AVVAIENRErRIYGLQYHPEVThSPKGMETLRHFL 199
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
2-108 5.31e-06

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 45.31  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379    2 TVAIVD------YGMGNLHsvskAVERLGYESL--VTGDPEEIFA-ADSVILPGVGAFGDAMDQLRSSGLDVIVKEAAAG 72
Cdd:pfam07685   1 RIAVIRlprisnYTDDNLD----PLRYEPAVRVrfVPLPDESLGPdADLIILPGGKPTIQDLALLRNSGMDEAIKEAAED 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 939707379   73 GQPLLGICLGMQLLFSS-SEEYG-EHTGLDILPGSVVL 108
Cdd:pfam07685  77 GGPVLGICGGYQMLGETiEDPEGvRIEGLGLLDIETVF 114
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
42-205 8.13e-06

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 45.48  E-value: 8.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  42 VILPGVGAFGDAmdqlrssGLDVIVKEAAAGGQPLLGICLGMQLLfssseeyGEHTGLDIlpgsvvlfaprVGYKVPHMG 121
Cdd:PRK14607  49 VISPGPGRPEEA-------GISVEVIRHFSGKVPILGVCLGHQAI-------GYAFGGKI-----------VHAKRILHG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379 122 wnKLSFLQPQSPLLTNLTEGHVYFVHsYHVQMGRESDL------LAVTDYGHpVTAVVGRDN-VFGMQFHPEKSG-ELGM 193
Cdd:PRK14607 104 --KTSPIDHNGKGLFRGIPNPTVATR-YHSLVVEEASLpeclevTAKSDDGE-IMGIRHKEHpIFGVQFHPESILtEEGK 179

                        170
                 ....*....|..
gi 939707379 194 KLLGNFLQLKRE 205
Cdd:PRK14607 180 RILKNFLNYQRE 191
PRK13566 PRK13566
anthranilate synthase component I;
1-202 2.76e-05

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 44.14  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   1 MTVAIVDYGMGNLHSVSKAVERLGYE--SLVTGDPEEIF---AADSVIL-PGVGafgdamdqlRSSGLDV--IVKEAAAG 72
Cdd:PRK13566 527 KRVLLVDHEDSFVHTLANYFRQTGAEvtTVRYGFAEEMLdrvNPDLVVLsPGPG---------RPSDFDCkaTIDAALAR 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  73 GQPLLGICLGMQLLfssseeyGEHTG--LDILPgsvvlfaprvgykVPHMGwnKLSFLQPQSP--LLTNLTEGHV---Yf 145
Cdd:PRK13566 598 NLPIFGVCLGLQAI-------VEAFGgeLGQLA-------------YPMHG--KPSRIRVRGPgrLFSGLPEEFTvgrY- 654

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939707379 146 vHSYHV---QMGRESDLLAVTDYGhPVTAVVGRDN-VFGMQFHPEK----SGELGMKLLGNFLQL 202
Cdd:PRK13566 655 -HSLFAdpeTLPDELLVTAETEDG-VIMAIEHKTLpVAAVQFHPESimtlGGDVGLRIIENVVRL 717
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
18-101 3.21e-05

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 42.84  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  18 KAVERLGYESLVTGDPEEIFAADSVILPGvgafGD--AMDQL-RSSGLDVIVKEAAAGGQPLLGICLGMQLLFSSSEEYG 94
Cdd:PRK13525  18 AALEALGAEAVEVRRPEDLDEIDGLILPG----GEstTMGKLlRDFGLLEPLREFIASGLPVFGTCAGMILLAKEIEGYE 93


                 ....*....
gi 939707379  95 EHT--GLDI 101
Cdd:PRK13525  94 QEHlgLLDI 102
PRK00758 PRK00758
GMP synthase subunit A; Validated
 3-98 6.27e-05

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 42.15  E-value: 6.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   3 VAIVDYGMGNLHSVSKAVERLGYES-LV--TGDPEEIFA-ADSVILPGvgafGDAMDQLRSSGLdvIVKEAaagGQPLLG 78
Cdd:PRK00758   2 IVVVDNGGQYNHLIHRTLRYLGVDAkIIpnTTPVEEIKAfEDGLILSG----GPDIERAGNCPE--YLKEL---DVPILG 72

                         90       100
                 ....*....|....*....|
gi 939707379  79 ICLGMQLLfssSEEYGEHTG 98
Cdd:PRK00758  73 ICLGHQLI---AKAFGGEVG 89
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 19-191 1.83e-04

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


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 40.59  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  19 AVERLGYESLVTGDPEEIFAADSVILPGvgafGD--AMDQL-RSSGLDVIVKEAAAGGQPLLGICLGMQLLFSSSEEYGE 95
Cdd:cd01749   16 ALERLGVEVIEVRTPEDLEGIDGLIIPG----GEstTIGKLlRRTGLLDPLREFIRAGKPVFGTCAGLILLAKEVEDQGG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  96 HTGLDILPGSV--VLFAPRVGykvphmgwnklSFlqpQSPL-LTNLTEG--HVYFVHSYHVQ-MGRESDLLAVTDyGHPV 169
Cdd:cd01749   92 QPLLGLLDITVrrNAFGRQVD-----------SF---EADLdIPGLGLGpfPAVFIRAPVIEeVGPGVEVLAEYD-GKIV 156

                        170       180
                 ....*....|....*....|..
gi 939707379 170 TAVVGrdNVFGMQFHPEKSGEL 191
Cdd:cd01749  157 AVRQG--NVLATSFHPELTDDT 176
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
40-86 3.83e-03

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 37.02  E-value: 3.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 939707379  40 DSVILPGVGAFGD------------AMDQlrssgldviVKEAAAGGQPLLGICLGMQLL 86
Cdd:PRK03619  43 DAVVLPGGFSYGDylrcgaiaafspIMKA---------VKEFAEKGKPVLGICNGFQIL 92
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-191 3.97e-03

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 36.79  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   1 MTVAIVDYgMGN----LHSVSKAVERLG--YESLVTGDPEEIFAADSVILPG-----VGAFgdamdqLRSSGLDVIVKEA 69
Cdd:PRK13527   1 MKIGVLAL-QGDveehIDALKRALDELGidGEVVEVRRPGDLPDCDALIIPGgesttIGRL------MKREGILDEIKEK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  70 AAGGQPLLGICLGMQLLfsSSEEYGEHTG------LDILPGSVVlfapRVGYkvphmGWNKLSFlqpQSPL-LTNLTEG- 141
Cdd:PRK13527  74 IEEGLPILGTCAGLILL--AKEVGDDRVTkteqplLGLMDVTVK----RNAF-----GRQRDSF---EAEIdLSGLDGPf 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 939707379 142 HVYFVHS-YHVQMGRESDLLAVTDyGHPVTAVVGrdNVFGMQFHPEKSGEL 191
Cdd:PRK13527 140 HAVFIRApAITKVGGDVEVLAKLD-DRIVAVEQG--NVLATAFHPELTDDT 187
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 65-86 4.93e-03

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: 36.69  E-value: 4.93e-03
                         10        20
                 ....*....|....*....|..
gi 939707379  65 IVKEAAAGGQPLLGICLGMQLL 86
Cdd:COG2071   88 LIRAALERGKPVLGICRGMQLL 109
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 65-186 5.40e-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: 36.47  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379   65 IVKEAAAGGQPLLGICLGMQL--------LFSSSEEYGEHTGLdILPGSVVLFAPRvgYKVPhmgwnklsfLQPQSpLLT 136
Cdd:pfam07722  97 LIRAALARGKPILGICRGFQLlnvalggtLYQDIQEQPGFTDH-REHCQVAPYAPS--HAVN---------VEPGS-LLA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939707379  137 NLTEGHVYFVHSYHVQ-----------MGRESDLL--AVTDYGHPVTAVvgrdnvfGMQFHPE 186
Cdd:pfam07722 164 SLLGSEEFRVNSLHHQaidrlapglrvEAVAPDGTieAIESPNAKGFAL-------GVQWHPE 219
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 21-117 6.25e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobB.


Pssm-ID: 153224 [Multi-domain]  Cd Length: 198  Bit Score: 36.42  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939707379  21 ERLGYEsLVTGDP---EEIFAADSVILPGvG---AFGDAMDQ---LRSSgldviVKEAAAGGQPLLGICLGMQLLFSS-- 89
Cdd:cd03130   21 EAAGAE-LVPFSPlkdEELPDADGLYLGG-GypeLFAEELSAnqsMRES-----IRAFAESGGPIYAECGGLMYLGESld 93

                         90       100
                 ....*....|....*....|....*....
gi 939707379  90 SEEYGEHTGLDILPGSVVLFA-PRVGYKV 117
Cdd:cd03130   94 DEEGQSYPMAGVLPGDARMTKrLGLGYRE 122
 
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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