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Conserved domains on  [gi|6324138|ref|NP_014208|]
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glutamine amidotransferase subunit DUG3 [Saccharomyces cerevisiae S288C]

Protein Classification

class II glutamine amidotransferase( domain architecture ID 10112377)

class II glutamine amidotransferase hydrolyzes ammonia from glutamine and transfers the amino group to the appropriate substrate; similar to Saccharomyces cerevisiae glutamine amidotransferase DUG3

CATH:  3.60.20.10
EC:  2.4.2.-
Gene Ontology:  GO:0016740|GO:0006541
PubMed:  8430515|9559052
SCOP:  3000131

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 1-292 1.06e-85

Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


:

Pssm-ID: 238889 [Multi-domain]  Cd Length: 257  Bit Score: 259.63  E-value: 1.06e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    1 MCRFLIFKGkQPIRLSHLLTRPAHSIINQSFDSRLRLDrrrPMNGDGFGVAYYpldtELSEDGPCLFKAITPAWNNQNLS 80
Cdd:cd01908   1 MCRLLGYSG-APIPLEPLLIRPSHSLLVQSGGPREMKG---TVHADGWGIGWY----EGKGGRPFRYRSPLPAWSDINLE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138   81 TLAEKTKSDLVFAHVRASTYGVLSETNCHPFTYHSLCFMHNGGISNFKGIKRKLLNHIKdeylNFIQGSTDSECAFALFL 160
Cdd:cd01908  73 SLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLLRLLP----RLPVGTTDSELAFALLL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138  161 DTLDKLGYDPKKqdgdfgnvALRKAMLRTIDYIRDWtkeankdeahVEPSLLNFAVTDGSTVVVSRYITsktdeAASLHF 240
Cdd:cd01908 149 SRLLERDPLDPA--------ELLDAILQTLRELAAL----------APPGRLNLLLSDGEYLIATRYAS-----APSLYY 205

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6324138  241 SCGSSFVETSPGEYRvERLDRNQDVIMVASEPLTFERgDWTAVPTNSILTIK 292
Cdd:cd01908 206 LTRRAPFGCARLLFR-SVTTPNDDGVVVASEPLTDDE-GWTEVPPGELVVVS 255
 
Name Accession Description Interval E-value
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 1-292 1.06e-85

Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238889 [Multi-domain]  Cd Length: 257  Bit Score: 259.63  E-value: 1.06e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    1 MCRFLIFKGkQPIRLSHLLTRPAHSIINQSFDSRLRLDrrrPMNGDGFGVAYYpldtELSEDGPCLFKAITPAWNNQNLS 80
Cdd:cd01908   1 MCRLLGYSG-APIPLEPLLIRPSHSLLVQSGGPREMKG---TVHADGWGIGWY----EGKGGRPFRYRSPLPAWSDINLE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138   81 TLAEKTKSDLVFAHVRASTYGVLSETNCHPFTYHSLCFMHNGGISNFKGIKRKLLNHIKdeylNFIQGSTDSECAFALFL 160
Cdd:cd01908  73 SLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLLRLLP----RLPVGTTDSELAFALLL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138  161 DTLDKLGYDPKKqdgdfgnvALRKAMLRTIDYIRDWtkeankdeahVEPSLLNFAVTDGSTVVVSRYITsktdeAASLHF 240
Cdd:cd01908 149 SRLLERDPLDPA--------ELLDAILQTLRELAAL----------APPGRLNLLLSDGEYLIATRYAS-----APSLYY 205

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6324138  241 SCGSSFVETSPGEYRvERLDRNQDVIMVASEPLTFERgDWTAVPTNSILTIK 292
Cdd:cd01908 206 LTRRAPFGCARLLFR-SVTTPNDDGVVVASEPLTDDE-GWTEVPPGELVVVS 255
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
2-292 3.05e-75

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 232.55  E-value: 3.05e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    2 CRFLIFKGKQPIRLSHLLTRPAHSIINQSfdsrlrLDRRRPMNGDGFGVAYYPldtelSEDGPCLFKAITPAWNNQNLST 81
Cdd:COG0121   1 CRLLGYSGNVPTDLEFLLLDPEHSLVRQS------GATREGPHADGWGIGWYE-----GDGEPRLYRDPLPAWSDPNLRL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138   82 LAEKTKSDLVFAHVRASTYGVLSETNCHPFTYHSLCFMHNGGISNFKGIKRKLLNHIKDEYLNFIQGSTDSECAFALFLD 161
Cdd:COG0121  70 LARPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEELPDELYFQPVGTTDSELAFALLLS 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138  162 TLDKLGYDPkkqdgdfgnvalRKAMLRTIDYIRDWTKeankdeahvEPSLLNFAVTDGSTVVVSRYitSKTDEAASLHFS 241
Cdd:COG0121 150 RLRDGGPDP------------AEALAEALRELAELAR---------APGRLNLLLSDGERLYATRY--TSDDPYPTLYYL 206

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6324138  242 cgssfvetspgeyrvERLDRNQDVIMVASEPLTfERGDWTAVPTNSILTIK 292
Cdd:COG0121 207 ---------------TRTTPDDRVVVVASEPLT-DDEGWTEVPPGELLVVR 241
GATase_4 pfam13230
Glutamine amidotransferases class-II; This family captures members that are not found in ...
 46-290 1.92e-13

Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.


Pssm-ID: 433047 [Multi-domain]  Cd Length: 272  Bit Score: 69.67  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138     46 DGFGVAYYPldtelsEDGPCLFKAITPAWNnqnlSTLAE-----KTKSDLVFAHVRASTYGVLSETNCHPFTyHSL---- 116
Cdd:pfam13230  34 DGWGIAFYE------GRGARVFKDPQPSAD----SPIAElvrryPIRSRNVIAHIRKATQGRVTLENTHPFM-RELwgry 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    117 -CFMHNGGISNFKGIKRKLLNHIkdeylnfiqGSTDSECAFALFLDTLDKLGYDPKKQDGDFGnvalrkAMLrtidyiRD 195
Cdd:pfam13230 103 wIFAHNGDLKGYAPKLSGRFQPV---------GSTDSELAFCWLLDRLASRFPYARPSAGELF------RAL------RE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    196 WTKEANKDeahvepSLLNFAVTDGSTVVVSR-----YITSK--------TDEAASLHFScgssfvetspgeyrvERLDRN 262
Cdd:pfam13230 162 LAREIAAH------GTFNFLLSDGRDLFAHCstrlhYILRRapfgeahlKDDDVSVDFA---------------RVTTPN 220

                         250       260
                  ....*....|....*....|....*...
gi 6324138    263 QDVIMVASEPLTFERgDWTAVPTNSILT 290
Cdd:pfam13230 221 DRVAVIATEPLTRNE-TWTRMEPGELLV 247
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 64-153 5.63e-04

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 41.79  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    64 PCLFKAITpawnnqNLSTLAEKTKSDLV----------------FAHVRASTYGVLSETNCHPFTYHSLCF--MHNGGIS 125
Cdd:PTZ00394  63 PCVVRSVG------NISQLREKVFSEAVaatlppmdattshhvgIAHTRWATHGGVCERNCHPQQSNNGEFtiVHNGIVT 136

                         90       100
                 ....*....|....*....|....*...
gi 6324138   126 NFKGIKRKLlnhiKDEYLNFiQGSTDSE 153
Cdd:PTZ00394 137 NYMTLKELL----KEEGYHF-SSDTDTE 159
 
Name Accession Description Interval E-value
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 1-292 1.06e-85

Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238889 [Multi-domain]  Cd Length: 257  Bit Score: 259.63  E-value: 1.06e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    1 MCRFLIFKGkQPIRLSHLLTRPAHSIINQSFDSRLRLDrrrPMNGDGFGVAYYpldtELSEDGPCLFKAITPAWNNQNLS 80
Cdd:cd01908   1 MCRLLGYSG-APIPLEPLLIRPSHSLLVQSGGPREMKG---TVHADGWGIGWY----EGKGGRPFRYRSPLPAWSDINLE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138   81 TLAEKTKSDLVFAHVRASTYGVLSETNCHPFTYHSLCFMHNGGISNFKGIKRKLLNHIKdeylNFIQGSTDSECAFALFL 160
Cdd:cd01908  73 SLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLLRLLP----RLPVGTTDSELAFALLL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138  161 DTLDKLGYDPKKqdgdfgnvALRKAMLRTIDYIRDWtkeankdeahVEPSLLNFAVTDGSTVVVSRYITsktdeAASLHF 240
Cdd:cd01908 149 SRLLERDPLDPA--------ELLDAILQTLRELAAL----------APPGRLNLLLSDGEYLIATRYAS-----APSLYY 205

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6324138  241 SCGSSFVETSPGEYRvERLDRNQDVIMVASEPLTFERgDWTAVPTNSILTIK 292
Cdd:cd01908 206 LTRRAPFGCARLLFR-SVTTPNDDGVVVASEPLTDDE-GWTEVPPGELVVVS 255
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
2-292 3.05e-75

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 232.55  E-value: 3.05e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    2 CRFLIFKGKQPIRLSHLLTRPAHSIINQSfdsrlrLDRRRPMNGDGFGVAYYPldtelSEDGPCLFKAITPAWNNQNLST 81
Cdd:COG0121   1 CRLLGYSGNVPTDLEFLLLDPEHSLVRQS------GATREGPHADGWGIGWYE-----GDGEPRLYRDPLPAWSDPNLRL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138   82 LAEKTKSDLVFAHVRASTYGVLSETNCHPFTYHSLCFMHNGGISNFKGIKRKLLNHIKDEYLNFIQGSTDSECAFALFLD 161
Cdd:COG0121  70 LARPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEELPDELYFQPVGTTDSELAFALLLS 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138  162 TLDKLGYDPkkqdgdfgnvalRKAMLRTIDYIRDWTKeankdeahvEPSLLNFAVTDGSTVVVSRYitSKTDEAASLHFS 241
Cdd:COG0121 150 RLRDGGPDP------------AEALAEALRELAELAR---------APGRLNLLLSDGERLYATRY--TSDDPYPTLYYL 206

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6324138  242 cgssfvetspgeyrvERLDRNQDVIMVASEPLTfERGDWTAVPTNSILTIK 292
Cdd:COG0121 207 ---------------TRTTPDDRVVVVASEPLT-DDEGWTEVPPGELLVVR 241
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 44-289 3.92e-22

Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.


Pssm-ID: 238212 [Multi-domain]  Cd Length: 220  Bit Score: 92.90  E-value: 3.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138   44 NGDGFGVAYYpldtelsEDGPCLFKAITPAWNNQNLSTLAEKTKSDLVFAHVRASTYGVLSETNCHPFTYHS--LCFMHN 121
Cdd:cd00352  31 GPDGAGIAVY-------DGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRSEDgrIALVHN 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138  122 GGISNFKGIKRKLLNHikdeYLNFiQGSTDSECAFALFLDTLDKLGydpkkqdgdfgnvaLRKAMLRTIDYIRdwtkean 201
Cdd:cd00352 104 GEIYNYRELREELEAR----GYRF-EGESDSEVILHLLERLGREGG--------------LFEAVEDALKRLD------- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138  202 kdeahvepSLLNFAVTDGS--TVVVSRYitskTDEAASLHfscgssFVETSPGEYrverldrnqdviMVASEPLTFERG- 278
Cdd:cd00352 158 --------GPFAFALWDGKpdRLFAARD----RFGIRPLY------YGITKDGGL------------VFASEPKALLALp 207

                       250
                ....*....|...
gi 6324138  279 --DWTAVPTNSIL 289
Cdd:cd00352 208 fkGVRRLPPGELL 220
GATase_4 pfam13230
Glutamine amidotransferases class-II; This family captures members that are not found in ...
 46-290 1.92e-13

Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.


Pssm-ID: 433047 [Multi-domain]  Cd Length: 272  Bit Score: 69.67  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138     46 DGFGVAYYPldtelsEDGPCLFKAITPAWNnqnlSTLAE-----KTKSDLVFAHVRASTYGVLSETNCHPFTyHSL---- 116
Cdd:pfam13230  34 DGWGIAFYE------GRGARVFKDPQPSAD----SPIAElvrryPIRSRNVIAHIRKATQGRVTLENTHPFM-RELwgry 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    117 -CFMHNGGISNFKGIKRKLLNHIkdeylnfiqGSTDSECAFALFLDTLDKLGYDPKKQDGDFGnvalrkAMLrtidyiRD 195
Cdd:pfam13230 103 wIFAHNGDLKGYAPKLSGRFQPV---------GSTDSELAFCWLLDRLASRFPYARPSAGELF------RAL------RE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    196 WTKEANKDeahvepSLLNFAVTDGSTVVVSR-----YITSK--------TDEAASLHFScgssfvetspgeyrvERLDRN 262
Cdd:pfam13230 162 LAREIAAH------GTFNFLLSDGRDLFAHCstrlhYILRRapfgeahlKDDDVSVDFA---------------RVTTPN 220

                         250       260
                  ....*....|....*....|....*...
gi 6324138    263 QDVIMVASEPLTFERgDWTAVPTNSILT 290
Cdd:pfam13230 221 DRVAVIATEPLTRNE-TWTRMEPGELLV 247
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 84-168 5.29e-07

Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238888 [Multi-domain]  Cd Length: 249  Bit Score: 50.34  E-value: 5.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138   84 EKTKSDLVFAHVRASTYGVLSETNCHPFTYHSLCFMHNGGISNFKGIKRKLLNH-IKDEYLnfiqgsTDSECAFALFLDT 162
Cdd:cd01907  73 EEYKGYHWIAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFgYKFETE------TDTEVIAYYLDLL 146


                ....*.
gi 6324138  163 LDKLGY 168
Cdd:cd01907 147 LRKGGL 152
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 88-166 7.66e-06

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.


Pssm-ID: 433279 [Multi-domain]  Cd Length: 130  Bit Score: 44.99  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138     88 SDLVFAHVRASTYGVLSETNcHPFT--YHSLCFMHNGGISNFKGIKRKLLNHIKDeylnfIQGSTDSECAFALFL----D 161
Cdd:pfam13522  10 GGVALGHVRLAIVDLPDAGN-QPMLsrDGRLVLVHNGEIYNYGELREELADLGHA-----FRSRSDTEVLLALYEewgeD 83


                  ....*
gi 6324138    162 TLDKL 166
Cdd:pfam13522  84 CLERL 88
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 94-153 8.91e-05

Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 44.24  E-value: 8.91e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324138   94 HVRASTYGVLSETNCHPFT----YHSLCFMHNGGISNFKGIKRKLLN--HIkdeylnfIQGSTDSE 153
Cdd:COG0034  77 HVRYSTTGSSSLENAQPFYvnspFGSIALAHNGNLTNAEELREELEEegAI-------FQTTSDTE 135
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 49-137 1.62e-04

Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.


Pssm-ID: 238366 [Multi-domain]  Cd Length: 215  Bit Score: 42.43  E-value: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138   49 GVAYypldteLSEDGPCLFKAITpawnnqNLSTLAEKTKSDLVF-----AHVRASTYGVLSETNCHPftyHSLCFM---- 119
Cdd:cd00714  32 GIAV------IGDGSLEVVKAVG------KVANLEEKLAEKPLSghvgiGHTRWATHGEPTDVNAHP---HRSCDGeiav 96

                        90
                ....*....|....*....
gi 6324138  120 -HNGGISNFKGIKRKLLNH 137
Cdd:cd00714  97 vHNGIIENYAELKEELEAK 115
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 64-153 5.63e-04

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 41.79  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    64 PCLFKAITpawnnqNLSTLAEKTKSDLV----------------FAHVRASTYGVLSETNCHPFTYHSLCF--MHNGGIS 125
Cdd:PTZ00394  63 PCVVRSVG------NISQLREKVFSEAVaatlppmdattshhvgIAHTRWATHGGVCERNCHPQQSNNGEFtiVHNGIVT 136

                         90       100
                 ....*....|....*....|....*...
gi 6324138   126 NFKGIKRKLlnhiKDEYLNFiQGSTDSE 153
Cdd:PTZ00394 137 NYMTLKELL----KEEGYHF-SSDTDTE 159
PLN02440 PLN02440
amidophosphoribosyltransferase
 84-165 4.41e-03

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 38.89  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324138    84 EKTKSDLVFAHVRASTYGVLSETNCHPFT----YHSLCFMHNGGISNFKGIKRKLlnhikDEYLNFIQGSTDSECAFALF 159
Cdd:PLN02440  61 DQLPGDIAIGHVRYSTAGASSLKNVQPFVanyrFGSIGVAHNGNLVNYEELRAKL-----EENGSIFNTSSDTEVLLHLI 135


                 ....*.
gi 6324138   160 LDTLDK 165
Cdd:PLN02440 136 AISKAR 141
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 93-153 6.64e-03

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 38.46  E-value: 6.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324138    93 AHVRASTYGVLSETNCHP-FTYH---SLCfmHNGGISNFKGIKRKLLnhikDEYLNFiQGSTDSE 153
Cdd:PTZ00295 100 AHTRWATHGGKTDENAHPhCDYKkriALV--HNGTIENYVELKSELI----AKGIKF-RSETDSE 157
 
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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