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Conserved domains on  [gi|167041154|gb|ABZ05913|]
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putative glutamine amidotransferases class-II [uncultured marine microorganism HF4000_001B09]

Protein Classification

class II glutamine amidotransferase domain-containing protein( domain architecture ID 1025)

class II glutamine amidotransferase domain-containing protein may hydrolyze ammonia from glutamine and transfer the amino group to the appropriate substrate

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gn_AT_II super family cl00319
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 2-311 3.73e-73

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.


The actual alignment was detected with superfamily member cd01907:

Pssm-ID: 469719 [Multi-domain]  Cd Length: 249  Bit Score: 225.61  E-value: 3.73e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154   2 CGIAGLIHKGKTVNIGKELKDMLQALKHRGP-DSTGYALYGegsngdyimrfkvgenvgegssavnedksvydsrkkqvd 80
Cdd:cd01907    1 CGIFGIMSKDGEPFVGALLVEMLDAMQERGPgDGAGFALYG--------------------------------------- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  81 shlkelgaqivkedrltpysfryiikyDKDLmefskkiesvemtEILSLGKSLELVKDLGDANTVSKQYGLDKIKGTHAI 160
Cdd:cd01907   42 ---------------------------DPDA-------------FVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWI 81

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 161 GHSRMATESGVDIRSAHPFWGYpfsDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELIAVYLADKMRSGVT------ 234
Cdd:cd01907   82 AHTRQPTNSAVWWYGAHPFSIG---DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLpleyyk 158

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 235 -------------LEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEIAIRTLLPQEIDT- 300
Cdd:cd01907  159 hiirmpeeerellLALRLTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKv 238

                        330
                 ....*....|.
gi 167041154 301 YDPYEGEVKVW 311
Cdd:cd01907  239 WEPRPGEYVIW 249
 
Name Accession Description Interval E-value
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-311 3.73e-73

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: 225.61  E-value: 3.73e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154   2 CGIAGLIHKGKTVNIGKELKDMLQALKHRGP-DSTGYALYGegsngdyimrfkvgenvgegssavnedksvydsrkkqvd 80
Cdd:cd01907    1 CGIFGIMSKDGEPFVGALLVEMLDAMQERGPgDGAGFALYG--------------------------------------- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  81 shlkelgaqivkedrltpysfryiikyDKDLmefskkiesvemtEILSLGKSLELVKDLGDANTVSKQYGLDKIKGTHAI 160
Cdd:cd01907   42 ---------------------------DPDA-------------FVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWI 81

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 161 GHSRMATESGVDIRSAHPFWGYpfsDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELIAVYLADKMRSGVT------ 234
Cdd:cd01907   82 AHTRQPTNSAVWWYGAHPFSIG---DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLpleyyk 158

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 235 -------------LEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEIAIRTLLPQEIDT- 300
Cdd:cd01907  159 hiirmpeeerellLALRLTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKv 238

                        330
                 ....*....|.
gi 167041154 301 YDPYEGEVKVW 311
Cdd:cd01907  239 WEPRPGEYVIW 249
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 130-293 6.69e-21

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: 92.39  E-value: 6.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFWG-YPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:COG0034   45 GGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGSSSLENAQPFYVnSPFGSIALAHNGNLTNAEELREELEEE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 209 GMRFMSECDSELIAVYLADKMRSGvTLEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEI 288
Cdd:COG0034  125 GAIFQTTSDTEVILHLIARELTKE-DLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASESC 203


                 ....*
gi 167041154 289 AIRTL 293
Cdd:COG0034  204 ALDIL 208
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
 130-310 1.34e-17

amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273461 [Multi-domain]  Cd Length: 442  Bit Score: 82.75  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFW-GYPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:TIGR01134  39 GNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSSGLENAQPFVvNSPYGGLALAHNGNLVNADELRRELEEE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  209 GMRFMSECDSELIAVYLADKMRSGVTLEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEI 288
Cdd:TIGR01134 119 GRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESC 198

                         170       180
                  ....*....|....*....|..
gi 167041154  289 AIRTLLPQEIDTYDPyeGEVKV 310
Cdd:TIGR01134 199 ALDILGAEFVRDVEP--GEVVV 218
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 130-302 2.44e-17

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 82.00  E-value: 2.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFWG-YPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:PRK05793  54 GEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGASDLDNAQPLVAnYKLGSIAIAHNGNLVNADVIRELLEDG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 209 GMRFMSECDSELIAVYLADKMRSGvtLEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEI 288
Cdd:PRK05793 134 GRIFQTSIDSEVILNLIARSAKKG--LEKALVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKLGDDYILSSESC 211

                        170       180
                 ....*....|....*....|..
gi 167041154 289 A--------IRTLLPQEIDTYD 302
Cdd:PRK05793 212 AldtigaefIRDVEPGEIVIID 233
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 159-286 3.35e-13

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: 65.40  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  159 AIGHSRMATeSGVDIRSAHPFWgYPFSDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELIAvyladkmrsgVTLEQG 238
Cdd:pfam13522  13 ALGHVRLAI-VDLPDAGNQPML-SRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLL----------ALYEEW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 167041154  239 MKDSIKELDGVFTYLV--ATKNSLGMAKDVMAAKPMVLYESDDLVALGSE 286
Cdd:pfam13522  81 GEDCLERLRGMFAFAIwdRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
 
Name Accession Description Interval E-value
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-311 3.73e-73

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: 225.61  E-value: 3.73e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154   2 CGIAGLIHKGKTVNIGKELKDMLQALKHRGP-DSTGYALYGegsngdyimrfkvgenvgegssavnedksvydsrkkqvd 80
Cdd:cd01907    1 CGIFGIMSKDGEPFVGALLVEMLDAMQERGPgDGAGFALYG--------------------------------------- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  81 shlkelgaqivkedrltpysfryiikyDKDLmefskkiesvemtEILSLGKSLELVKDLGDANTVSKQYGLDKIKGTHAI 160
Cdd:cd01907   42 ---------------------------DPDA-------------FVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWI 81

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 161 GHSRMATESGVDIRSAHPFWGYpfsDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELIAVYLADKMRSGVT------ 234
Cdd:cd01907   82 AHTRQPTNSAVWWYGAHPFSIG---DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLpleyyk 158

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 235 -------------LEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEIAIRTLLPQEIDT- 300
Cdd:cd01907  159 hiirmpeeerellLALRLTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKv 238

                        330
                 ....*....|.
gi 167041154 301 YDPYEGEVKVW 311
Cdd:cd01907  239 WEPRPGEYVIW 249
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 2-298 4.49e-31

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: 116.01  E-value: 4.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154   2 CGIAGLIHKGKTVNIGKELK-DMLQALKHRGPDSTGYALYGegsngdyimrfkvgenvgegssavnedksvydsrkkqvd 80
Cdd:cd00352    1 CGIFGIVGADGAASLLLLLLlRGLAALEHRGPDGAGIAVYD--------------------------------------- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  81 shlkelgaqivkedrltpysfryiikydkdlmefskkiesvemteilslGKSLELVKDLGDANTVSKQYGLDKIKGTHAI 160
Cdd:cd00352   42 -------------------------------------------------GDGLFVEKRAGPVSDVALDLLDEPLKSGVAL 72

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 161 GHSRMATESGVDIRSAHPFWgYPFSDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELIAVYLADKMRSGvTLEQGMK 240
Cdd:cd00352   73 GHVRLATNGLPSEANAQPFR-SEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREG-GLFEAVE 150

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041154 241 DSIKELDGVFTYLVATK--NSLGMAKDVMAAKPMVLYE-SDDLVALGSEEIAIRTLLPQEI 298
Cdd:cd00352  151 DALKRLDGPFAFALWDGkpDRLFAARDRFGIRPLYYGItKDGGLVFASEPKALLALPFKGV 211
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 130-293 6.69e-21

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: 92.39  E-value: 6.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFWG-YPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:COG0034   45 GGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGSSSLENAQPFYVnSPFGSIALAHNGNLTNAEELREELEEE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 209 GMRFMSECDSELIAVYLADKMRSGvTLEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEI 288
Cdd:COG0034  125 GAIFQTTSDTEVILHLIARELTKE-DLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASESC 203


                 ....*
gi 167041154 289 AIRTL 293
Cdd:COG0034  204 ALDIL 208
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
 130-293 1.88e-18

Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.


Pssm-ID: 238367 [Multi-domain]  Cd Length: 252  Bit Score: 82.89  E-value: 1.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFWG-YPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:cd00715   38 GKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSSSLENAQPFVVnSPLGGIALAHNGNLVNAKELREELEEE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 209 GMRFMSECDSELIAVYLAdKMRSGVTLEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVL--YESDDLVaLGSE 286
Cdd:cd00715  118 GRIFQTTSDSEVILHLIA-RSLAKDDLFEAIIDALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLgkLEGDGYV-VASE 195


                 ....*..
gi 167041154 287 EIAIRTL 293
Cdd:cd00715  196 SCALDII 202
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
 130-310 1.34e-17

amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273461 [Multi-domain]  Cd Length: 442  Bit Score: 82.75  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFW-GYPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:TIGR01134  39 GNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSSGLENAQPFVvNSPYGGLALAHNGNLVNADELRRELEEE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  209 GMRFMSECDSELIAVYLADKMRSGVTLEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEI 288
Cdd:TIGR01134 119 GRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESC 198

                         170       180
                  ....*....|....*....|..
gi 167041154  289 AIRTLLPQEIDTYDPyeGEVKV 310
Cdd:TIGR01134 199 ALDILGAEFVRDVEP--GEVVV 218
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 130-302 2.44e-17

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 82.00  E-value: 2.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFWG-YPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:PRK05793  54 GEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGASDLDNAQPLVAnYKLGSIAIAHNGNLVNADVIRELLEDG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 209 GMRFMSECDSELIAVYLADKMRSGvtLEQGMKDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVLYESDDLVALGSEEI 288
Cdd:PRK05793 134 GRIFQTSIDSEVILNLIARSAKKG--LEKALVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKLGDDYILSSESC 211

                        170       180
                 ....*....|....*....|..
gi 167041154 289 A--------IRTLLPQEIDTYD 302
Cdd:PRK05793 212 AldtigaefIRDVEPGEIVIID 233
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 132-290 3.63e-16

glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 273462 [Multi-domain]  Cd Length: 607  Bit Score: 78.84  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  132 SLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHpfwgyPFSDMS----VVHNGQLTSYWNNRRILER 207
Cdd:TIGR01135  40 KLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKPTDENAH-----PHTDEGgriaVVHNGIIENYAELREELEA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  208 KGMRFMSECDSELIAVYLADKMRSGVTLEQGMKDSIKELDGVFTYLVATKNSLGMakdVMAAKpmvlYESDDLVALGSEE 287
Cdd:TIGR01135 115 RGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYALAVLHADHPET---LVAAR----SGSPLIVGLGDGE 187


                  ...
gi 167041154  288 IAI 290
Cdd:TIGR01135 188 NFV 190
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 130-258 1.17e-15

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: 74.41  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFWGYPfSDMSVVHNGQLTSYWNNRRILERKG 209
Cdd:cd00714   38 DGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPTDVNAHPHRSCD-GEIAVVHNGIIENYAELKEELEAKG 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 167041154 210 MRFMSECDSELIAVYLADKMRSGVTLEQGMKDSIKELDGVFTYLVATKN 258
Cdd:cd00714  117 YKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYALAVISKD 165
PLN02440 PLN02440
amidophosphoribosyltransferase
 130-293 9.08e-15

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 74.33  E-value: 9.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFW-GYPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:PLN02440  39 GNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGASSLKNVQPFVaNYRFGSIGVAHNGNLVNYEELRAKLEEN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 209 GMRFMSECDSE----LIAVYLADKMRSGVTleqgmkDSIKELDGVFTYLVATKNSLGMAKDVMAAKPMVL-YESDDLVAL 283
Cdd:PLN02440 119 GSIFNTSSDTEvllhLIAISKARPFFSRIV------DACEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMgRRSNGAVVF 192

                        170
                 ....*....|
gi 167041154 284 GSEEIAIRTL 293
Cdd:PLN02440 193 ASETCALDLI 202
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 159-286 3.35e-13

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: 65.40  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  159 AIGHSRMATeSGVDIRSAHPFWgYPFSDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELIAvyladkmrsgVTLEQG 238
Cdd:pfam13522  13 ALGHVRLAI-VDLPDAGNQPML-SRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLL----------ALYEEW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 167041154  239 MKDSIKELDGVFTYLV--ATKNSLGMAKDVMAAKPMVLYESDDLVALGSE 286
Cdd:pfam13522  81 GEDCLERLRGMFAFAIwdRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 130-302 1.95e-12

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 67.73  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFWGyPFSDMSVVHNG------QLtsywnnRR 203
Cdd:COG0449   39 DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAPSDENAHPHTS-CSGRIAVVHNGiienyaEL------RE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 204 ILERKGMRFMSECDSELIAVYLADKMRSGVTLEQGMKDSIKELDGVFTYLV-----------ATKNS-----LG-----M 262
Cdd:COG0449  112 ELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYALAVisadepdrivaARKGSplvigLGegenfL 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 167041154 263 AKDVMAakpmVLYESDDLVALGSEEIAIrtLLPQEIDTYD 302
Cdd:COG0449  192 ASDVPA----LLPYTRRVIYLEDGEIAV--LTRDGVEIYD 225
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 127-289 1.18e-11

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 65.04  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 127 LSLGKSLELVK-----DLGDANTVSKQYGLDKIKGTH-AIGHSRMATESGVDIRSAHPFWGYPfSDMSVVHNGQLTSYWN 200
Cdd:PTZ00295  60 ISSGGELKTTKyasdgTTSDSIEILKEKLLDSHKNSTiGIAHTRWATHGGKTDENAHPHCDYK-KRIALVHNGTIENYVE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 201 NRRILERKGMRFMSECDSELIAVYLADKMRSGVTLEQGMKDSIKELDGVFTYLVATK---NSLGMAKDvmaAKPMVLYES 277
Cdd:PTZ00295 139 LKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISRLQGTWGLCIIHKdnpDSLIVARN---GSPLLVGIG 215

                        170
                 ....*....|..
gi 167041154 278 DDLVALGSEEIA 289
Cdd:PTZ00295 216 DDSIYVASEPSA 227
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
130-274 2.47e-11

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 64.29  E-value: 2.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTVSKQYGLDKIKGTHAIGHSRMATESGVDIRSAHPFWgypfsDMS----VVHNG------QLtsyw 199
Cdd:PRK00331  39 DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKPTERNAHPHT-----DCSgriaVVHNGiienyaEL---- 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167041154 200 nnRRILERKGMRFMSECDSELIAVYLADKMRSGVTLEQGMKDSIKELDGVFTYLVATKNslgmAKDVM-AAK---PMVL 274
Cdd:PRK00331 110 --KEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYALAVIDKD----EPDTIvAARngsPLVI 182
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 130-274 3.63e-10

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 60.92  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 130 GKSLELVKDLGDANTvSKQYGLDKIKGTHA-IGHSRMATESGVDIRSAHPFWGYPFSDMSVVHNGQLTSYWNNRRILERK 208
Cdd:PLN02981  60 GKIESLVRSVYEEVA-ETDLNLDLVFENHAgIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRH 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167041154 209 GMRFMSECDSELI---AVYLADKM---RSGVTLEQGMKDSIKELDGVFTYLVatkNSLGMAKDVMAAK---PMVL 274
Cdd:PLN02981 139 GFTFESDTDTEVIpklAKFVFDKLneeEGDVTFSQVVMEVMRQLEGAYALIF---KSPHYPNELVACKrgsPLLL 210
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
152-260 1.64e-09

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 57.28  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 152 DKIKGTHAIGHSRMATESGVDIRSAHPFWGYPFSDMsvvHNGQLTSYWNNRRILERK-----GMRFMSECDSELIAVYLA 226
Cdd:COG0121   72 RPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFA---HNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELAFALLL 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 167041154 227 DKMRSGV-TLEQGMKDSIKELD------GVFTYLVATKNSL 260
Cdd:COG0121  149 SRLRDGGpDPAEALAEALRELAelarapGRLNLLLSDGERL 189
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 162-286 2.98e-09

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: 433289 [Multi-domain]  Cd Length: 123  Bit Score: 54.06  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  162 HSRMATesgVDIRSAH-PFWGYPFSDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELIAVYLAdkmrsgvtlEQGMK 240
Cdd:pfam13537   1 HRRLSI---IDLEGGAqPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE---------AEWGE 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 167041154  241 DSIKELDGVFTYLV--ATKNSLGMAKDVMAAKPMVLYESDD-LVALGSE 286
Cdd:pfam13537  69 DCVDRLNGMFAFAIwdRRRQRLFLARDRFGIKPLYYGRDDGgRLLFASE 117
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 141-256 1.86e-08

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: 54.32  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 141 DANTVSKQYgldKIKGTHAIGHSRMATESGVDIRSAHPF----WgypfsdmSVVHNGQLTSYWNNRRILERKGMRFM-SE 215
Cdd:cd01908   68 DINLESLAR---PIKSPLVLAHVRAATVGPVSLENCHPFtrgrW-------LFAHNGQLDGFRLLRRRLLRLLPRLPvGT 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 167041154 216 CDSELIAVYLADKMRSG-----VTLEQGMKDSIKELDGVFTYLVAT 256
Cdd:cd01908  138 TDSELAFALLLSRLLERdpldpAELLDAILQTLRELAALAPPGRLN 183
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 1-37 4.56e-08

Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis


Pssm-ID: 440136 [Multi-domain]  Cd Length: 558  Bit Score: 54.07  E-value: 4.56e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 167041154   1 MCGIAGLIHKGKTVNiGKELKDMLQALKHRGPDSTGY 37
Cdd:COG0367    1 MCGIAGIIDFDGGAD-REVLERMLDALAHRGPDGSGI 36
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 2-37 1.33e-07

Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.


Pssm-ID: 238364 [Multi-domain]  Cd Length: 220  Bit Score: 51.40  E-value: 1.33e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 167041154   2 CGIAGLIHKGKTVNIGKELKDMLQALKHRGPDSTGY 37
Cdd:cd00712    1 CGIAGIIGLDGASVDRATLERMLDALAHRGPDGSGI 36
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 157-290 2.10e-06

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 48.94  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 157 THAIGHSRMATesgVDIRSAHPfwgyPFSDMS----VVHNGQLTSYWNNRRILERKGMRFMSECDSELI-AVYladkmrs 231
Cdd:PTZ00077  48 YNILAHERLAI---VDLSDGKQ----PLLDDDetvaLMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIgHLY------- 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167041154 232 gvtLEQGMKDSIKELDGVFTYLV--ATKNSLGMAKDVMAAKPMVL-YESDDLVALGSEEIAI 290
Cdd:PTZ00077 114 ---KEYGPKDFWNHLDGMFATVIydMKTNTFFAARDHIGIIPLYIgYAKDGSIWFSSELKAL 172
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 159-295 3.47e-05

Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.


Pssm-ID: 238364 [Multi-domain]  Cd Length: 220  Bit Score: 44.09  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154 159 AIGHSRMATesgVDIRSAH-PFWGyPFSDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELI-AVYladkmrsgvtLE 236
Cdd:cd00712   43 ALGHRRLSI---IDLSGGAqPMVS-EDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVIlHLY----------EE 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041154 237 QGmKDSIKELDGVFTYLV--ATKNSLGMAKDVMAAKPMVLYESDDLVALGSEeiaIRTLLP 295
Cdd:cd00712  109 WG-EDCLERLNGMFAFALwdKRKRRLFLARDRFGIKPLYYGRDGGGLAFASE---LKALLA 165
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 160-223 4.61e-05

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 44.87  E-value: 4.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167041154 160 IGHSRMATESGVDIRSAHPfWGYPFSDMSVVHNGQLTSYWNNRRILERKGMRFMSECDSELIAV 223
Cdd:PTZ00394 101 IAHTRWATHGGVCERNCHP-QQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVISV 163
GATase_4 pfam13230
Glutamine amidotransferases class-II; This family captures members that are not found in ...
 154-231 1.88e-03

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


Pssm-ID: 433047 [Multi-domain]  Cd Length: 272  Bit Score: 39.24  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041154  154 IKGTHAIGHSRMATESGVDIRSAHPF----WGypfSDMSVVHNGQLtsywnnRRILERKGMRFM--SECDSELIAVYLAD 227
Cdd:pfam13230  69 IRSRNVIAHIRKATQGRVTLENTHPFmrelWG---RYWIFAHNGDL------KGYAPKLSGRFQpvGSTDSELAFCWLLD 139


                  ....
gi 167041154  228 KMRS 231
Cdd:pfam13230 140 RLAS 143
asnB PRK09431
asparagine synthetase B; Provisional
 1-36 2.15e-03

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 39.51  E-value: 2.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 167041154   1 MCGIAGLIH-KGKTVNIGKELKDMLQALKHRGPDSTG 36
Cdd:PRK09431   1 MCGIFGILDiKTDADELRKKALEMSRLMRHRGPDWSG 37
 
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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