NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1545384385|ref|WP_126540492|]
View 

glutamine amidotransferase family protein [Oharaeibacter diazotrophicus]

Protein Classification

class II glutamine amidotransferase( domain architecture ID 10112366)

class II glutamine amidotransferase hydrolyzes ammonia from glutamine and transfers the amino group to the appropriate substrate; similar to Sinorhizobium meliloti glutamine amidotransferase-like protein GlxB

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-296 2.21e-83

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: 251.42  E-value: 2.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385   2 CGIVGLFLKDEalRPDLGRLLSEMLVTMTDRGP-DSAGIAIYGAetpgrtkitvqspapardfpglaealaaatgsavei 80
Cdd:cd01907     1 CGIFGIMSKDG--EPFVGALLVEMLDAMQERGPgDGAGFALYGD------------------------------------ 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385  81 arrdthgvltvaedaaaavraalttvaPEVRVMGVGAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTL 160
Cdd:cd01907    43 ---------------------------PDAFVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWIAHTRQPTNSAVWWY 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 161 GAHPFSTGpDQCLVHNGSLSNHNNVRRVLRHRGARFETENDSEVAAAYLTDAMAGGRDLGAALAGALADLDG-------- 232
Cdd:cd01907    96 GAHPFSIG-DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYYKHIIRMPEEerelllal 174

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545384385 233 -----------FFTFVVGTRSGFGVLRDPIACKPAVMAETDAYVAFGSEYRALAGLPGIETARVWEPEPATVYFW 296
Cdd:cd01907   175 rltyrladldgPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKVWEPRPGEYVIW 249
 
Name Accession Description Interval E-value
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-296 2.21e-83

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: 251.42  E-value: 2.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385   2 CGIVGLFLKDEalRPDLGRLLSEMLVTMTDRGP-DSAGIAIYGAetpgrtkitvqspapardfpglaealaaatgsavei 80
Cdd:cd01907     1 CGIFGIMSKDG--EPFVGALLVEMLDAMQERGPgDGAGFALYGD------------------------------------ 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385  81 arrdthgvltvaedaaaavraalttvaPEVRVMGVGAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTL 160
Cdd:cd01907    43 ---------------------------PDAFVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWIAHTRQPTNSAVWWY 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 161 GAHPFSTGpDQCLVHNGSLSNHNNVRRVLRHRGARFETENDSEVAAAYLTDAMAGGRDLGAALAGALADLDG-------- 232
Cdd:cd01907    96 GAHPFSIG-DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYYKHIIRMPEEerelllal 174

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545384385 233 -----------FFTFVVGTRSGFGVLRDPIACKPAVMAETDAYVAFGSEYRALAGLPGIETARVWEPEPATVYFW 296
Cdd:cd01907   175 rltyrladldgPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKVWEPRPGEYVIW 249
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 116-216 2.04e-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: 79.22  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 116 GAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHP-FSTGPDQCLVHNGSLSNHNNVRRVLRHRGA 194
Cdd:TIGR01135  38 EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKPTDENAHPhTDEGGRIAVVHNGIIENYAELREELEARGH 117

                          90       100
                  ....*....|....*....|..
gi 1545384385 195 RFETENDSEVAAAYLTDAMAGG 216
Cdd:TIGR01135 118 VFSSDTDTEVIAHLIEEELREG 139
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
116-206 4.81e-16

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 78.16  E-value: 4.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 116 GAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHP-FSTGPDQCLVHNGSLSNHNNVRRVLRHRGA 194
Cdd:PRK00331   39 DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKPTERNAHPhTDCSGRIAVVHNGIIENYAELKEELLAKGH 118

                          90
                  ....*....|..
gi 1545384385 195 RFETENDSEVAA 206
Cdd:PRK00331  119 VFKSETDTEVIA 130
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 116-217 3.01e-15

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: 75.82  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 116 GAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHP-FSTGPDQCLVHNGSLSNHNNVRRVLRHRGA 194
Cdd:COG0449    39 DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAPSDENAHPhTSCSGRIAVVHNGIIENYAELREELEAKGH 118

                          90       100
                  ....*....|....*....|...
gi 1545384385 195 RFETENDSEVAAAYLTDAMAGGR 217
Cdd:COG0449   119 TFKSETDTEVIAHLIEEYLKGGG 141
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 145-270 1.79e-12

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: 63.48  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 145 GIGHTRMATeSAVTTLGAHPFSTGPDQ-CLVHNGSLSNHNNVRRVLRHRGARFETENDSEV-AAAYL-----TDAMAGGR 217
Cdd:pfam13522  13 ALGHVRLAI-VDLPDAGNQPMLSRDGRlVLVHNGEIYNYGELREELADLGHAFRSRSDTEVlLALYEewgedCLERLRGM 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1545384385 218 dlgaalagaladldgfFTFVV--GTRSGFGVLRDPIACKPAVMAETDAYVAFGSE 270
Cdd:pfam13522  92 ----------------FAFAIwdRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
 
Name Accession Description Interval E-value
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-296 2.21e-83

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: 251.42  E-value: 2.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385   2 CGIVGLFLKDEalRPDLGRLLSEMLVTMTDRGP-DSAGIAIYGAetpgrtkitvqspapardfpglaealaaatgsavei 80
Cdd:cd01907     1 CGIFGIMSKDG--EPFVGALLVEMLDAMQERGPgDGAGFALYGD------------------------------------ 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385  81 arrdthgvltvaedaaaavraalttvaPEVRVMGVGAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTL 160
Cdd:cd01907    43 ---------------------------PDAFVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWIAHTRQPTNSAVWWY 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 161 GAHPFSTGpDQCLVHNGSLSNHNNVRRVLRHRGARFETENDSEVAAAYLTDAMAGGRDLGAALAGALADLDG-------- 232
Cdd:cd01907    96 GAHPFSIG-DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYYKHIIRMPEEerelllal 174

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545384385 233 -----------FFTFVVGTRSGFGVLRDPIACKPAVMAETDAYVAFGSEYRALAGLPGIETARVWEPEPATVYFW 296
Cdd:cd01907   175 rltyrladldgPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKVWEPRPGEYVIW 249
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 2-294 3.19e-30

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: 113.70  E-value: 3.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385   2 CGIVGLFLKDEALRPDLGRLLSeMLVTMTDRGPDSAGIAIYGAETpgrtkitvqspapardfpglaealaaatgsaveia 81
Cdd:cd00352     1 CGIFGIVGADGAASLLLLLLLR-GLAALEHRGPDGAGIAVYDGDG----------------------------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385  82 rrdthgvltvaedaaaavraalttvapevrvmgvgaaVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLG 161
Cdd:cd00352    45 -------------------------------------LFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATNGLPSEAN 87

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 162 AHPFSTGPDQ-CLVHNGSLSNHNNVRRVLRHRGARFETENDSEVAAAYLTDAMAGGRDLGAALAGALADLDGF-FTFVVG 239
Cdd:cd00352    88 AQPFRSEDGRiALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGGLFEAVEDALKRLDGPFaFALWDG 167

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1545384385 240 TRSGFGVLRDPIACKPAVMAET-DAYVAFGSEYRALAGLPGietARVWEPEPATVY 294
Cdd:cd00352   168 KPDRLFAARDRFGIRPLYYGITkDGGLVFASEPKALLALPF---KGVRRLPPGELL 220
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 119-216 1.31e-16

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: 76.72  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 119 VEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHP-FSTGPDQCLVHNGSLSNHNNVRRVLRHRGARFE 197
Cdd:cd00714    41 LEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPTDVNAHPhRSCDGEIAVVHNGIIENYAELKEELEAKGYKFE 120

                          90
                  ....*....|....*....
gi 1545384385 198 TENDSEVAAAYLTDAMAGG 216
Cdd:cd00714   121 SETDTEVIAHLIEYYYDGG 139
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 116-216 2.04e-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: 79.22  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 116 GAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHP-FSTGPDQCLVHNGSLSNHNNVRRVLRHRGA 194
Cdd:TIGR01135  38 EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKPTDENAHPhTDEGGRIAVVHNGIIENYAELREELEARGH 117

                          90       100
                  ....*....|....*....|..
gi 1545384385 195 RFETENDSEVAAAYLTDAMAGG 216
Cdd:TIGR01135 118 VFSSDTDTEVIAHLIEEELREG 139
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
116-206 4.81e-16

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 78.16  E-value: 4.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 116 GAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHP-FSTGPDQCLVHNGSLSNHNNVRRVLRHRGA 194
Cdd:PRK00331   39 DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKPTERNAHPhTDCSGRIAVVHNGIIENYAELKEELLAKGH 118

                          90
                  ....*....|..
gi 1545384385 195 RFETENDSEVAA 206
Cdd:PRK00331  119 VFKSETDTEVIA 130
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 116-217 3.01e-15

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: 75.82  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 116 GAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHP-FSTGPDQCLVHNGSLSNHNNVRRVLRHRGA 194
Cdd:COG0449    39 DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAPSDENAHPhTSCSGRIAVVHNGIIENYAELREELEAKGH 118

                          90       100
                  ....*....|....*....|...
gi 1545384385 195 RFETENDSEVAAAYLTDAMAGGR 217
Cdd:COG0449   119 TFKSETDTEVIAHLIEEYLKGGG 141
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 145-270 1.79e-12

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: 63.48  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 145 GIGHTRMATeSAVTTLGAHPFSTGPDQ-CLVHNGSLSNHNNVRRVLRHRGARFETENDSEV-AAAYL-----TDAMAGGR 217
Cdd:pfam13522  13 ALGHVRLAI-VDLPDAGNQPMLSRDGRlVLVHNGEIYNYGELREELADLGHAFRSRSDTEVlLALYEewgedCLERLRGM 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1545384385 218 dlgaalagaladldgfFTFVV--GTRSGFGVLRDPIACKPAVMAETDAYVAFGSE 270
Cdd:pfam13522  92 ----------------FAFAIwdRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
 114-295 5.74e-11

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: 62.72  E-value: 5.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 114 GVGAAVE------IFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHPF---STGPDQCLVHNGSLSNHNN 184
Cdd:TIGR01134  31 SAGISVFdgnrfrLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSSGLENAQPFvvnSPYGGLALAHNGNLVNADE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 185 VRRVLRHRGARFETENDSEVAAAYLTDAMAGGRDLGAALAGALADLDGFFTFVVGTRSGFGVLRDPIACKPAVMAETDAY 264
Cdd:TIGR01134 111 LRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRRGDG 190

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1545384385 265 VAFGSEYRALAGLpGIETARVWEPEPATVYF 295
Cdd:TIGR01134 191 YVVASESCALDIL-GAEFVRDVEPGEVVVIF 220
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 117-297 1.16e-10

asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273676 [Multi-domain]  Cd Length: 466  Bit Score: 61.97  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 117 AAVEIFKEVGKPADVVRR-----FGVAAMAGTHGIGHTRMAteSAVTTLGAHPFS-TGPDQCLVHNGSLSNHNNVRRVLR 190
Cdd:TIGR01536  10 KAVEEDEAIKRMSDTIAHrgpdaSGIEYKDGNAILGHRRLA--IIDLSGGAQPMSnEGKTYVIVFNGEIYNHEELREELE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 191 HRGARFETENDSEVA-AAYLT------DAMAGgrdlgaalagaladldgFFTFVV--GTRSGFGVLRDPIACKPAVMAET 261
Cdd:TIGR01536  88 AKGYTFQTDSDTEVIlHLYEEwgeecvDRLDG-----------------MFAFALwdSEKGELFLARDRFGIKPLYYAYD 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1545384385 262 DAYVAFGSEYRALAGLPGIetarvwEPEPATVYFWD 297
Cdd:TIGR01536 151 GGQLYFASEIKALLAHPNI------KPFPDGAALAP 180
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 121-204 2.02e-09

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 58.22  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 121 IFKEVGKPADVVRR-FGVAAMAGTH---------GIGHTRMATESAVTTLGAHPFSTGP--DQCLVHNGSLSNHNNVRRV 188
Cdd:PLN02981   55 VFREEGKIESLVRSvYEEVAETDLNldlvfenhaGIAHTRWATHGPPAPRNSHPQSSGPgnEFLVVHNGIITNYEVLKET 134

                          90
                  ....*....|....*.
gi 1545384385 189 LRHRGARFETENDSEV 204
Cdd:PLN02981  135 LLRHGFTFESDTDTEV 150
PLN02440 PLN02440
amidophosphoribosyltransferase
 123-293 3.40e-09

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 57.38  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 123 KEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHPFSTGPDQ---CLVHNGSLSNHNNVRRVLRHRGARFETE 199
Cdd:PLN02440   46 TGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGASSLKNVQPFVANYRFgsiGVAHNGNLVNYEELRAKLEENGSIFNTS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 200 NDSEVAAAYLTDAMAggrdlgaalagaladlDGFFTFVVGT----RSGFGVL----------RDPIACKPAVMA--ETDA 263
Cdd:PLN02440  126 SDTEVLLHLIAISKA----------------RPFFSRIVDAceklKGAYSMVfltedklvavRDPHGFRPLVMGrrSNGA 189

                         170       180       190
                  ....*....|....*....|....*....|
gi 1545384385 264 YVaFGSEYRALaGLPGIETARVWEPEPATV 293
Cdd:PLN02440  190 VV-FASETCAL-DLIGATYEREVNPGEVIV 217
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
 142-270 1.51e-08

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: 54.39  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 142 GTHGIGHTRMATESAVTTLGAHPF---STGPDQCLVHNGSLSNHNNVRRVLRHRGARFETENDSEV-----AAAY----L 209
Cdd:cd00715    64 GNIAIGHVRYSTAGSSSLENAQPFvvnSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVilhliARSLakddL 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 210 TDAMA-------GGrdlgaalagaladldgfFTFVVGTRSGFGVLRDPIACKPAVMA--ETDAYVaFGSE 270
Cdd:cd00715   144 FEAIIdalervkGA-----------------YSLVIMTADGLIAVRDPHGIRPLVLGklEGDGYV-VASE 195
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 125-206 1.80e-08

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 55.41  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 125 VGKPAD---VVRRFGVAAMAGTH-GIGHTRMATESAVTTLGAHPFStgpDQ----CLVHNGSLSNHNNVRRVLRHRGARF 196
Cdd:PTZ00295   74 DGTTSDsieILKEKLLDSHKNSTiGIAHTRWATHGGKTDENAHPHC---DYkkriALVHNGTIENYVELKSELIAKGIKF 150

                          90
                  ....*....|
gi 1545384385 197 ETENDSEVAA 206
Cdd:PTZ00295  151 RSETDSEVIA 160
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 138-209 6.95e-08

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: 53.49  E-value: 6.95e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545384385 138 AAMAGTHGIGHTRMATESAVTTLGAHPF---STGPDQCLVHNGSLSNHNNVRRVLRHRGARFETENDSEVAAAYL 209
Cdd:COG0034    67 ERLKGNIAIGHVRYSTTGSSSLENAQPFyvnSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLI 141
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 116-204 1.54e-07

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 52.34  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 116 GAAVEIFKEVGKPADVVRRFGVAAMAGTHGIGHTRMATESAVTTLGAHP----FSTGPdQCLVHNGSLSNHNNVRRVLRH 191
Cdd:PRK05793   54 GEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGASDLDNAQPlvanYKLGS-IAIAHNGNLVNADVIRELLED 132

                          90
                  ....*....|...
gi 1545384385 192 RGARFETENDSEV 204
Cdd:PRK05793  133 GGRIFQTSIDSEV 145
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 145-294 2.07e-07

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: 52.15  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 145 GIGHTRMAT--ESAvttLGAHPFSTGPDQ-CLVHNGSLSNHNNVRRVLRHRGARFETENDSEVA-AAYL---TDAMA--- 214
Cdd:COG0367    43 ALGHRRLSIidLSE---GGHQPMVSEDGRyVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVIlHAYEewgEDCLErln 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 215 GgrdlgaalagaladldgFFTFVV---GTRSGFGVlRDPIACKPAVMAETDAYVAFGSEYRALAGLPGIETARVWE---- 287
Cdd:COG0367   120 G-----------------MFAFAIwdrRERRLFLA-RDRFGIKPLYYAEDGGGLAFASELKALLAHPGVDRELDPEalae 181

                         170
                  ....*....|....
gi 1545384385 288 -------PEPATVY 294
Cdd:COG0367   182 yltlgyvPAPRTIF 195
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 148-274 2.86e-07

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: 48.28  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 148 HTRMATEsaVTTLGAHPFSTGPDQ--CLVHNGSLSNHNNVRRVLRHRGARFETENDSEV-----AAAYLTDA------Ma 214
Cdd:pfam13537   1 HRRLSII--DLEGGAQPMVSSEDGryVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVilhlyEAEWGEDCvdrlngM- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1545384385 215 ggrdlgaalagaladldgfFTFVVGTRSGFGVL--RDPIACKPAVMAETD-AYVAFGSEYRAL 274
Cdd:pfam13537  78 -------------------FAFAIWDRRRQRLFlaRDRFGIKPLYYGRDDgGRLLFASELKAL 121
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 145-294 3.40e-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: 49.86  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 145 GIGHTRMAT--ESAvttlGAHPFSTGPDQ-CLVHNGSLSNHNNVRRVLRHRGARFETENDSEVA-AAYL---TDAMA--- 214
Cdd:cd00712    43 ALGHRRLSIidLSG----GAQPMVSEDGRlVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVIlHLYEewgEDCLErln 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 215 GgrdlgaalagaladldgFFTFVV---GTRSGFGVlRDPIACKPAVMAETDAYVAFGSEYRALAGLPGIET--------- 282
Cdd:cd00712   119 G-----------------MFAFALwdkRKRRLFLA-RDRFGIKPLYYGRDGGGLAFASELKALLALPGVPReldeaalae 180

                         170
                  ....*....|....
gi 1545384385 283 --ARVWEPEPATVY 294
Cdd:cd00712   181 ylAFQYVPAPRTIF 194
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 146-211 6.04e-07

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: 49.69  E-value: 6.04e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1545384385 146 IGHTRMATESAVTTLGAHPFSTGPdQCLVHNGSLSNHNNVRR-VLRHRGARFETENDSEVAAAYLTD 211
Cdd:cd01908    84 LAHVRAATVGPVSLENCHPFTRGR-WLFAHNGQLDGFRLLRRrLLRLLPRLPVGTTDSELAFALLLS 149
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
143-216 7.81e-06

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 46.11  E-value: 7.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1545384385 143 THGIGHTRMATESAVTTLGAHPFsTGPDQCLVHNGSLSNHNNVRRVLR-----HRGARFETENDSEVAAAYLTDAMAGG 216
Cdd:COG0121    77 RLVIAHVRKATVGPVSLENTHPF-RGGRWLFAHNGQLDGFDRLRRRLAeelpdELYFQPVGTTDSELAFALLLSRLRDG 154
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 145-206 1.03e-04

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 43.71  E-value: 1.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1545384385 145 GIGHTRMATESAVTTLGAHP-FSTGPDQCLVHNGSLSNHNNVRRVLRHRGARFETENDSEVAA 206
Cdd:PTZ00394  100 GIAHTRWATHGGVCERNCHPqQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVIS 162
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 143-274 1.05e-03

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 40.47  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 143 THGIGHTRMATESAVTtlGAHPFSTgPDQ--CLVHNGSLSNHNNVRRVLRHRGARFETENDSEVAAAYLTDAMAGGrdlg 220
Cdd:PTZ00077   48 YNILAHERLAIVDLSD--GKQPLLD-DDEtvALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKD---- 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1545384385 221 aalagALADLDGFFTFVV--GTRSGFGVLRDPIACKPAVMA-ETDAYVAFGSEYRAL 274
Cdd:PTZ00077  121 -----FWNHLDGMFATVIydMKTNTFFAARDHIGIIPLYIGyAKDGSIWFSSELKAL 172
asnB PRK09431
asparagine synthetase B; Provisional
 141-277 8.70e-03

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 37.58  E-value: 8.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545384385 141 AGTHGI-GHTRMATESaVTTLGAHPFSTGPDQCLVHNGSLSNHNNVRRVLRHRGArFETENDSEVAAA-YLT-------- 210
Cdd:PRK09431   40 ASDNAIlGHERLSIVD-VNGGAQPLYNEDGTHVLAVNGEIYNHQELRAELGDKYA-FQTGSDCEVILAlYQEkgpdfldd 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1545384385 211 -DAMaggrdlgaalagaladldgfFTFVV--GTRSGFGVLRDPIACKPAVMAETDA-YVAFGSEYRALAGL 277
Cdd:PRK09431  118 lDGM--------------------FAFALydSEKDAYLIARDPIGIIPLYYGYDEHgNLYFASEMKALVPV 168
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH