NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1173250071|ref|WP_081110765|]
View 

glutamine--fructose-6-phosphate transaminase (isomerizing), partial [Aggregatibacter actinomycetemcomitans]

Protein Classification

glutamine--fructose-6-phosphate aminotransferase( domain architecture ID 1005808)

glutamine--fructose-6-phosphate aminotransferase catalyzes the formation of glucosamine 6-phosphate from fructose-6-phosphate and glutamine in the hexosamine biosynthetic pathway

CATH:  3.40.50.10490|3.60.20.10
EC:  2.6.1.16
Gene Ontology:  GO:0006541|GO:0097367|GO:0004360|GO:0005975|GO:0006002
PubMed:  12044898

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GlmS super family cl33881
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 1-349 0e+00

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


The actual alignment was detected with superfamily member COG0449:

Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 613.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSqHELQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGE 80
Cdd:COG0449     1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDD-GGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  81 PSEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYG 158
Cdd:COG0449    80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 159 MVVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDGNKVEREAHDSN 238
Cdd:COG0449   160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 239 LENDAAEKGKYRHFMQKEIYEQPTALINTMEGRVTHNNVIVEAIGNSAKEILEKVEHVQIVACGTSYNSGMVARYWFESL 318
Cdd:COG0449   240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1173250071 319 AGISCDIEIASEFRYRKFVVRPNSLLITLSQ 349
Cdd:COG0449   320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQ 350
 
Name Accession Description Interval E-value
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 1-349 0e+00

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: 613.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSqHELQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGE 80
Cdd:COG0449     1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDD-GGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  81 PSEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYG 158
Cdd:COG0449    80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 159 MVVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDGNKVEREAHDSN 238
Cdd:COG0449   160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 239 LENDAAEKGKYRHFMQKEIYEQPTALINTMEGRVTHNNVIVEAIGNSAKEILEKVEHVQIVACGTSYNSGMVARYWFESL 318
Cdd:COG0449   240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1173250071 319 AGISCDIEIASEFRYRKFVVRPNSLLITLSQ 349
Cdd:COG0449   320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQ 350
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
1-349 0e+00

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 603.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHeLQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGE 80
Cdd:PRK00331    1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGG-LEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  81 PSEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYG 158
Cdd:PRK00331   80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 159 MVVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDGNKVEREAHDSN 238
Cdd:PRK00331  160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 239 LENDAAEKGKYRHFMQKEIYEQPTALINTMEGRVTHNNVIVEAIgnsakEILEKVEHVQIVACGTSYNSGMVARYWFESL 318
Cdd:PRK00331  240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELGEGELAD-----EDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1173250071 319 AGISCDIEIASEFRYRKFVVRPNSLLITLSQ 349
Cdd:PRK00331  315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQ 345
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 2-349 0e+00

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: 534.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHeLQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGEP 81
Cdd:TIGR01135   1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGK-LFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  82 SEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYGM 159
Cdd:TIGR01135  80 TDENAHPHTDegGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 160 VVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDGNKVEREAHDSNL 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 240 ENDAAEKGKYRHFMQKEIYEQPTALINTMEGRVTHNNVIVEAIGnsAKEILEKVEHVQIVACGTSYNSGMVARYWFESLA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 1173250071 320 GISCDIEIASEFRYRKFVVRPNSLLITLSQ 349
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQ 347
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 2-215 5.58e-131

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: 372.55  E-value: 5.58e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQhELQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGEP 81
Cdd:cd00714     1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDG-SLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  82 SEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYGM 159
Cdd:cd00714    80 TDVNAHPHRScdGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1173250071 160 VVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEI 215
Cdd:cd00714   160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 66-174 3.75e-18

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: 79.66  E-value: 3.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  66 GGTGIAHTRWATHGEPSEENaHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEwemrtagsll 143
Cdd:pfam13522  10 GGVALGHVRLAIVDLPDAGN-QPMLSrdGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYE---------- 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1173250071 144 EAVQKVVKQLTGAYGMVVMDRmQPEHLVAAR 174
Cdd:pfam13522  79 EWGEDCLERLRGMFAFAIWDR-RRRTLFLAR 108
 
Name Accession Description Interval E-value
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 1-349 0e+00

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: 613.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSqHELQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGE 80
Cdd:COG0449     1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDD-GGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  81 PSEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYG 158
Cdd:COG0449    80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 159 MVVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDGNKVEREAHDSN 238
Cdd:COG0449   160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 239 LENDAAEKGKYRHFMQKEIYEQPTALINTMEGRVTHNNVIVEAIGNSAKEILEKVEHVQIVACGTSYNSGMVARYWFESL 318
Cdd:COG0449   240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1173250071 319 AGISCDIEIASEFRYRKFVVRPNSLLITLSQ 349
Cdd:COG0449   320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQ 350
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
1-349 0e+00

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 603.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHeLQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGE 80
Cdd:PRK00331    1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGG-LEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  81 PSEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYG 158
Cdd:PRK00331   80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 159 MVVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDGNKVEREAHDSN 238
Cdd:PRK00331  160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 239 LENDAAEKGKYRHFMQKEIYEQPTALINTMEGRVTHNNVIVEAIgnsakEILEKVEHVQIVACGTSYNSGMVARYWFESL 318
Cdd:PRK00331  240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELGEGELAD-----EDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1173250071 319 AGISCDIEIASEFRYRKFVVRPNSLLITLSQ 349
Cdd:PRK00331  315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQ 345
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 2-349 0e+00

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: 534.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHeLQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGEP 81
Cdd:TIGR01135   1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGK-LFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  82 SEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYGM 159
Cdd:TIGR01135  80 TDENAHPHTDegGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 160 VVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDGNKVEREAHDSNL 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 240 ENDAAEKGKYRHFMQKEIYEQPTALINTMEGRVTHNNVIVEAIGnsAKEILEKVEHVQIVACGTSYNSGMVARYWFESLA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 1173250071 320 GISCDIEIASEFRYRKFVVRPNSLLITLSQ 349
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQ 347
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 2-215 5.58e-131

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: 372.55  E-value: 5.58e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQhELQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGEP 81
Cdd:cd00714     1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDG-SLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  82 SEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYGM 159
Cdd:cd00714    80 TDVNAHPHRScdGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1173250071 160 VVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEI 215
Cdd:cd00714   160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 1-349 3.18e-86

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 272.67  E-value: 3.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHELQRVRCLGK------VKALDDAVKKTPLIGGTGIAHTR 74
Cdd:PTZ00295   24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELKTTKYASDgttsdsIEILKEKLLDSHKNSTIGIAHTR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  75 WATHGEPSEENAHPHV--SGNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQ 152
Cdd:PTZ00295  104 WATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISR 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 153 LTGAYGMVVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDgNKVER 232
Cdd:PTZ00295  184 LQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQ-RRVEK 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 233 EAHdsnlENDAAEKGKYRHFMQKEIYEQPTALINTME--GRVT--HNNVIVEAIGNSAKEILeKVEHVQIVACGTSYNSG 308
Cdd:PTZ00295  263 IPE----EVIEKSPEPYPHWTLKEIFEQPIALSRALNngGRLSgyNNRVKLGGLDQYLEELL-NIKNLILVGCGTSYYAA 337

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1173250071 309 MVARYWFESLAGI-SCDIEIASEF-RYRkfVVRPNSLLITLSQ 349
Cdd:PTZ00295  338 LFAASIMQKLKCFnTVQVIDASELtLYR--LPDEDAGVIFISQ 378
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 1-335 3.48e-82

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 263.15  E-value: 3.48e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAV------AQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHELQR----VRCLGKVKALDDAV----KKTPLIG 66
Cdd:PLN02981    1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSsplvFREEGKIESLVRSVyeevAETDLNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  67 G------TGIAHTRWATHGEPSEENAHPHVSGN---FAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEW--- 134
Cdd:PLN02981   81 DlvfenhAGIAHTRWATHGPPAPRNSHPQSSGPgneFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFvfd 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 135 ---EMRTAGSLLEAVQKVVKQLTGAYGMVVMDRMQPEHLVAARSGSPLVIG---LGIGEN-------------------- 188
Cdd:PLN02981  161 klnEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkpke 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 189 -FLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDRDGNKVEREAHDS------------NLENDAAEKGKYRHFMQK 255
Cdd:PLN02981  241 fFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGGLSrpasveralstlEMEVEQIMKGNYDHYMQK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 256 EIYEQPTALINTMEGRVTHNN------VIVEAIGNSAKEIlEKVEHVQIVACGTSYNSGMVARYWFESLAGISCDIEIAS 329
Cdd:PLN02981  321 EIHEQPESLTTTMRGRLIRGGsgkakrVLLGGLKDHLKTI-RRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELAS 399


                  ....*.
gi 1173250071 330 EFRYRK 335
Cdd:PLN02981  400 DLLDRQ 405
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 1-349 5.36e-74

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 241.32  E-value: 5.36e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQ------RDIAEILINGLHRLEYRGYDSAGLAV---VNSQHELQR-----------VRCLGKVKALDD--- 57
Cdd:PTZ00394    1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAIdanIGSEKEDGTaasaptprpcvVRSVGNISQLREkvf 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  58 ----AVKKTPLIGGT----GIAHTRWATHGEPSEENAHPHVSGN--FAVVHNGIIENYEELRTLLKERGYVFTSQTDTEV 127
Cdd:PTZ00394   81 seavAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSNNgeFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 128 IAHLVEW--EMRTAGSLLEAVQKVVKQLTGAYGMVVMDRMQPEHLVAARSGSPLVIGL---------------------G 184
Cdd:PTZ00394  161 ISVLSEYlyTRKGIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdlsG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 185 IGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIY---DRDGNKVEREAHDSNLENDAAEKGKYRHFMQKEIYEQP 261
Cdd:PTZ00394  241 PLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYnaaERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 262 TALINTMEGRVTHNNVIVEAIGNSAKEI--LEKVEHVQIVACGTSYNSGMVARYWFESLAGISCDIEIASEFRYRKFVVR 339
Cdd:PTZ00394  321 ESVISSMHGRIDFSSGTVQLSGFTQQSIraILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQ 400

                         410
                  ....*....|
gi 1173250071 340 PNSLLITLSQ 349
Cdd:PTZ00394  401 RDDVCFFVSQ 410
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 2-213 2.45e-67

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: 211.15  E-value: 2.45e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVAQRDIAEILI----NGLHRLEYRGYDSAGLAVVNSqHELQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWAT 77
Cdd:cd00352     1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYDG-DGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  78 HGEPSEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTaGSLLEAVQKVVKQLTG 155
Cdd:cd00352    80 NGLPSEANAQPFRSedGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRE-GGLFEAVEDALKRLDG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173250071 156 AYGMVVMDRmQPEHLVAARSG---SPLVIGLGI-GENFLASDQLALLSVT-RRFIFLEEGDIA 213
Cdd:cd00352   159 PFAFALWDG-KPDRLFAARDRfgiRPLYYGITKdGGLVFASEPKALLALPfKGVRRLPPGELL 220
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
 2-229 2.61e-41

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: 144.91  E-value: 2.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHeLQRVRCLGKVK-ALDDAVKKTpLIGGTGIAHTRWATHGE 80
Cdd:cd00715     1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKR-FHTHKGMGLVSdVFDEEKLRR-LPGNIAIGHVRYSTAGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  81 PSEENAHPHV----SGNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAgSLLEAVQKVVKQLTGA 156
Cdd:cd00715    79 SSLENAQPFVvnspLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKD-DLFEAIIDALERVKGA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173250071 157 YGMVVMDrmqPEHLVAARSGS---PLVIG-LGIGENFLASDQLALLSVTRRFIF-LEEGDIAEITRRSVDIYDRDGNK 229
Cdd:cd00715   158 YSLVIMT---ADGLIAVRDPHgirPLVLGkLEGDGYVVASESCALDIIGAEFVRdVEPGEIVVIDDDGLESSQRAPKP 232
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 1-182 1.81e-40

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: 147.86  E-value: 1.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHeLQRVRCLGKVK-ALDDAVKKTpLIGGTGIAHTRWATHG 79
Cdd:COG0034     7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGR-FHLHKGMGLVSdVFDEEDLER-LKGNIAIGHVRYSTTG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  80 EPSEENAHPHV----SGNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMrTAGSLLEAVQKVVKQLTG 155
Cdd:COG0034    85 SSSLENAQPFYvnspFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAREL-TKEDLEEAIKEALRRVKG 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1173250071 156 AYGMVVMDrmqPEHLVAAR--SG-SPLVIG 182
Cdd:COG0034   164 AYSLVILT---GDGLIAARdpNGiRPLVLG 190
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
 2-197 9.54e-31

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: 120.89  E-value: 9.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVAQR-DIAEILINGLHRLEYRGYDSAGLAVVNSQHELQRvRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGE 80
Cdd:TIGR01134   1 CGVVGIYGQEeVAASLTYYGLYALQHRGQESAGISVFDGNRFRLH-KGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  81 PSEENAHPHVS----GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGA 156
Cdd:TIGR01134  80 SGLENAQPFVVnspyGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1173250071 157 YGMVVMDrmqPEHLVAARS--G-SPLVIGlGIGENF-LASDQLAL 197
Cdd:TIGR01134 160 YALVLMT---EDGLVAVRDphGiRPLVLG-RRGDGYvVASESCAL 200
PLN02440 PLN02440
amidophosphoribosyltransferase
 1-182 2.03e-30

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 120.55  E-value: 2.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNsQHELQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHGE 80
Cdd:PLN02440    1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVD-GNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  81 PSEENAHPHVS----GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMrtAGSLLEAVQKVVKQLTGA 156
Cdd:PLN02440   80 SSLKNVQPFVAnyrfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISK--ARPFFSRIVDACEKLKGA 157

                         170       180
                  ....*....|....*....|....*....
gi 1173250071 157 YGMVVMDRMQpehLVAARSGS---PLVIG 182
Cdd:PLN02440  158 YSMVFLTEDK---LVAVRDPHgfrPLVMG 183
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 2-215 4.42e-30

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 119.37  E-value: 4.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVA--QRDIAEILINGLHRLEYRGYDSAGLAVVNSQhELQRVRCLGKVKALDDAVKKTPLIGGTGIAHTRWATHG 79
Cdd:PRK05793   15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAVSDGE-KIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  80 EPSEENAHPHVS----GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRtaGSLLEAVQKVVKQLTG 155
Cdd:PRK05793   94 ASDLDNAQPLVAnyklGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK--KGLEKALVDAIQAIKG 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173250071 156 AYGMVVMDRmqpEHLVAARSGS---PLVIGLGIGENFLASDQLALLSVTRRFIF-LEEGDIAEI 215
Cdd:PRK05793  172 SYALVILTE---DKLIGVRDPHgirPLCLGKLGDDYILSSESCALDTIGAEFIRdVEPGEIVII 232
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-221 4.15e-24

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: 98.88  E-value: 4.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAV---AQRDIAEILINGLHRLEYRG-YDSAGLAVVNsqheLQRVRCLGKVKALD---------DAVK--KTPLIG 66
Cdd:cd01907     1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYG----DPDAFVYSSGKDMEvfkgvgypeDIARryDLEEYK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  67 GT-GIAHTRWATHGEPSEENAHPHVSGNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEA 145
Cdd:cd01907    77 GYhWIAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 146 VQKVvkqltgaygMVVMDRMQPEHLVAARSGSPL--------VIGLGiGENFLASDQLAL----LSVTRRFIFL--EEGD 211
Cdd:cd01907   157 YKHI---------IRMPEEERELLLALRLTYRLAdldgpftiIVGTP-DGFIVIRDRIKLrpavVAETDDYVAIasEECA 226

                         250
                  ....*....|
gi 1173250071 212 IAEITRRSVD 221
Cdd:cd01907   227 IREIPDRDNA 236
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 295-349 8.57e-21

SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.


Pssm-ID: 240141 [Multi-domain]  Cd Length: 126  Bit Score: 86.40  E-value: 8.57e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1173250071 295 HVQIVACGTSYNSGMVARYWFESLAGISCDIEIASEFRYRKFVVRPNSLLITLSQ 349
Cdd:cd05008     1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQ 55
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 66-174 3.75e-18

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: 79.66  E-value: 3.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  66 GGTGIAHTRWATHGEPSEENaHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEwemrtagsll 143
Cdd:pfam13522  10 GGVALGHVRLAIVDLPDAGN-QPMLSrdGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYE---------- 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1173250071 144 EAVQKVVKQLTGAYGMVVMDRmQPEHLVAAR 174
Cdd:pfam13522  79 EWGEDCLERLRGMFAFAIWDR-RRRTLFLAR 108
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 92-198 1.69e-16

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: 74.86  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  92 GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEwemrtagslLEAVQKVVKQLTGAYGMVVMDRMQPEhLV 171
Cdd:pfam13537  22 GRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE---------AEWGEDCVDRLNGMFAFAIWDRRRQR-LF 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1173250071 172 AAR--SG-SPLVIGLGIGENFL-ASDQLALL 198
Cdd:pfam13537  92 LARdrFGiKPLYYGRDDGGRLLfASELKALL 122
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 1-174 1.26e-14

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: 74.87  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVA--QRDIAEILINGLHRLEYRGYDSAGLAVvnsqhelqrvrclgkvkalDDAVkktpliggtGIAHTRWATH 78
Cdd:COG0367     1 MCGIAGIIDfdGGADREVLERMLDALAHRGPDGSGIWV-------------------DGGV---------ALGHRRLSII 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  79 GEpsEENAH-PHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHL-VEWemrtaGslleavQKVVKQLT 154
Cdd:COG0367    53 DL--SEGGHqPMVSedGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAyEEW-----G------EDCLERLN 119

                         170       180
                  ....*....|....*....|
gi 1173250071 155 GAYGMVVMDRmQPEHLVAAR 174
Cdd:COG0367   120 GMFAFAIWDR-RERRLFLAR 138
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
3-177 1.65e-14

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 72.31  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   3 GIVGAVAqRDIAEILINGLHRLEYRGYDSA--------GLAVVNSQHELQRVRCLGKvkALDDAVK---KTPLIGGTGIA 71
Cdd:COG0121     5 GYSGNVP-TDLEFLLLDPEHSLVRQSGATRegphadgwGIGWYEGDGEPRLYRDPLP--AWSDPNLrllARPIKSRLVIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  72 HTRWATHGEPSEENAHPHVSGNFAVVHNGIIENYEELRTLLKER---GYVFT--SQTDTEVIAHLV--EWEmRTAGSLLE 144
Cdd:COG0121    82 HVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEElpdELYFQpvGTTDSELAFALLlsRLR-DGGPDPAE 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1173250071 145 AVQKVVKQLT------GAYGMVVMDrmqPEHLVAARSGS 177
Cdd:COG0121   161 ALAEALRELAelarapGRLNLLLSD---GERLYATRYTS 196
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 2-198 2.78e-14

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: 71.05  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   2 CGIVGAVAQRDIA---EILINGLHRLEYRGYDSAGLAVVnsqhelqrvrclgkvkalddavkktpliGGTGIAHTRWATH 78
Cdd:cd00712     1 CGIAGIIGLDGASvdrATLERMLDALAHRGPDGSGIWID----------------------------EGVALGHRRLSII 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  79 GEpseENAH-PHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHL-VEWemrtaGslLEAVQKvvkqLT 154
Cdd:cd00712    53 DL---SGGAqPMVSedGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLyEEW-----G--EDCLER----LN 118

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1173250071 155 GAYGMVVMDRmQPEHLVAAR--SGS-PLVIGLGiGENFL-ASDQLALL 198
Cdd:cd00712   119 GMFAFALWDK-RKRRLFLARdrFGIkPLYYGRD-GGGLAfASELKALL 164
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 57-178 2.88e-13

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: 68.95  E-value: 2.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  57 DAVKKTPLIGGTGIAHTRWATHGEPSEENAHPHVSGNFAVVHNGIIENYEELRTLLKERGYVFT-SQTDTEVIAHLV--E 133
Cdd:cd01908    71 LESLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLLRLLPRLPvGTTDSELAFALLlsR 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1173250071 134 WEMR---TAGSLLEAVQKVVKQLT-----GAYGMVVMDrmqPEHLVAARSGSP 178
Cdd:cd01908   151 LLERdplDPAELLDAILQTLRELAalappGRLNLLLSD---GEYLIATRYASA 200
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 1-197 4.97e-11

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 63.58  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEIL----INGLHRLEYRGYDSAGLAVVNSQHELQRVrclgkvkalddavkktpliggtgIAHTRWA 76
Cdd:PTZ00077    1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERLA 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  77 THGepSEENAHPHVS--GNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEwemrTAGSlleavQKVVKQLT 154
Cdd:PTZ00077   58 IVD--LSDGKQPLLDddETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYK----EYGP-----KDFWNHLD 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1173250071 155 GAYGMVVMDrMQPEHLVAARSG---SPLVIGLGI-GENFLASDQLAL 197
Cdd:PTZ00077  127 GMFATVIYD-MKTNTFFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 1-197 1.70e-10

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 62.09  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIA---EILINGL-HRLEYRGYDSAGLAVvnsqhelqrvrclgkvkalddavkktplIGGTGIAHTRWA 76
Cdd:PLN02549    1 MCGILAVLGCSDDSqakRSRVLELsRRLRHRGPDWSGLYG----------------------------NEDCYLAHERLA 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  77 THGEPSEENAHPHVSGNFAVVHNGIIENYEELRTLLKErgYVFTSQTDTEVIAHLVEwemrtagsllEAVQKVVKQLTGA 156
Cdd:PLN02549   53 IMDPESGDQPLYNEDKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYE----------EHGEEFVDMLDGM 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1173250071 157 YGMVVMDRmQPEHLVAARSG---SPLVIGLGI-GENFLASDQLAL 197
Cdd:PLN02549  121 FSFVLLDT-RDNSFIAARDHigiTPLYIGWGLdGSVWFASEMKAL 164
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 289-349 5.66e-10

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 56.54  E-value: 5.66e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173250071 289 ILEKVEHVQIVACGTSYNSGMVARYWFESLAGISCDIEIASEFRYR-KFVVRPNSLLITLSQ 349
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISY 62
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 255-349 7.80e-09

Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 56.45  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071 255 KEIYEQPTALINTMEgrvtHNNVIVEAIGNSAKEilEKVEHVQIVACGTSYNSGMVARYWFESLAGISCDIEIASEF-RY 333
Cdd:COG2222     2 REIAQQPEAWRRALA----ALAAAIAALLARLRA--KPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVY 75

                          90
                  ....*....|....*.
gi 1173250071 334 RKFVVRPNSLLITLSQ 349
Cdd:COG2222    76 PAYLKLEGTLVVAISR 91
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 96-174 3.86e-08

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: 54.65  E-value: 3.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  96 VVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVE-WEMRTagslleavqkvVKQLTGAYGMVVMDRmQPEHLVAAR 174
Cdd:TIGR01536  70 IVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEeWGEEC-----------VDRLDGMFAFALWDS-EKGELFLAR 137
asnB PRK09431
asparagine synthetase B; Provisional
 1-172 4.06e-05

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 45.28  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071   1 MCGIVGAVAQRDIAEIL----INGLHRLEYRGYDSAGlavvnsqhelqrvrclgkVKALDDAVkktpliggtgIAHTRWA 76
Cdd:PRK09431    1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSG------------------IYASDNAI----------LGHERLS 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173250071  77 ----THGepseenAHPHVS--GNFAVVHNGIIENYEELRTLLKERgYVFTSQTDTEVIAHLVEwemrtagsllEAVQKVV 150
Cdd:PRK09431   53 ivdvNGG------AQPLYNedGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILALYQ----------EKGPDFL 115

                         170       180
                  ....*....|....*....|..
gi 1173250071 151 KQLTGAYGMVVMDRMQPEHLVA 172
Cdd:PRK09431  116 DDLDGMFAFALYDSEKDAYLIA 137
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 295-348 2.42e-03

A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240214 [Multi-domain]  Cd Length: 120  Bit Score: 37.56  E-value: 2.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1173250071 295 HVQIVACGTSYNSGMVARYWFESLAGISCDIEIASEFRYRKFV-VRPNSLLITLS 348
Cdd:cd05710     1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILAS 55
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 296-349 5.89e-03

SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 35.43  E-value: 5.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1173250071 296 VQIVACGTSYNSGMVARYWFESLAGISCDIEIASEFRY--RKFVVRPNSLLITLSQ 349
Cdd:cd04795     1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSY 56
 
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