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Conserved domains on  [gi|16131597|ref|NP_418185|]
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L-glutamine--D-fructose-6-phosphate aminotransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

glutamine--fructose-6-phosphate aminotransferase( domain architecture ID 11418683)

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

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
1-609 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: 1084.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:COG0449   1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  81 PSEVNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYG 158
Cdd:COG0449  80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 159 TVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESN 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 239 LQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRIS-HGQVDLSELgPNADELLSKVEHIQILACGTSYNSGMVSRYWFES 317
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDEL-NLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 318 LAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTE 397
Cdd:COG0449 319 LARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPE 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 398 IGVASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQ 476
Cdd:COG0449 398 IGVASTKAFTTQLAALYLLALYLARARGtLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGIN 477
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 477 YPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVS 556
Cdd:COG0449 478 YPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVE 557
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|...
gi 16131597 557 SDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG0449 558 ELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
 
Name Accession Description Interval E-value
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
1-609 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: 1084.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:COG0449   1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  81 PSEVNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYG 158
Cdd:COG0449  80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 159 TVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESN 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 239 LQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRIS-HGQVDLSELgPNADELLSKVEHIQILACGTSYNSGMVSRYWFES 317
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDEL-NLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 318 LAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTE 397
Cdd:COG0449 319 LARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPE 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 398 IGVASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQ 476
Cdd:COG0449 398 IGVASTKAFTTQLAALYLLALYLARARGtLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGIN 477
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 477 YPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVS 556
Cdd:COG0449 478 YPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVE 557
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|...
gi 16131597 557 SDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG0449 558 ELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
1-609 0e+00

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 1080.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:PRK00331   1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   81 PSEVNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYG 158
Cdd:PRK00331  80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  159 TVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESN 238
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  239 LQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRIshgqvDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESL 318
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRL-----DELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  319 AGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTEI 398
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  399 GVASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQY 477
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGtLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  478 PIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDaGFVSS 557
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEG-DEVAE 552
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16131597  558 DNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
2-609 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: 1019.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597     2 CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEP 81
Cdd:TIGR01135   1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVD-EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    82 SEVNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGT 159
Cdd:TIGR01135  80 TDENAHPHTDEGgrIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   160 VIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNL 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   240 QYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGpnADELLSKVEHIQILACGTSYNSGMVSRYWFESLA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   320 GIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTEIG 399
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   400 VASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYP 478
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGtLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   479 IALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSD 558
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16131597   559 NMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
2-215 1.01e-127

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: 374.09  E-value: 1.01e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   2 CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEP 81
Cdd:cd00714   1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIG-DGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  82 SEVNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGT 159
Cdd:cd00714  80 TDVNAHPHRSCDgeIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131597 160 VIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEI 215
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
289-419 1.73e-34

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: 127.03  E-value: 1.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   289 LLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYR-KSAVRRNSLMITLSQSGETADTLAGLRLSKELG 367
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16131597   368 yLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:pfam01380  81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
 
Name Accession Description Interval E-value
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
1-609 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: 1084.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:COG0449   1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  81 PSEVNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYG 158
Cdd:COG0449  80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 159 TVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESN 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 239 LQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRIS-HGQVDLSELgPNADELLSKVEHIQILACGTSYNSGMVSRYWFES 317
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDEL-NLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 318 LAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTE 397
Cdd:COG0449 319 LARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPE 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 398 IGVASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQ 476
Cdd:COG0449 398 IGVASTKAFTTQLAALYLLALYLARARGtLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGIN 477
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 477 YPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVS 556
Cdd:COG0449 478 YPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVE 557
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|...
gi 16131597 557 SDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG0449 558 ELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
1-609 0e+00

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 1080.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:PRK00331   1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   81 PSEVNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYG 158
Cdd:PRK00331  80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  159 TVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESN 238
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  239 LQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRIshgqvDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESL 318
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRL-----DELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  319 AGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTEI 398
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  399 GVASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQY 477
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGtLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  478 PIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDaGFVSS 557
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEG-DEVAE 552
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16131597  558 DNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
2-609 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: 1019.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597     2 CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEP 81
Cdd:TIGR01135   1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVD-EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    82 SEVNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGT 159
Cdd:TIGR01135  80 TDENAHPHTDEGgrIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   160 VIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNL 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   240 QYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGpnADELLSKVEHIQILACGTSYNSGMVSRYWFESLA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   320 GIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTEIG 399
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   400 VASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYP 478
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGtLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   479 IALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSD 558
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16131597   559 NMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
1-609 6.93e-175

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 511.99  E-value: 6.93e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAI------AQRDVAEILLEGLRRLEYRGYDSAGLAVvDAEGHMTR-----LRRLGKVQMLA----QAAEEHPLH 65
Cdd:PLN02981   1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAI-DNDPSLESssplvFREEGKIESLVrsvyEEVAETDLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   66 GG------TGIAHTRWATHGEPSEVNAHPHVSE---HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNW-- 134
Cdd:PLN02981  80 LDlvfenhAGIAHTRWATHGPPAPRNSHPQSSGpgnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFvf 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  135 ----ELKQGGTLREAVLRAIPQLRGAYGtVIMDSRH-PDTLLAARSGSPLVIG---LGMGEN------------------ 188
Cdd:PLN02981 160 dklnEEEGDVTFSQVVMEVMRQLEGAYA-LIFKSPHyPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkp 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  189 ---FIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIF------------DKTGAEVKRQDIESNLQYDAGDKGIYRHYM 253
Cdd:PLN02981 239 kefFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYkfenekgrggggLSRPASVERALSTLEMEVEQIMKGNYDHYM 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  254 QKEIYEQPNAIKNTLTGRISHGQVDLSE---LGPNADEL--LSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIA 328
Cdd:PLN02981 319 QKEIHEQPESLTTTMRGRLIRGGSGKAKrvlLGGLKDHLktIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  329 SEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTT 408
Cdd:PLN02981 399 SDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGAL-CVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTS 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  409 QLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLK 488
Cdd:PLN02981 478 QIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVK 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  489 EISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFA--DQDAGFVSSDNMHIIEMP 566
Cdd:PLN02981 558 EVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICskGDASSVCPSGGCRVIEVP 637
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|...
gi 16131597  567 HVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PLN02981 638 QVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
1-608 3.81e-167

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 491.07  E-value: 3.81e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHM--TRLRRLGK----VQMLAQAAEEHPLHGGTGIAHTR 74
Cdd:PTZ00295  24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELktTKYASDGTtsdsIEILKEKLLDSHKNSTIGIAHTR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   75 WATHGEPSEVNAHPHV--SEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQ 152
Cdd:PTZ00295 104 WATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISR 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  153 LRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVK- 231
Cdd:PTZ00295 184 LQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRRVEKi 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  232 -RQDIESNlqydagdKGIYRHYMQKEIYEQPNAIKNTLT--GRISHGQ--VDLSELGPNADELLSkVEHIQILACGTSYN 306
Cdd:PTZ00295 264 pEEVIEKS-------PEPYPHWTLKEIFEQPIALSRALNngGRLSGYNnrVKLGGLDQYLEELLN-IKNLILVGCGTSYY 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  307 SGMVSRYWFESLAGI-PCDVEIASEF-RYRKSavRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVR 384
Cdd:PTZ00295 336 AALFAASIMQKLKCFnTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLP-KISVVNTVGSLIAR 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  385 ESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEH--DIVHGLQALPSRIEQMLSQDKRI-EALAED 461
Cdd:PTZ00295 413 STDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKcsSLINSLHRLPTYIGMTLKSCEEQcKRIAEK 492
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  462 FSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDAD--MPVIVVAPNNELLEKLKSNIEEVRA 539
Cdd:PTZ00295 493 LKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKA 572
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131597  540 RGGQLYVFADqDAGFVSSDNMHIIEMPHVeEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTV 608
Cdd:PTZ00295 573 RGAYIIVITD-DEDLVKDFADEIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
1-609 3.26e-156

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 463.97  E-value: 3.26e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAIAQ------RDVAEILLEGLRRLEYRGYDSAGLA-----------------------VVDAEGHMTRLRRlgK 51
Cdd:PTZ00394   1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAidanigsekedgtaasaptprpcVVRSVGNISQLRE--K 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   52 VQMLAQAAEEHPLHGGT----GIAHTRWATHGEPSEVNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDT 125
Cdd:PTZ00394  79 VFSEAVAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSNNgeFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  126 EVIAHLVNWELKQGG--TLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGL-------------------- 183
Cdd:PTZ00394 159 EVISVLSEYLYTRKGihNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdl 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  184 -GMGENFIASDQLALLPVTRRFIFLEEGDIAEI---TRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYE 259
Cdd:PTZ00394 239 sGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYcdgALRFYNAAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  260 QPNAIKNTLTGRI--SHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSA 337
Cdd:PTZ00394 319 QPESVISSMHGRIdfSSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  338 VRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLV 417
Cdd:PTZ00394 399 IQRDDVCFFVSQSGETADTLMALQLCKEAGAM-CVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVA 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  418 AKLSRLKGLDASIEHDIVHGLQALPSRIEQMLS-QDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAE 496
Cdd:PTZ00394 478 LLLSSDSVRLQERRNEIIRGLAELPAAISECLKiTHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTE 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  497 AYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIF 576
Cdd:PTZ00394 558 GIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQCVV 637
                        650       660       670
                 ....*....|....*....|....*....|...
gi 16131597  577 YTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PTZ00394 638 NVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
2-215 1.01e-127

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: 374.09  E-value: 1.01e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   2 CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEP 81
Cdd:cd00714   1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIG-DGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  82 SEVNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGT 159
Cdd:cd00714  80 TDVNAHPHRSCDgeIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131597 160 VIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEI 215
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
255-609 1.02e-74

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: 242.11  E-value: 1.02e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 255 KEIYEQPNAIKNTLtgriSHGQVDLSELgpnADELLSK-VEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEF-R 332
Cdd:COG2222   2 REIAQQPEAWRRAL----AALAAAIAAL---LARLRAKpPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 333 YRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTV 412
Cdd:COG2222  75 YPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGAR-TLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 413 LLMLVAKLSRLKGLDASiehdivhgLQALPSRIEQMLSQDKRIEALAEdFSDKHHALFLGRGDQYPIALEGALKLKEISY 492
Cdd:COG2222 154 LLALLAAWGGDDALLAA--------LDALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALKLKELSA 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 493 IHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVssdnmHIIEMPHVEEVI 572
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAI-----TLPAIPDLHDAL 299
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 16131597 573 APIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG2222 300 DPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
453-607 1.07e-69

SIS (Sugar ISomerase) domain repeat 2 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: 240142 [Multi-domain]  Cd Length: 153  Bit Score: 222.14  E-value: 1.07e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 453 KRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKS 532
Cdd:cd05009   1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131597 533 NIEEVRARGGQLYVFADQDAGFVSSDnmHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVT 607
Cdd:cd05009  81 LIKEVKARGAKVIVITDDGDAKDLAD--VVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
2-213 8.75e-65

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: 211.92  E-value: 8.75e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   2 CGIVGAIAQRDVAEILLE----GLRRLEYRGYDSAGLAVVDAEGHMTRlRRLGKVQMLAQAAEEHPLHGGTGIAHTRWAT 77
Cdd:cd00352   1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVE-KRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  78 HGEPSEVNAHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVnWELKQGGTLREAVLRAIPQLRG 155
Cdd:cd00352  80 NGLPSEANAQPFRSEdgRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLL-ERLGREGGLFEAVEDALKRLDG 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131597 156 AYGTVIMDsRHPDTLLAARSG---SPLVIGLGM-GENFIASDQLALLPVT-RRFIFLEEGDIA 213
Cdd:cd00352 159 PFAFALWD-GKPDRLFAARDRfgiRPLYYGITKdGGLVFASEPKALLALPfKGVRRLPPGELL 220
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
295-421 2.95e-58

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: 191.17  E-value: 2.95e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 295 HIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAI 374
Cdd:cd05008   1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 16131597 375 CNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLS 421
Cdd:cd05008  80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
1-182 5.41e-38

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: 146.32  E-value: 5.41e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVqmlAQA-AEEH--PLHGGTGIAHTRWAT 77
Cdd:COG0034   7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSD-GGRFHLHKGMGLV---SDVfDEEDleRLKGNIAIGHVRYST 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  78 HGEPSEVNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKqGGTLREAVLRAIPQL 153
Cdd:COG0034  83 TGSSSLENAQPFYVNSpfgsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELT-KEDLEEAIKEALRRV 161
                       170       180       190
                ....*....|....*....|....*....|..
gi 16131597 154 RGAYGTVIMDsrhPDTLLAAR--SG-SPLVIG 182
Cdd:COG0034 162 KGAYSLVILT---GDGLIAARdpNGiRPLVLG 190
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
2-226 4.27e-37

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: 138.36  E-value: 4.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   2 CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGkvqMLAQAAEEH---PLHGGTGIAHTRWATH 78
Cdd:cd00715   1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSD-GKRFHTHKGMG---LVSDVFDEEklrRLPGNIAIGHVRYSTA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  79 GEPSEVNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQgGTLREAVLRAIPQLR 154
Cdd:cd00715  77 GSSSLENAQPFVVNSplggIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK-DDLFEAIIDALERVK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 155 GAYGTVIMdsrHPDTLLAAR--SG-SPLVIG-LGMGENFIASDQLALLPVTRRFIF-LEEGDIAEITR---RSVNIFDKT 226
Cdd:cd00715 156 GAYSLVIM---TADGLIAVRdpHGiRPLVLGkLEGDGYVVASESCALDIIGAEFVRdVEPGEIVVIDDdglESSQRAPKP 232
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
289-419 1.73e-34

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: 127.03  E-value: 1.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   289 LLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYR-KSAVRRNSLMITLSQSGETADTLAGLRLSKELG 367
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16131597   368 yLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:pfam01380  81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
2-197 3.28e-33

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: 132.44  E-value: 3.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597     2 CGIVGAIAQR-DVAEILLEGLRRLEYRGYDSAGLAVVDaeGHMTRLRR-LGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:TIGR01134   1 CGVVGIYGQEeVAASLTYYGLYALQHRGQESAGISVFD--GNRFRLHKgNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    80 EPSEVNAHPHVSE----HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRG 155
Cdd:TIGR01134  79 SSGLENAQPFVVNspygGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 16131597   156 AYGTVIMdsrHPDTLLAARS--G-SPLVIGlGMGENF-IASDQLAL 197
Cdd:TIGR01134 159 AYALVLM---TEDGLVAVRDphGiRPLVLG-RRGDGYvVASESCAL 200
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
462-592 5.03e-31

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: 117.40  E-value: 5.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   462 FSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKsNIEEVRARG 541
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16131597   542 GQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIK 592
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
2-226 5.74e-27

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 114.36  E-value: 5.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    2 CGIVGAIA--QRDVAEILLEGLRRLEYRGYDSAGLAVVDAEgHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:PRK05793  15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAVSDGE-KIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   80 EPSEVNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGgtLREAVLRAIPQLRG 155
Cdd:PRK05793  94 ASDLDNAQPLVANYklgsIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKG--LEKALVDAIQAIKG 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131597  156 AYGTVIMDSrhpDTLLAARSGS---PLVIGLGMGENFIASDQLALLPVTRRFIF-LEEGDIAEITR---RSVNIFDKT 226
Cdd:PRK05793 172 SYALVILTE---DKLIGVRDPHgirPLCLGKLGDDYILSSESCALDTIGAEFIRdVEPGEIVIIDEdgiKSIKFAEKT 246
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
2-197 8.37e-25

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: 103.50  E-value: 8.37e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   2 CGIVGAI---AQRDVAEILLEGLRRLEYRG-YDSAGLAVVDAEG--------HMTRLRRLGKVQMLAQAAEEHPLHGGTG 69
Cdd:cd01907   1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgkDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  70 IAHTRWATHgepSEVN---AHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAV 146
Cdd:cd01907  81 IAHTRQPTN---SAVWwygAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYY 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131597 147 LRAI----------PQLRGAYGTVIMDSrhPDTLLAARSGS-----------PLVIGLGMGENFIASDQLAL 197
Cdd:cd01907 158 KHIIrmpeeerellLALRLTYRLADLDG--PFTIIVGTPDGfivirdriklrPAVVAETDDYVAIASEECAI 227
PLN02440 PLN02440
amidophosphoribosyltransferase
1-200 1.92e-22

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 100.91  E-value: 1.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGlaVVDAEGHMTRLRR-LGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:PLN02440   1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAG--IVTVDGNRLQSITgNGLVSDVFDESKLDQLPGDIAIGHVRYSTAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   80 EPSEVNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQggTLREAVLRAIPQLRG 155
Cdd:PLN02440  79 ASSLKNVQPFVANYrfgsIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKAR--PFFSRIVDACEKLKG 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16131597  156 AYGTVIMDSrhpDTLLAARSGS---PLVIGL-GMGENFIASDQLALLPV 200
Cdd:PLN02440 157 AYSMVFLTE---DKLVAVRDPHgfrPLVMGRrSNGAVVFASETCALDLI 202
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
65-174 6.26e-20

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: 85.82  E-value: 6.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    65 HGGTGIAHTRWATHGEPSEVNaHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvnwelkqggtL 142
Cdd:pfam13522   9 EGGVALGHVRLAIVDLPDAGN-QPMLSRdgRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL----------Y 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 16131597   143 REAVLRAIPQLRGAYGTVIMDSRhPDTLLAAR 174
Cdd:pfam13522  78 EEWGEDCLERLRGMFAFAIWDRR-RRTLFLAR 108
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
94-199 9.22e-17

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: 76.79  E-value: 9.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    94 IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNwelKQGGTlrEAVLRaipqLRGAYGTVIMDSRHpDTLLAA 173
Cdd:pfam13537  24 YVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE---AEWGE--DCVDR----LNGMFAFAIWDRRR-QRLFLA 93
                          90       100       110
                  ....*....|....*....|....*....|
gi 16131597   174 R--SG-SPLVIGLGMGENFI-ASDQLALLP 199
Cdd:pfam13537  94 RdrFGiKPLYYGRDDGGRLLfASELKALLA 123
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
2-200 1.03e-15

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: 76.44  E-value: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   2 CGIVGAI---AQRDVAEILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWATH 78
Cdd:cd00712   1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWI----------------------------DEGVALGHRRLSII 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  79 GEPSEvnAHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvnweLKQGGTlreavlRAIPQLRGA 156
Cdd:cd00712  53 DLSGG--AQPMVSEdgRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL----YEEWGE------DCLERLNGM 120
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 16131597 157 YGTVIMDSRhPDTLLAAR--SGS-PLVIGLGmGENFI-ASDQLALLPV 200
Cdd:cd00712 121 FAFALWDKR-KRRLFLARdrFGIkPLYYGRD-GGGLAfASELKALLAL 166
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
1-174 1.37e-15

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: 79.88  E-value: 1.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   1 MCGIVGAIAQRDVA--EILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWATH 78
Cdd:COG0367   1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIWV----------------------------DGGVALGHRRLSII 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  79 GEPSevNAH-PHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvnWElkQGGTlreavlRAIPQLRG 155
Cdd:COG0367  53 DLSE--GGHqPMVSEdgRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA--YE--EWGE------DCLERLNG 120
                       170
                ....*....|....*....
gi 16131597 156 AYGTVIMDSRHpDTLLAAR 174
Cdd:COG0367 121 MFAFAIWDRRE-RRLFLAR 138
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
62-177 2.37e-13

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 69.99  E-value: 2.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  62 HPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKAR-----GYTFVSETDTEVIAHLVNWEL 136
Cdd:COG0121  72 RPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELAFALLLSRL 151
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16131597 137 KQGG-TLREAVLRAIPQLR------GAYGTVIMDsrhPDTLLAARSGS 177
Cdd:COG0121 152 RDGGpDPAEALAEALRELAelarapGRLNLLLSD---GERLYATRYTS 196
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
1-197 9.79e-13

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 70.90  E-value: 9.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAIAQRDVAEIL----LEGLRRLEYRGYDSAGLAVVDAEGHMTRLrrlgkvqmlaqaaeehplhggtgIAHTRWA 76
Cdd:PTZ00077   1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERLA 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   77 -----THGEPSEVNAHPhvsehIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvnweLKQGGTlreavlRAIP 151
Cdd:PTZ00077  58 ivdlsDGKQPLLDDDET-----VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL----YKEYGP------KDFW 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16131597  152 -QLRGAYGTVIMDSRHpDTLLAARSG---SPLVIGLGM-GENFIASDQLAL 197
Cdd:PTZ00077 123 nHLDGMFATVIYDMKT-NTFFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
62-178 1.30e-12

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: 68.18  E-value: 1.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  62 HPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREEL-KARGYTFVSETDTEVIAHLVnweLKQGG 140
Cdd:cd01908  76 RPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLlRLLPRLPVGTTDSELAFALL---LSRLL 152
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 16131597 141 T--------LREAVLRAIPQLR-----GAYGTVIMDSrhpDTLLAARSGSP 178
Cdd:cd01908 153 ErdpldpaeLLDAILQTLRELAalappGRLNLLLSDG---EYLIATRYASA 200
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
1-197 1.76e-12

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 70.18  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAIAQRDVA----EILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWA 76
Cdd:PLN02549   1 MCGILAVLGCSDDSqakrSRVLELSRRLRHRGPDWSGLYG----------------------------NEDCYLAHERLA 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   77 THGEPSevNAHPHVSEH--IVVVHNGIIENHEPLREELKArgYTFVSETDTEVIAHLvnWELKQGGTLREavlraipqLR 154
Cdd:PLN02549  53 IMDPES--GDQPLYNEDktIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHL--YEEHGEEFVDM--------LD 118
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 16131597  155 GAYGTVIMDSRHpDTLLAARSG---SPLVIGLGM-GENFIASDQLAL 197
Cdd:PLN02549 119 GMFSFVLLDTRD-NSFIAARDHigiTPLYIGWGLdGSVWFASEMKAL 164
asnB PRK09431
asparagine synthetase B; Provisional
1-202 7.85e-12

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 68.01  E-value: 7.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    1 MCGIVGAIAQRDVAEIL----LEGLRRLEYRGYDSAGLAVVDAeghmtrlrrlgkvqmlaqaaeehplhggtGI-AHTRW 75
Cdd:PRK09431   1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYASDN-----------------------------AIlGHERL 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597   76 A----THGepsevnAHPHVSEH--IVVVHNGIIENHEPLREELKARgYTFVSETDTEVIAHLvnwelkqggtLREAVLRA 149
Cdd:PRK09431  52 SivdvNGG------AQPLYNEDgtHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL----------YQEKGPDF 114
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131597  150 IPQLRGAYGTVIMDSRHpDTLLAARsgSPL-VIGLGMGEN-----FIASDQLALLPVTR 202
Cdd:PRK09431 115 LDDLDGMFAFALYDSEK-DAYLIAR--DPIgIIPLYYGYDehgnlYFASEMKALVPVCK 170
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
296-375 5.29e-11

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: 58.92  E-value: 5.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 296 IQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRY--RKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLA 373
Cdd:cd04795   1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELG-IPVIA 79

                ..
gi 16131597 374 IC 375
Cdd:cd04795  80 IT 81
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
295-420 1.48e-10

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: 58.74  E-value: 1.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 295 HIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRK-SAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLA 373
Cdd:cd05710   1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGpKRLTEKSVVILASHSGNTKETVAAAKFAKEKGAT-VIG 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 16131597 374 ICNVPGSSLVRESDLALMTNAGteigvasTKAFTTQLTVLLMLVAKL 420
Cdd:cd05710  80 LTDDEDSPLAKLADYVIVYGFE-------IDAVEEKYLLLYMLALRL 119
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
95-174 1.59e-09

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: 60.43  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    95 VVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVnweLKQGGtlreavlRAIPQLRGAYGTVIMDSRHpDTLLAAR 174
Cdd:TIGR01536  69 VIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY---EEWGE-------ECVDRLDGMFAFALWDSEK-GELFLAR 137
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
469-549 1.45e-08

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: 51.99  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 469 LFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGP-LALIDADMPVIVVAPNNElLEKLKSNIEEVRARGGQLYVF 547
Cdd:cd04795   2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80

                ..
gi 16131597 548 AD 549
Cdd:cd04795  81 TD 82
frlB PRK11382
fructoselysine 6-phosphate deglycase;
287-600 9.44e-08

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 54.24  E-value: 9.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  287 DELLSK-VEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEF----RYRKSAvrrNSLMITLSQSGETADTLAGLR 361
Cdd:PRK11382  37 EEMVKRdIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFcdntPYRLDD---RCAVIGVSDYGKTEEVIKALE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  362 LSKELGYLgSLAICNVPGSSLVRESDLALMTNAGT--EIGVASTKAFTTQLTVLLMLVAKLSRLKgldasiehdivHGLQ 439
Cdd:PRK11382 114 LGRACGAL-TAAFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNAEIGKIK-----------NDLK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  440 ALPSRIEQML-SQDKRIEALAEDFSDKHHALFLGRGDQYPIAL-EGALKLKEISYIHAEAYAAGELKHGPLALIDADMPV 517
Cdd:PRK11382 182 QLPNALGHLVrTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPF 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  518 IVVAPNNELLEKLKSNIEEVRARggqlyvfadqdagfvsSDNMHIIEMPHVEE----VIAPIFYTVPLQLLAYHVALIKG 593
Cdd:PRK11382 262 LFLLGNDESRHTTERAINFVKQR----------------TDNVIVIDYAEISQglhpWLAPFLMFVPMEWLCYYLSIYKD 325

                 ....*..
gi 16131597  594 TDVDQPR 600
Cdd:PRK11382 326 HNPDERR 332
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
288-419 3.78e-07

RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.


Pssm-ID: 240144 [Multi-domain]  Cd Length: 139  Bit Score: 49.53  E-value: 3.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 288 ELLSKVEHIQILACGTSYNSGM-VSRYWFesLAGIPCDVEIAS-EFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKE 365
Cdd:cd05013   8 DLLAKARRIYIFGVGSSGLVAEyLAYKLL--RLGKPVVLLSDPhLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKE 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16131597 366 LGyLGSLAICNVPGSSLVRESDLALMTNA-GTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:cd05013  86 RG-AKVIAITDSANSPLAKLADIVLLVSSeEGDFRSSAFSSRIAQLALIDALFLA 139
GATase_4 pfam13230
Glutamine amidotransferases class-II; This family captures members that are not found in ...
55-166 1.32e-05

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


Pssm-ID: 433047 [Multi-domain]  Cd Length: 272  Bit Score: 47.32  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597    55 LAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSE----HIVVVHNGIIENHEPLREELkargYTFVSETDTEVI-A 129
Cdd:pfam13230  60 IAELVRRYPIRSRNVIAHIRKATQGRVTLENTHPFMRElwgrYWIFAHNGDLKGYAPKLSGR----FQPVGSTDSELAfC 135
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 16131597   130 HLVNWELKQGGTLRE------AVLRAIPQLRGAYGT---VIMDSRH 166
Cdd:pfam13230 136 WLLDRLASRFPYARPsagelfRALRELAREIAAHGTfnfLLSDGRD 181
SIS_AgaS_like cd05010
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ...
470-599 1.56e-04

AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli. It is similar to the glucosamine-6-phosphate synthases (GlmS) which catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source.


Pssm-ID: 240143 [Multi-domain]  Cd Length: 151  Bit Score: 42.23  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 470 FLGRGDQYPIALEGALKLKEIS--YIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSN-IEEVRARGGQLYV 546
Cdd:cd05010   3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDlLKELRRDGIAARV 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131597 547 FA---DQDAGFVSSDNMHIIEMPHVEEV-IAPIfYTVPLQLLAYHVALIKGTDVDQP 599
Cdd:cd05010  83 IAispESDAGIEDNSHYYLPGSRDLDDVyLAFP-YILYAQLFALFNSIALGLTPDNP 138
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
324-416 1.30e-03

N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.


Pssm-ID: 240140 [Multi-domain]  Cd Length: 257  Bit Score: 40.97  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597 324 DVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVAST 403
Cdd:cd05007 102 DDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGAL-TIGIACNPGSPLLQLADIAIALITGPEVVAGST 180
                        90
                ....*....|....*
gi 16131597 404 --KAFTTQLTVLLML 416
Cdd:cd05007 181 rlKAGTAQKLALNML 195
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
338-416 5.10e-03

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 39.38  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131597  338 VRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVAST--KAFTTQLTVLLM 415
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGAL-TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNM 207

                 .
gi 16131597  416 L 416
Cdd:PRK05441 208 I 208
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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