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Conserved domains on  [gi|75273435|sp|Q9LIP9|]
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RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1; Short=AtGFAT; Short=AtGFAT1; Short=Glutamine:fructose-6-phosphate amidotransferase 1; AltName: Full=D-fructose-6-phosphate amidotransferase GFAT1; AltName: Full=Hexosephosphate aminotransferase GFAT1

Protein Classification

glutamine--fructose-6-phosphate aminotransferase( domain architecture ID 11477341)

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

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List of domain hits

Name Accession Description Interval E-value
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
1-677 0e+00

glucosamine:fructose-6-phosphate aminotransferase


:

Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 1443.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    1 MCGIFAYLNFHANKERRYILDVLFNGLRRLEYRGYDSAGIAIDN--SSPSSSPLVFRQAGNIESLVNSVNEEITNTDLNL 78
Cdd:PLN02981   1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNdpSLESSSPLVFREEGKIESLVRSVYEEVAETDLNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   79 DEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFD 158
Cdd:PLN02981  81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  159 KANEEGGqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKELDQGESNSHVFQDAHFLSKN-DHPK 237
Cdd:PLN02981 161 KLNEEEG-DVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELPEEKNSSAVFTSEGFLTKNrDKPK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  238 EFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERGRCNG-LSRPASVERALSVLEMEVEQISKGKYDHYMQ 316
Cdd:PLN02981 240 EFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGgLSRPASVERALSTLEMEVEQIMKGNYDHYMQ 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  317 KEIHEQPESLTTTMRGRLIRGGSRKTKTVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIAS 396
Cdd:PLN02981 320 KEIHEQPESLTTTMRGRLIRGGSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELAS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  397 DLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQI 476
Cdd:PLN02981 400 DLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQI 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  477 VVMVMLALAIGSDTISSQKRREAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEV 556
Cdd:PLN02981 480 VAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEV 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  557 ALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSSSGSCRAIEVPQV 636
Cdd:PLN02981 560 ALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCPSGGCRVIEVPQV 639
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 75273435  637 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 677
Cdd:PLN02981 640 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
 
Name Accession Description Interval E-value
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
1-677 0e+00

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 1443.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    1 MCGIFAYLNFHANKERRYILDVLFNGLRRLEYRGYDSAGIAIDN--SSPSSSPLVFRQAGNIESLVNSVNEEITNTDLNL 78
Cdd:PLN02981   1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNdpSLESSSPLVFREEGKIESLVRSVYEEVAETDLNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   79 DEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFD 158
Cdd:PLN02981  81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  159 KANEEGGqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKELDQGESNSHVFQDAHFLSKN-DHPK 237
Cdd:PLN02981 161 KLNEEEG-DVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELPEEKNSSAVFTSEGFLTKNrDKPK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  238 EFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERGRCNG-LSRPASVERALSVLEMEVEQISKGKYDHYMQ 316
Cdd:PLN02981 240 EFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGgLSRPASVERALSTLEMEVEQIMKGNYDHYMQ 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  317 KEIHEQPESLTTTMRGRLIRGGSRKTKTVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIAS 396
Cdd:PLN02981 320 KEIHEQPESLTTTMRGRLIRGGSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELAS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  397 DLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQI 476
Cdd:PLN02981 400 DLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQI 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  477 VVMVMLALAIGSDTISSQKRREAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEV 556
Cdd:PLN02981 480 VAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEV 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  557 ALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSSSGSCRAIEVPQV 636
Cdd:PLN02981 560 ALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCPSGGCRVIEVPQV 639
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 75273435  637 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 677
Cdd:PLN02981 640 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
1-675 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: 735.67  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   1 MCGIFAYLnfhANKErryILDVLFNGLRRLEYRGYDSAGIAIDNSSpssSPLVFRQAGNIESLVNSVNEEITNTdlnlde 80
Cdd:COG0449   1 MCGIVGYI---GKRD---AAPILLEGLKRLEYRGYDSAGIAVLDDG---GLEVRKAVGKLANLEEKLAEEPLSG------ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  81 vfyfHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLakfvFDKA 160
Cdd:COG0449  66 ----TIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHL----IEEY 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 161 NEEGGqtvTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVkeldqGEsnshvfqdahflskndhpKEFF 240
Cdd:COG0449 137 LKGGG---DLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL-----GE------------------GENF 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 241 LSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERgrcnglsrpasVERALSVLEMEVEQISKGKYDHYMQKEIH 320
Cdd:COG0449 191 LASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEP-----------VEREVKTVDWDAEAAEKGGYPHFMLKEIH 259
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 321 EQPESLTTTMRGRLIRGGsrktkTVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWD 400
Cdd:COG0449 260 EQPEAIRDTLRGRLDEDG-----RVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRY 334
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 401 RQgPIYREDT-AVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVM 479
Cdd:COG0449 335 RD-PVVDPGTlVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAAL 413
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 480 VMLALAIGSD--TISSQKRREaIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVA 557
Cdd:COG0449 414 YLLALYLARArgTLSAEEEAE-LLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEIS 492
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 558 LMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAAsvSSSGSCRAIEVPQVE 637
Cdd:COG0449 493 YIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEE--VEELADDVIEVPEVD 570
                       650       660       670
                ....*....|....*....|....*....|....*...
gi 75273435 638 DCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:COG0449 571 ELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVT 608
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
2-675 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: 618.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435     2 CGIFAYLNfhankeRRYILDVLFNGLRRLEYRGYDSAGIA-IDNSSPSssplVFRQAGNIESLVNSVNEEitntdlnldE 80
Cdd:TIGR01135   1 CGIVGYIG------QRDAVPILLEGLKRLEYRGYDSAGIAvVDEGKLF----VRKAVGKVAELANKLGEK---------P 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    81 VFYFhAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvfdka 160
Cdd:TIGR01135  62 LPGG-VGIGHTRWATHGKPTDENAHPHTDEGGR-IAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLI------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   161 NEEGGQTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpKEFF 240
Cdd:TIGR01135 133 EEELREGGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGLGD-----------------------GENF 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   241 LSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERgrcnglsrpasVERALSVLEMEVEQISKGKYDHYMQKEIH 320
Cdd:TIGR01135 190 VASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAP-----------VQREVRVIDWDLDAAEKGGYRHFMLKEIY 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   321 EQPESLTTTMRGRLIRGGsrktKTVLLGGLKDHLKTIRRsrrIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWD 400
Cdd:TIGR01135 259 EQPRALRDTLEGRIEENG----GVFEELGAEELLKNIDR---IQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRY 331
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   401 RQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMV 480
Cdd:TIGR01135 332 RKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLY 411
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   481 MLALAIGSDT-ISSQKRREAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVALM 559
Cdd:TIGR01135 412 LLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYI 491
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   560 HSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSSSGScrAIEVPQVEDC 639
Cdd:TIGR01135 492 HAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADD--VIKLPEVEEL 569
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 75273435   640 LQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:TIGR01135 570 LAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVT 605
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
2-264 5.04e-101

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: 307.84  E-value: 5.04e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   2 CGIFAYLNFhankerRYILDVLFNGLRRLEYRGYDSAGIAIDNSSpssSPLVFRQAGNIESLVNSVNEEITNtdlnldev 81
Cdd:cd00714   1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---SLEVVKAVGKVANLEEKLAEKPLS-------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  82 fyFHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFDKan 161
Cdd:cd00714  64 --GHVGIGHTRWATHGEPTDVNAHPHRSCDGE-IAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDG-- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 162 eeggqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpKEFFL 241
Cdd:cd00714 139 -----GLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGD-----------------------GENFV 190
                       250       260
                ....*....|....*....|...
gi 75273435 242 SSDPHALVEHTKKVLVIEDGEVV 264
Cdd:cd00714 191 ASDAPALLEHTRRVIYLEDGDIA 213
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
357-485 1.06e-37

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: 136.66  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   357 IRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQ-GPIYREDTAVFVSQSGETADTLLALDYARENGA 435
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 75273435   436 LCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMVMLALA 485
Cdd:pfam01380  82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
 
Name Accession Description Interval E-value
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
1-677 0e+00

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 1443.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    1 MCGIFAYLNFHANKERRYILDVLFNGLRRLEYRGYDSAGIAIDN--SSPSSSPLVFRQAGNIESLVNSVNEEITNTDLNL 78
Cdd:PLN02981   1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNdpSLESSSPLVFREEGKIESLVRSVYEEVAETDLNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   79 DEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFD 158
Cdd:PLN02981  81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  159 KANEEGGqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKELDQGESNSHVFQDAHFLSKN-DHPK 237
Cdd:PLN02981 161 KLNEEEG-DVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELPEEKNSSAVFTSEGFLTKNrDKPK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  238 EFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERGRCNG-LSRPASVERALSVLEMEVEQISKGKYDHYMQ 316
Cdd:PLN02981 240 EFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGgLSRPASVERALSTLEMEVEQIMKGNYDHYMQ 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  317 KEIHEQPESLTTTMRGRLIRGGSRKTKTVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIAS 396
Cdd:PLN02981 320 KEIHEQPESLTTTMRGRLIRGGSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELAS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  397 DLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQI 476
Cdd:PLN02981 400 DLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQI 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  477 VVMVMLALAIGSDTISSQKRREAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEV 556
Cdd:PLN02981 480 VAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEV 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  557 ALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSSSGSCRAIEVPQV 636
Cdd:PLN02981 560 ALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCPSGGCRVIEVPQV 639
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 75273435  637 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 677
Cdd:PLN02981 640 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
1-675 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: 735.67  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   1 MCGIFAYLnfhANKErryILDVLFNGLRRLEYRGYDSAGIAIDNSSpssSPLVFRQAGNIESLVNSVNEEITNTdlnlde 80
Cdd:COG0449   1 MCGIVGYI---GKRD---AAPILLEGLKRLEYRGYDSAGIAVLDDG---GLEVRKAVGKLANLEEKLAEEPLSG------ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  81 vfyfHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLakfvFDKA 160
Cdd:COG0449  66 ----TIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHL----IEEY 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 161 NEEGGqtvTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVkeldqGEsnshvfqdahflskndhpKEFF 240
Cdd:COG0449 137 LKGGG---DLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL-----GE------------------GENF 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 241 LSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERgrcnglsrpasVERALSVLEMEVEQISKGKYDHYMQKEIH 320
Cdd:COG0449 191 LASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEP-----------VEREVKTVDWDAEAAEKGGYPHFMLKEIH 259
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 321 EQPESLTTTMRGRLIRGGsrktkTVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWD 400
Cdd:COG0449 260 EQPEAIRDTLRGRLDEDG-----RVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRY 334
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 401 RQgPIYREDT-AVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVM 479
Cdd:COG0449 335 RD-PVVDPGTlVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAAL 413
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 480 VMLALAIGSD--TISSQKRREaIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVA 557
Cdd:COG0449 414 YLLALYLARArgTLSAEEEAE-LLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEIS 492
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 558 LMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAAsvSSSGSCRAIEVPQVE 637
Cdd:COG0449 493 YIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEE--VEELADDVIEVPEVD 570
                       650       660       670
                ....*....|....*....|....*....|....*...
gi 75273435 638 DCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:COG0449 571 ELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVT 608
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
1-677 0e+00

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 698.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    1 MCGIFAYLNFHANKERRYILDVLFNGLRRLEYRGYDSAGIAIDN------------SSPSSSPLVFRQAGNIESLVNSV- 67
Cdd:PTZ00394   1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDAnigsekedgtaaSAPTPRPCVVRSVGNISQLREKVf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   68 NEEITNTDLNLDEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTE 147
Cdd:PTZ00394  81 SEAVAATLPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGE-FTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  148 VIPKLAKFVFDKANeeggqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKeldQGESNSHVFQ-D 226
Cdd:PTZ00394 160 VISVLSEYLYTRKG-----IHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR---RTDDRGCVMKlQ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  227 AHFLSKNDHPKEFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGvsiLKFENERGRCNGLsrpasVERALSVLEMEVEQI 306
Cdd:PTZ00394 232 TYDLTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGA---LRFYNAAERQRSI-----VKREVQHLDAKPEGL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  307 SKGKYDHYMQKEIHEQPESLTTTMRGRLirggSRKTKTVLLGGLKDH-LKTIRRSRRIVFIGCGTSYNAALASRPILEEL 385
Cdd:PTZ00394 304 SKGNYPHFMLKEIYEQPESVISSMHGRI----DFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPLFEEL 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  386 SGIPVSMEIASDLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIG 465
Cdd:PTZ00394 380 VPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVG 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  466 VASTKAYTSQIVVMVMLALAIGSDTISSQKRREAIIDGLLDLPYKVKEVLKL-DDEMKDLAQLLIDEQSLLVFGRGYNYA 544
Cdd:PTZ00394 460 VASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYDLA 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  545 TALEGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSS 624
Cdd:PTZ00394 540 TAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAA 619
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|...
gi 75273435  625 SGSCraIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 677
Cdd:PTZ00394 620 ASEI--VLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
1-675 0e+00

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 687.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    1 MCGIFAYLnfhANKErryILDVLFNGLRRLEYRGYDSAGIA-IDNSSPSssplVFRQAGNIESLVNSVNEEITNTdlnld 79
Cdd:PRK00331   1 MCGIVGYV---GQRN---AAEILLEGLKRLEYRGYDSAGIAvLDDGGLE----VRKAVGKVANLEAKLEEEPLPG----- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   80 evfyfHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLakfvFDK 159
Cdd:PRK00331  66 -----TTGIGHTRWATHGKPTERNAHPHTDCSGR-IAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHL----IEE 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  160 ANEEGGQTVtfcEVVFEVMRHLEGAYAL--IFKSwhYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpK 237
Cdd:PRK00331 136 ELKEGGDLL---EAVRKALKRLEGAYALavIDKD--EPDTIVAARNGSPLVIGLGE-----------------------G 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  238 EFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERgrcnglsrpasVERALSVLEMEVEQISKGKYDHYMQK 317
Cdd:PRK00331 188 ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNP-----------VEREVYTVDWDASAAEKGGYRHFMLK 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  318 EIHEQPESLTTTMRGRLIrggsrktktvLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASD 397
Cdd:PRK00331 257 EIYEQPEAIRDTLEGRLD----------ELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASE 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  398 LWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIV 477
Cdd:PRK00331 327 FRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLA 406
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  478 VMVMLALAIGSD--TISSQKRREaIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKE 555
Cdd:PRK00331 407 VLYLLALALAKArgTLSAEEEAD-LVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLKE 485
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  556 VALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAAsvsSSGSCRAIEVPQ 635
Cdd:PRK00331 486 ISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEV---AEEADDVIEVPE 562
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|
gi 75273435  636 VEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:PRK00331 563 VHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVT 602
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
2-675 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: 618.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435     2 CGIFAYLNfhankeRRYILDVLFNGLRRLEYRGYDSAGIA-IDNSSPSssplVFRQAGNIESLVNSVNEEitntdlnldE 80
Cdd:TIGR01135   1 CGIVGYIG------QRDAVPILLEGLKRLEYRGYDSAGIAvVDEGKLF----VRKAVGKVAELANKLGEK---------P 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    81 VFYFhAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvfdka 160
Cdd:TIGR01135  62 LPGG-VGIGHTRWATHGKPTDENAHPHTDEGGR-IAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLI------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   161 NEEGGQTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpKEFF 240
Cdd:TIGR01135 133 EEELREGGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGLGD-----------------------GENF 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   241 LSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERgrcnglsrpasVERALSVLEMEVEQISKGKYDHYMQKEIH 320
Cdd:TIGR01135 190 VASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAP-----------VQREVRVIDWDLDAAEKGGYRHFMLKEIY 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   321 EQPESLTTTMRGRLIRGGsrktKTVLLGGLKDHLKTIRRsrrIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWD 400
Cdd:TIGR01135 259 EQPRALRDTLEGRIEENG----GVFEELGAEELLKNIDR---IQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRY 331
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   401 RQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMV 480
Cdd:TIGR01135 332 RKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLY 411
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   481 MLALAIGSDT-ISSQKRREAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVALM 559
Cdd:TIGR01135 412 LLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYI 491
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   560 HSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSSSGScrAIEVPQVEDC 639
Cdd:TIGR01135 492 HAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADD--VIKLPEVEEL 569
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 75273435   640 LQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:TIGR01135 570 LAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVT 605
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
1-676 3.01e-157

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 467.96  E-value: 3.01e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    1 MCGIFAYLnfhANKERRyilDVLFNGLRRLEYRGYDSAGIAIDNSSPSsspLVFRQAGNIESLVNSVN---EEITNTDLN 77
Cdd:PTZ00295  24 CCGIVGYL---GNEDAS---KILLEGIEILQNRGYDSCGISTISSGGE---LKTTKYASDGTTSDSIEilkEKLLDSHKN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   78 ldevfyFHAGIAHTRWATHGEPAPRNSHPQSSgPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVF 157
Cdd:PTZ00295  95 ------STIGIAHTRWATHGGKTDENAHPHCD-YKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLEL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  158 DkaneeggQTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpK 237
Cdd:PTZ00295 168 D-------QGEDFQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGD-----------------------D 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  238 EFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENErgrcnglsrpasVERalsvLEMEVEQISKGKYDHYMQK 317
Cdd:PTZ00295 218 SIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRR------------VEK----IPEEVIEKSPEPYPHWTLK 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  318 EIHEQPESLTTTM--RGRLIRGGSRktktVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGI-PVSMEI 394
Cdd:PTZ00295 282 EIFEQPIALSRALnnGGRLSGYNNR----VKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVID 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  395 ASDLwDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTS 474
Cdd:PTZ00295 358 ASEL-TLYRLPDEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTS 436
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  475 QIVVMVMLALAIGS--DTISSQKRREAIIDGLLDLPYKVKEVLKL-DDEMKDLAQLLIDEQSLLVFGRGYNYATALEGAL 551
Cdd:PTZ00295 437 QVTVLSLIALWFAQnkEYSCSNYKCSSLINSLHRLPTYIGMTLKScEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGAL 516
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  552 KVKEVALMHSEGILAGEMKHGPLALVDE--NLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCskgDAASVSSSGSCR 629
Cdd:PTZ00295 517 KIKEITYIHAEGFSGGALKHGPFALIDKekNTPVILIILDDEHKELMINAAEQVKARGAYIIVIT---DDEDLVKDFADE 593
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*..
gi 75273435  630 AIEVPQVeDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTT 676
Cdd:PTZ00295 594 IILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
2-264 5.04e-101

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: 307.84  E-value: 5.04e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   2 CGIFAYLNFhankerRYILDVLFNGLRRLEYRGYDSAGIAIDNSSpssSPLVFRQAGNIESLVNSVNEEITNtdlnldev 81
Cdd:cd00714   1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---SLEVVKAVGKVANLEEKLAEKPLS-------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  82 fyFHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFDKan 161
Cdd:cd00714  64 --GHVGIGHTRWATHGEPTDVNAHPHRSCDGE-IAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDG-- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 162 eeggqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpKEFFL 241
Cdd:cd00714 139 -----GLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGD-----------------------GENFV 190
                       250       260
                ....*....|....*....|...
gi 75273435 242 SSDPHALVEHTKKVLVIEDGEVV 264
Cdd:cd00714 191 ASDAPALLEHTRRVIYLEDGDIA 213
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
317-676 3.70e-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: 3.70e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 317 KEIHEQPESLtttmrgrlirggsRKTKTVLLGGLKDHLKTIRRS--RRIVFIGCGTSYNAALASRPILEELSGIPVSMEI 394
Cdd:COG2222   2 REIAQQPEAW-------------RRALAALAAAIAALLARLRAKppRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 395 ASDLWDRQGPIYREDTAVF-VSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYT 473
Cdd:COG2222  69 PSELVVYPAYLKLEGTLVVaISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 474 SQIVVMVMLALAIGSDtissqkrrEAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLiDEQSLLVFGRGYNYATALEGALKV 553
Cdd:COG2222 149 TMLLALLALLAAWGGD--------DALLAALDALPAALEAALAADWPAAALAALA-DAERVVFLGRGPLYGLAREAALKL 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 554 KEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAasvsssgscrAIEV 633
Cdd:COG2222 220 KELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDA----------AITL 289
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 75273435 634 PQVEDC---LQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTT 676
Cdd:COG2222 290 PAIPDLhdaLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKT 335
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
519-675 4.70e-64

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: 208.66  E-value: 4.70e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 519 DEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQS 598
Cdd:cd05009   1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75273435 599 VIQQLHARKGRLIVMCSKGDAasvsSSGSCRAIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:cd05009  81 LIKEVKARGAKVIVITDDGDA----KDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
362-487 1.45e-59

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: 195.79  E-value: 1.45e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 362 RIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGIT 441
Cdd:cd05008   1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 75273435 442 NTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMVMLALAIG 487
Cdd:cd05008  81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
2-264 6.93e-50

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: 173.40  E-value: 6.93e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   2 CGIFAYLNFHANKERRYILDvlFNGLRRLEYRGYDSAGIAIDNSSPSSSPLVFRQAGNIEslvnsvneeitntDLNLDEV 81
Cdd:cd00352   1 CGIFGIVGADGAASLLLLLL--LRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVA-------------LDLLDEP 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  82 FYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvfdkan 161
Cdd:cd00352  66 LKSGVALGHVRLATNGLPSEANAQPFRSEDGR-IALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLL-------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 162 EEGGQTVTFCEVVFEVMRHLEGAYALIFKSwHYPNELIAC--KLG-SPLLLGVkeldqgesnshvfqdahflsknDHPKE 238
Cdd:cd00352 137 ERLGREGGLFEAVEDALKRLDGPFAFALWD-GKPDRLFAArdRFGiRPLYYGI----------------------TKDGG 193
                       250       260
                ....*....|....*....|....*..
gi 75273435 239 FFLSSDPHALVEHT-KKVLVIEDGEVV 264
Cdd:cd00352 194 LVFASEPKALLALPfKGVRRLPPGELL 220
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
357-485 1.06e-37

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: 136.66  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   357 IRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQ-GPIYREDTAVFVSQSGETADTLLALDYARENGA 435
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 75273435   436 LCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMVMLALA 485
Cdd:pfam01380  82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
2-215 5.79e-21

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: 92.91  E-value: 5.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   2 CGIFA-YLNFHANKerryildVLFNGLRRLEYRGYDSAGIAIDNSSpsssplVFRQ-AGNieSLVNSV-NEEITNtdlNL 78
Cdd:cd00715   1 CGVFGiYGAEDAAR-------LTYLGLYALQHRGQESAGIATSDGK------RFHThKGM--GLVSDVfDEEKLR---RL 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  79 DEvfyfHAGIAHTRWATHGEPAPRNSHPQSSG-PGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvf 157
Cdd:cd00715  63 PG----NIAIGHVRYSTAGSSSLENAQPFVVNsPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLI---- 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75273435 158 dkANEEGGQTVTfcEVVFEVMRHLEGAYALIFKSwhyPNELIACK--LG-SPLLLGVKELD 215
Cdd:cd00715 135 --ARSLAKDDLF--EAIIDALERVKGAYSLVIMT---ADGLIAVRdpHGiRPLVLGKLEGD 188
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
527-660 9.54e-21

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: 88.51  E-value: 9.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   527 LLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQsVIQQLHAR 606
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 75273435   607 KGRLIVMCSKGDaaSVSSSGSCRAIEVPQVEDCLQPVINIVPLQLLAYHLTVLR 660
Cdd:pfam01380  80 GAKIIAITDSPG--SPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
1-213 1.34e-19

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


Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 92.39  E-value: 1.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   1 MCGIFA-YLNFHANKerryildVLFNGLRRLEYRGYDSAGIAidnSSPSSSPLVFRQAGniesLVNSV-NEEITNtdlNL 78
Cdd:COG0034   7 ECGVFGiYGHEDVAQ-------LTYYGLYALQHRGQESAGIA---TSDGGRFHLHKGMG----LVSDVfDEEDLE---RL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  79 DEvfyfHAGIAHTRWATHGEPAPRNSHP-QSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKL-AKFV 156
Cdd:COG0034  70 KG----NIAIGHVRYSTTGSSSLENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLiAREL 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 157 FDKaneeggqtvTFCEVVFEVMRHLEGAYALIFKSwhyPNELIACK--LG-SPLLLGVKE 213
Cdd:COG0034 146 TKE---------DLEEAIKEALRRVKGAYSLVILT---GDGLIAARdpNGiRPLVLGKLE 193
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
2-292 1.16e-16

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: 83.14  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435     2 CGIFAYLNfHANKERRYILDvlfnGLRRLEYRGYDSAGIAIDNSSpssSPLVFRQAGniesLVNSVNEEITNTDLNLdev 81
Cdd:TIGR01134   1 CGVVGIYG-QEEVAASLTYY----GLYALQHRGQESAGISVFDGN---RFRLHKGNG----LVSDVFNEEHLQRLKG--- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    82 fyfHAGIAHTRWATHGEPAPRNSHP--QSSGPGDDfLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFDk 159
Cdd:TIGR01134  66 ---NVGIGHVRYSTAGSSGLENAQPfvVNSPYGGL-ALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDE- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   160 aneeggQTVTFCEVVFEVMRHLEGAYALIFKSWHypnELIACK--LG-SPLLLGVKEldqgesnshvfqdahflskndhp 236
Cdd:TIGR01134 141 ------SKDDLFDAVARVLERVRGAYALVLMTED---GLVAVRdpHGiRPLVLGRRG----------------------- 188
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75273435   237 KEFFLSSDPHAL----VEHTKKVlviEDGEVVNLKDGGVSILKFENE-RGRCN----GLSRPASV 292
Cdd:TIGR01134 189 DGYVVASESCALdilgAEFVRDV---EPGEVVVIFDGGLESRQCARRpRAPCVfeyvYFARPDSV 250
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
85-189 1.02e-13

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


Pssm-ID: 433279 [Multi-domain]  Cd Length: 130  Bit Score: 68.49  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    85 HAGIAHTRWATHGEPAPRNsHPQSSgPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvfdkanEEG 164
Cdd:pfam13522  11 GVALGHVRLAIVDLPDAGN-QPMLS-RDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALY--------EEW 80
                          90       100
                  ....*....|....*....|....*
gi 75273435   165 GQtvtfcevvfEVMRHLEGAYALIF 189
Cdd:pfam13522  81 GE---------DCLERLRGMFAFAI 96
PLN02440 PLN02440
amidophosphoribosyltransferase
1-189 1.83e-13

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 73.17  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    1 MCGIFA-YLNFHANKErryildvLFNGLRRLEYRGYDSAGIAidnsspSSSPLVFRQ-AGNieSLVNSVNEEITNTDLNl 78
Cdd:PLN02440   1 ECGVVGiFGDPEASRL-------CYLGLHALQHRGQEGAGIV------TVDGNRLQSiTGN--GLVSDVFDESKLDQLP- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   79 devfyFHAGIAHTRWATHGEPAPRNSHPQSSG-PGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIpkLAKFVF 157
Cdd:PLN02440  65 -----GDIAIGHVRYSTAGASSLKNVQPFVANyRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVL--LHLIAI 137
                        170       180       190
                 ....*....|....*....|....*....|..
gi 75273435  158 DKANeeggqtvTFCEVVFEVMRHLEGAYALIF 189
Cdd:PLN02440 138 SKAR-------PFFSRIVDACEKLKGAYSMVF 162
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
2-305 1.85e-13

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 73.14  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    2 CGIF-AYLNfhankERRYILDVLFNGLRRLEYRGYDSAGIAIDNSSPSSsplVFRQAGniesLVNSV-NEEITNTdlnld 79
Cdd:PRK05793  15 CGVFgVFSK-----NNIDVASLTYYGLYALQHRGQESAGIAVSDGEKIK---VHKGMG----LVSEVfSKEKLKG----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   80 evFYFHAGIAHTRWATHGEPAPRNSHP-QSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLakfvFD 158
Cdd:PRK05793  78 --LKGNSAIGHVRYSTTGASDLDNAQPlVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNL----IA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  159 KANEEGgqtvtFCEVVFEVMRHLEGAYALIFKSwhyPNELIACKLGS---PLLLGVKELDqgesnshvfqdahflskndh 235
Cdd:PRK05793 152 RSAKKG-----LEKALVDAIQAIKGSYALVILT---EDKLIGVRDPHgirPLCLGKLGDD-------------------- 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75273435  236 pkeFFLSSDPHAL-VEHTKKVLVIEDGEVVNLKDGGVSILKFEnERGRCNG-------LSRPASVERALSVLEMEVEQ 305
Cdd:PRK05793 204 ---YILSSESCALdTIGAEFIRDVEPGEIVIIDEDGIKSIKFA-EKTKCQTcafeyiyFARPDSVIDGISVYESRVRA 277
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
355-487 2.57e-13

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: 67.64  E-value: 2.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 355 KTIRRSRRIVFIGCGTSYNAAlasrpilEELS------GIPVSMEIASDLW-DRQGPIYREDTAVFVSQSGETADTLLAL 427
Cdd:cd05013   8 DLLAKARRIYIFGVGSSGLVA-------EYLAykllrlGKPVVLLSDPHLQlMSAANLTPGDVVIAISFSGETKETVEAA 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75273435 428 DYARENGALCVGITNTVGSSIARKTHcgVHINAGAEIGVASTKAYTSQIVVMVML-ALAIG 487
Cdd:cd05013  81 EIAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLALIdALFLA 139
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
2-149 3.72e-13

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: 69.60  E-value: 3.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   2 CGIFAylnFHANKERRYILDVLFNGLRRLEYRG-YDSAGIAI----DNSSPSSSPL--VFRQAGNIESLVNSvneeitnt 74
Cdd:cd01907   1 CGIFG---IMSKDGEPFVGALLVEMLDAMQERGpGDGAGFALygdpDAFVYSSGKDmeVFKGVGYPEDIARR-------- 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75273435  75 dLNLDEVFYFHaGIAHTRWATHGEPAPRNSHPQSSGpgdDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVI 149
Cdd:cd01907  70 -YDLEEYKGYH-WIAHTRQPTNSAVWWYGAHPFSIG---DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVI 139
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
357-504 7.51e-13

DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 69.57  E-value: 7.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 357 IRRSRRIVFIGCGTSYNAAlasrpilEELS------GIPVSM-EIASDLWDRQ-GPIYREDTAVFVSQSGETADTLLALD 428
Cdd:COG1737 131 LAKARRIYIFGVGASAPVA-------EDLAykllrlGKNVVLlDGDGHLQAESaALLGPGDVVIAISFSGYTRETLEAAR 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 429 YARENGALCVGITNTVGSSIARktHCGVHINAGAEIGVASTKAYTSQIVVMVM-------LALAIGSDTISSQKRREAII 501
Cdd:COG1737 204 LAKERGAKVIAITDSPLSPLAK--LADVVLYVPSEEPTLRSSAFSSRVAQLALidalaaaVAQRDGDKARERLERTEALL 281

                ...
gi 75273435 502 DGL 504
Cdd:COG1737 282 SEL 284
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
362-453 1.22e-12

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: 64.90  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 362 RIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGPIYREDT-AVFVSQSGETADTLLALDYARENGALCVGI 440
Cdd:cd05710   1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKSvVILASHSGNTKETVAAAKFAKEKGATVIGL 80
                        90
                ....*....|...
gi 75273435 441 TNTVGSSIARKTH 453
Cdd:cd05710  81 TDDEDSPLAKLAD 93
frlB PRK11382
fructoselysine 6-phosphate deglycase;
362-668 3.79e-10

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 61.94  E-value: 3.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  362 RIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGpiYRED---TAVFVSQSGETADTLLALDYARENGALCV 438
Cdd:PRK11382  46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTP--YRLDdrcAVIGVSDYGKTEEVIKALELGRACGALTA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  439 GITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTsqiVVMVMLALAIGSDTISSQKrreaiiDGLLDLPYKVKEVLKL- 517
Cdd:PRK11382 124 AFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMITRLAPNAEIGKIK------NDLKQLPNALGHLVRTw 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  518 DDEMKDLAQLLIDEQSLLVFGRGYNYATAL-EGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQ 596
Cdd:PRK11382 195 EEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTT 274
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75273435  597 QSVIQQLHARKGRLIVMcskgDAASVSSSgscraievpqVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPR 668
Cdd:PRK11382 275 ERAINFVKQRTDNVIVI----DYAEISQG----------LHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
1-152 3.87e-10

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: 62.93  E-value: 3.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   1 MCGIFAYLNFHANKERryilDVLFNGLRRLEYRGYDSAGIAIDNsspsssplvfrqagnieslvnsvneeitntdlnlde 80
Cdd:COG0367   1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------ 40
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75273435  81 vfyfHAGIAHTRWATHGEPAprNSH-PQSSgPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKL 152
Cdd:COG0367  41 ----GVALGHRRLSIIDLSE--GGHqPMVS-EDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
106-188 1.64e-09

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


Pssm-ID: 433289 [Multi-domain]  Cd Length: 123  Bit Score: 55.99  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   106 PQSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKfvfdkanEEGGQtvtfcevvfEVMRHLEGAY 185
Cdd:pfam13537  15 PMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE-------AEWGE---------DCVDRLNGMF 78

                  ...
gi 75273435   186 ALI 188
Cdd:pfam13537  79 AFA 81
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
2-152 2.83e-09

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: 57.57  E-value: 2.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   2 CGIFAYLNFHANKERRyilDVLFNGLRRLEYRGYDSAGIAIDNsspsssplvfrqagnieslvnsvneeitntdlnldev 81
Cdd:cd00712   1 CGIAGIIGLDGASVDR---ATLERMLDALAHRGPDGSGIWIDE------------------------------------- 40
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75273435  82 fyfHAGIAHTRWATHGepaPRNSH-PQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKL 152
Cdd:cd00712  41 ---GVALGHRRLSIID---LSGGAqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL 105
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
395-482 1.81e-08

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 56.33  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  395 ASDLWDRQgpIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVAST--KAY 472
Cdd:PRK05441 121 AADLKAIN--LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAG 198
                         90
                 ....*....|
gi 75273435  473 TSQIVVMVML 482
Cdd:PRK05441 199 TAQKLVLNMI 208
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
361-486 2.44e-08

KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.


Pssm-ID: 240145 [Multi-domain]  Cd Length: 128  Bit Score: 52.93  E-value: 2.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 361 RRIVFIGCGTSYnaalasrPILEELSGIPVSMEIAS-----------DLwdrqGPIYREDTAVFVSQSGETADTLLALDY 429
Cdd:cd05014   1 GKVVVTGVGKSG-------HIARKIAATLSSTGTPAfflhptealhgDL----GMVTPGDVVIAISNSGETDELLNLLPH 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75273435 430 ARENGALCVGITNTVGSSIARktHCGVHINAGAE-----IGVASTkayTSQIVVMVML-ALAI 486
Cdd:cd05014  70 LKRRGAPIIAITGNPNSTLAK--LSDVVLDLPVEeeacpLGLAPT---TSTTAMLALGdALAV 127
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
2-149 4.54e-08

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 54.59  E-value: 4.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   2 CGIFAYLnfhANKER--RYILDVLFNGLRRleyRGYDSA--------GIAIDNSSPSssPLVFRQAGNIESlvnsvneei 71
Cdd:COG0121   1 CRLLGYS---GNVPTdlEFLLLDPEHSLVR---QSGATRegphadgwGIGWYEGDGE--PRLYRDPLPAWS--------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  72 tntDLNLDEV---FYFHAGIAHTRWATHGEPAPRNSHPQSsgpGDDFLVVHNGVITNYEVLKETL-----VRHGFTFESD 143
Cdd:COG0121  64 ---DPNLRLLarpIKSRLVIAHVRKATVGPVSLENTHPFR---GGRWLFAHNGQLDGFDRLRRRLaeelpDELYFQPVGT 137

                ....*.
gi 75273435 144 TDTEVI 149
Cdd:COG0121 138 TDSELA 143
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
49-149 9.38e-08

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


Pssm-ID: 238889 [Multi-domain]  Cd Length: 257  Bit Score: 53.93  E-value: 9.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  49 SSPLVFRQAGNIESLVNsvneeitntDLNLDEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPgddFLVVHNGVITNYEV 128
Cdd:cd01908  54 GRPFRYRSPLPAWSDIN---------LESLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGR---WLFAHNGQLDGFRL 121
                        90       100
                ....*....|....*....|..
gi 75273435 129 LKETLVRHGFTF-ESDTDTEVI 149
Cdd:cd01908 122 LRRRLLRLLPRLpVGTTDSELA 143
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
363-441 2.01e-07

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: 48.91  E-value: 2.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 363 IVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGPIY--REDTAVFVSQSGETADTLLALDYARENGALCVGI 440
Cdd:cd04795   1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80

                .
gi 75273435 441 T 441
Cdd:cd04795  81 T 81
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
409-486 7.14e-07

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: 50.98  E-value: 7.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 409 DTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVAST--KAYTSQIVVMVML--AL 484
Cdd:cd05007 120 DVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQKLALNMLstAV 199

                ..
gi 75273435 485 AI 486
Cdd:cd05007 200 MI 201
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
1-155 3.23e-06

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 50.48  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435    1 MCGIFAYLNfhaNKERRYILDVLFNGL-RRLEYRGYDSAGIAIDNSSPSSSplvfrqagNIeslvnsvneeitntdlnld 79
Cdd:PTZ00077   1 MCGILAIFN---SKGERHELRRKALELsKRLRHRGPDWSGIIVLENSPGTY--------NI------------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435   80 evfyfhagIAHTRWA-----THGEPAPRNSHPqssgpgddFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAK 154
Cdd:PTZ00077  51 --------LAHERLAivdlsDGKQPLLDDDET--------VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYK 114

                 .
gi 75273435  155 F 155
Cdd:PTZ00077 115 E 115
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
109-149 6.25e-06

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: 49.25  E-value: 6.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 75273435   109 SGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVI 149
Cdd:TIGR01536  62 SNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVI 102
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
355-486 1.47e-05

D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440557 [Multi-domain]  Cd Length: 317  Bit Score: 47.66  E-value: 1.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435 355 KTIRRSR-RIVFIGCGTS-----YNAA-LASrpileelSGIPvSMEI----AS--DLwdrqGPIYREDTAVFVSQSGETA 421
Cdd:COG0794  38 ELILNCKgRVVVTGMGKSghiarKIAAtLAS-------TGTP-AFFLhpaeAShgDL----GMITPGDVVIAISNSGETE 105
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75273435 422 DTLLALDYARENGALCVGITNTVGSSIARktHCGVHINAGAE-----IGVASTkayTSQIVVMVML-ALAI 486
Cdd:COG0794 106 ELLALLPLLKRLGVPLIAITGNPDSTLAR--AADVVLDLPVEreacpLNLAPT---TSTTATLALGdALAV 171
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
408-453 2.51e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 43.60  E-value: 2.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 75273435  408 EDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTH 453
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLAD 233
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
409-486 8.47e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 41.99  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273435  409 DTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVAST--KAYTSQIVVMVMLALAI 486
Cdd:PRK12570 129 DVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNMLSTAS 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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