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Conserved domains on  [gi|158262747|ref|NP_001103431|]
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Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02981 super family cl33615
glucosamine:fructose-6-phosphate aminotransferase
1-681 0e+00

glucosamine:fructose-6-phosphate aminotransferase


The actual alignment was detected with superfamily member PLN02981:

Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 929.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGIDggNDKDWEANACKIqlIKKKGKVKALDEEVHK---QQ 77
Cdd:PLN02981   1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLV--FREEGKIESLVRSVYEevaET 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  78 DMDLDIEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVK 157
Cdd:PLN02981  77 DLNLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 158 YMYD--NRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtGKDKKGS 235
Cdd:PLN02981 157 FVFDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKEL--------------PEEKNSS 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 236 cnlSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPG---------RAV 306
Cdd:PLN02981 223 ---AVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGglsrpasveRAL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 307 QTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDD----YTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGV 382
Cdd:PLN02981 300 STLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGsgkaKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAAL 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 383 ATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGV 462
Cdd:PLN02981 380 AARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGV 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 463 HINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLI 542
Cdd:PLN02981 460 HINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLV 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 543 MGRGYHYATCLEGALKIKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDK 622
Cdd:PLN02981 540 FGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSK 619
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262747 623 EDTETIKNTK--RTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:PLN02981 620 GDASSVCPSGgcRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
 
Name Accession Description Interval E-value
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
1-681 0e+00

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 929.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGIDggNDKDWEANACKIqlIKKKGKVKALDEEVHK---QQ 77
Cdd:PLN02981   1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLV--FREEGKIESLVRSVYEevaET 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  78 DMDLDIEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVK 157
Cdd:PLN02981  77 DLNLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 158 YMYD--NRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtGKDKKGS 235
Cdd:PLN02981 157 FVFDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKEL--------------PEEKNSS 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 236 cnlSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPG---------RAV 306
Cdd:PLN02981 223 ---AVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGglsrpasveRAL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 307 QTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDD----YTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGV 382
Cdd:PLN02981 300 STLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGsgkaKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAAL 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 383 ATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGV 462
Cdd:PLN02981 380 AARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGV 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 463 HINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLI 542
Cdd:PLN02981 460 HINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLV 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 543 MGRGYHYATCLEGALKIKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDK 622
Cdd:PLN02981 540 FGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSK 619
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262747 623 EDTETIKNTK--RTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:PLN02981 620 GDASSVCPSGgcRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
1-681 0e+00

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


Pssm-ID: 223526 [Multi-domain]  Cd Length: 597  Bit Score: 753.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYhvprtRREILETLIKGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmd 80
Cdd:COG0449    1 MCGIVGYIGF-----LREAIDILLEGLKRLEYRGYDSAGIAVVGDG---------SLNVRKQVGKISNLEELLNKE---- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  81 ldiEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKnneFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMY 160
Cdd:COG0449   63 ---PLIGGVGIAHTRWATHGGPTRANAHPHSDGE---FAVVHNGIIENFAELKEELEAKGYVFKSDTDTEVIAHLLEEIY 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 161 DnresqdTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscnlsr 240
Cdd:COG0449  137 D------TSLLEAVKKVLKRLEGSYALLCTHSDFPDELVAARKGSPLVIGV-----------------GEG--------- 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 241 vdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTagdhpgRAVQTLQMELQQIMKGN 320
Cdd:COG0449  185 ---------------ENFLASDVSALLNFTRRFVYLEEGDIAKLTTDGVSINDGNVL------RDVPVIEWDLCAAEKGG 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 321 FSSFMQKEIFEQPESVVNTMRGRVNFDDytVNLGGLKDhikeIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVEL 400
Cdd:COG0449  244 FRHFMLKEIYEQPEALRNTLQGRLDELV--QNELDLDI----LREVDRIIIVACGTSYHAGLVAKYFFERLAKIPVEVEE 317
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 401 ASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTS 480
Cdd:COG0449  318 ASEFRYREPALNPNTLVIAISQSGETADTLAALRLAKEQGAKTLAITNVPGSTIARESDHTLLIRAGPEIGVASTKAFTA 397
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 481 QFVSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKI 559
Cdd:COG0449  398 QVLALYLLALYLAKQRgTISEEEERSLIKELQKLPNHIPKVLAAEEKIKELAKRLADAKDFFFLGRGVLYPVALEGALKL 477
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 560 KEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTEtiKNTKRTIKVPH 639
Cdd:COG0449  478 KEISYIHAEGYAAGELKHGPIALIDENTPVIAIAPKPDLFEKTKSNIQEVRARGGKIIVIADEGDVA--EDGDDLILLPE 555
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 158262747 640 SVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:COG0449  556 VDELLAPLLYTIPLQLLAYHIALAKGIDVDKPRNLAKSVTVE 597
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
2-681 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: 637.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747    2 CGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGIdggndkdweANACKIQLIKKKGKVKALDEEVhkqQDMDL 81
Cdd:TIGR01135   1 CGIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAV---------VDEGKLFVRKAVGKVAELANKL---GEKPL 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   82 DIEFdvhlGIAHTRWATHGEPNPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:TIGR01135  63 PGGV----GIGHTRWATHGKPTDENAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELR 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  162 NresqDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscnlsrv 241
Cdd:TIGR01135 138 E----GGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGL-----------------GDG---------- 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  242 dsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKrtaGDHPGRAVQTLQMELQQIMKGNF 321
Cdd:TIGR01135 187 --------------ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFE---GAPVQREVRVIDWDLDAAEKGGY 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  322 SSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIqrcRRLILIACGTSYHAGVATRQVLEELTELPVMVELA 401
Cdd:TIGR01135 250 RHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNI---DRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIA 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  402 SDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQ 481
Cdd:TIGR01135 327 SEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQ 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  482 FVSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIK 560
Cdd:TIGR01135 407 LTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLK 486
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  561 EITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHS 640
Cdd:TIGR01135 487 EISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEV 566
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 158262747  641 VDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:TIGR01135 567 EELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
2-284 6.33e-111

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: 333.26  E-value: 6.33e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdl 81
Cdd:cd00714    1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---------SLEVVKAVGKVANLEEKLAEK----- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  82 diEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNnEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00714   61 --PLSGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 162 nresQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtgkdkkgscnlsrv 241
Cdd:cd00714  138 ----GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG--------------------------- 186
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 158262747 242 dsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAV 284
Cdd:cd00714  187 --------------ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
362-491 5.45e-38

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: 334514 [Multi-domain]  Cd Length: 131  Bit Score: 137.02  E-value: 5.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  362 EIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSGETADTLMGLRYCKERG 440
Cdd:pfam01380   1 LLAKAKRIYVIGRGTSYAIALELALKLEEIGYIHVEVELAGELKHGpLALVDEDDLVIAISFSGETKDLLALAELAKERG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 158262747  441 ALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALM 491
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHTLYIPASPETGVASTKSITAQLAALDALAVA 131
 
Name Accession Description Interval E-value
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
1-681 0e+00

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 929.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGIDggNDKDWEANACKIqlIKKKGKVKALDEEVHK---QQ 77
Cdd:PLN02981   1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLV--FREEGKIESLVRSVYEevaET 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  78 DMDLDIEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVK 157
Cdd:PLN02981  77 DLNLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 158 YMYD--NRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtGKDKKGS 235
Cdd:PLN02981 157 FVFDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKEL--------------PEEKNSS 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 236 cnlSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPG---------RAV 306
Cdd:PLN02981 223 ---AVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGglsrpasveRAL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 307 QTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDD----YTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGV 382
Cdd:PLN02981 300 STLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGsgkaKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAAL 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 383 ATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGV 462
Cdd:PLN02981 380 AARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGV 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 463 HINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLI 542
Cdd:PLN02981 460 HINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLV 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 543 MGRGYHYATCLEGALKIKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDK 622
Cdd:PLN02981 540 FGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSK 619
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262747 623 EDTETIKNTK--RTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:PLN02981 620 GDASSVCPSGgcRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
1-681 0e+00

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


Pssm-ID: 223526 [Multi-domain]  Cd Length: 597  Bit Score: 753.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYhvprtRREILETLIKGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmd 80
Cdd:COG0449    1 MCGIVGYIGF-----LREAIDILLEGLKRLEYRGYDSAGIAVVGDG---------SLNVRKQVGKISNLEELLNKE---- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  81 ldiEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKnneFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMY 160
Cdd:COG0449   63 ---PLIGGVGIAHTRWATHGGPTRANAHPHSDGE---FAVVHNGIIENFAELKEELEAKGYVFKSDTDTEVIAHLLEEIY 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 161 DnresqdTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscnlsr 240
Cdd:COG0449  137 D------TSLLEAVKKVLKRLEGSYALLCTHSDFPDELVAARKGSPLVIGV-----------------GEG--------- 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 241 vdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTagdhpgRAVQTLQMELQQIMKGN 320
Cdd:COG0449  185 ---------------ENFLASDVSALLNFTRRFVYLEEGDIAKLTTDGVSINDGNVL------RDVPVIEWDLCAAEKGG 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 321 FSSFMQKEIFEQPESVVNTMRGRVNFDDytVNLGGLKDhikeIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVEL 400
Cdd:COG0449  244 FRHFMLKEIYEQPEALRNTLQGRLDELV--QNELDLDI----LREVDRIIIVACGTSYHAGLVAKYFFERLAKIPVEVEE 317
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 401 ASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTS 480
Cdd:COG0449  318 ASEFRYREPALNPNTLVIAISQSGETADTLAALRLAKEQGAKTLAITNVPGSTIARESDHTLLIRAGPEIGVASTKAFTA 397
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 481 QFVSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKI 559
Cdd:COG0449  398 QVLALYLLALYLAKQRgTISEEEERSLIKELQKLPNHIPKVLAAEEKIKELAKRLADAKDFFFLGRGVLYPVALEGALKL 477
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 560 KEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTEtiKNTKRTIKVPH 639
Cdd:COG0449  478 KEISYIHAEGYAAGELKHGPIALIDENTPVIAIAPKPDLFEKTKSNIQEVRARGGKIIVIADEGDVA--EDGDDLILLPE 555
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 158262747 640 SVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:COG0449  556 VDELLAPLLYTIPLQLLAYHIALAKGIDVDKPRNLAKSVTVE 597
PRK00331 PRK00331
glucosamine--fructose-6-phosphate aminotransferase; Reviewed
1-681 0e+00

glucosamine--fructose-6-phosphate aminotransferase; Reviewed


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 737.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAGVG-IDGGNdkdweanackIQLIKKKGKVKALDEEVHKQqdm 79
Cdd:PRK00331   1 MCGIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAvLDDGG----------LEVRKAVGKVANLEAKLEEE--- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  80 dldiEFDVHLGIAHTRWATHGEPNPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 159
Cdd:PRK00331  62 ----PLPGTTGIGHTRWATHGKPTERNAHPHT-DCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEE 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 160 YDnresQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscnls 239
Cdd:PRK00331 137 LK----EGGDLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL-----------------GEG-------- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 240 rvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVvdGRLSIHrIKRTAGDHPGRAVQTLQMELQQIMKG 319
Cdd:PRK00331 188 ----------------ENFLASDALALLPYTRRVIYLEDGEIAVL--TRDGVE-IFDFDGNPVEREVYTVDWDASAAEKG 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 320 NFSSFMQKEIFEQPESVVNTMRGRVNFDdytvnlGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVE 399
Cdd:PRK00331 249 GYRHFMLKEIYEQPEAIRDTLEGRLDEL------GEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVE 322
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 400 LASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYT 479
Cdd:PRK00331 323 IASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFT 402
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 480 SQFVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALK 558
Cdd:PRK00331 403 AQLAVLYLLALALAKARGTLsAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALK 482
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 559 IKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDtETIKNTKRTIKVP 638
Cdd:PRK00331 483 LKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGD-EVAEEADDVIEVP 561
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|...
gi 158262747 639 HSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:PRK00331 562 EVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
1-681 0e+00

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 721.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGIDGGNDKDWEANACKIQ------LIKKKGKVKALDEEVH 74
Cdd:PTZ00394   1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAASAptprpcVVRSVGNISQLREKVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  75 KQQD----MDLDIEFDVHLGIAHTRWATHGEPNPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTE 150
Cdd:PTZ00394  81 SEAVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 151 TIAKLVKYMYDNRESQdtSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSehklstdhipilyrtGK 230
Cdd:PTZ00394 160 VISVLSEYLYTRKGIH--NFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRR---------------TD 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 231 DKKGSCNLSRVDsttclFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPGRAVQTLQ 310
Cdd:PTZ00394 223 DRGCVMKLQTYD-----LTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQHLD 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 311 MELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDH-IKEIQRCRRLILIACGTSYHAGVATRQVLE 389
Cdd:PTZ00394 298 AKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPLFE 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 390 ELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPE 469
Cdd:PTZ00394 378 ELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVE 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 470 IGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSM-DDEIQKLATELYHQKSVLIMGRGYH 548
Cdd:PTZ00394 458 VGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYD 537
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 549 YATCLEGALKIKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETI 628
Cdd:PTZ00394 538 LATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELK 617
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158262747 629 KNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:PTZ00394 618 AAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
2-681 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: 637.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747    2 CGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGIdggndkdweANACKIQLIKKKGKVKALDEEVhkqQDMDL 81
Cdd:TIGR01135   1 CGIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAV---------VDEGKLFVRKAVGKVAELANKL---GEKPL 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   82 DIEFdvhlGIAHTRWATHGEPNPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:TIGR01135  63 PGGV----GIGHTRWATHGKPTDENAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELR 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  162 NresqDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscnlsrv 241
Cdd:TIGR01135 138 E----GGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGL-----------------GDG---------- 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  242 dsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKrtaGDHPGRAVQTLQMELQQIMKGNF 321
Cdd:TIGR01135 187 --------------ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFE---GAPVQREVRVIDWDLDAAEKGGY 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  322 SSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIqrcRRLILIACGTSYHAGVATRQVLEELTELPVMVELA 401
Cdd:TIGR01135 250 RHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNI---DRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIA 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  402 SDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQ 481
Cdd:TIGR01135 327 SEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQ 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  482 FVSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIK 560
Cdd:TIGR01135 407 LTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLK 486
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  561 EITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHS 640
Cdd:TIGR01135 487 EISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEV 566
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 158262747  641 VDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:TIGR01135 567 EELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
1-680 2.23e-155

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 463.34  E-value: 2.23e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVG-IDGGND------KDWEANACKIQLIKKKGKvkaldeEV 73
Cdd:PTZ00295  24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGElkttkyASDGTTSDSIEILKEKLL------DS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  74 HKQQdmdldiefdvHLGIAHTRWATHGEPNPVNSHPQrSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIA 153
Cdd:PTZ00295  92 HKNS----------TIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 154 KLVKYMYDNRESqdtsFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklSTDHIpilyrtgkdkk 233
Cdd:PTZ00295 161 NLIGLELDQGED----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGI------GDDSI----------- 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 234 gscnlsrvdsttclfpveekaveyYFASDASAVIEHTNRVIFLEDDDVAAV-VDGRLSIHRIKRtagdhpgraVQTLQME 312
Cdd:PTZ00295 220 ------------------------YVASEPSAFAKYTNEYISLKDGEIAELsLENVNDLYTQRR---------VEKIPEE 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 313 LQQIMKGNFSSFMQKEIFEQPESVVNTM--RGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEE 390
Cdd:PTZ00295 267 VIEKSPEPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQK 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 391 LTEL-PVMVELASDF-LDRNTpvfRDDVCF-FISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAG 467
Cdd:PTZ00295 347 LKCFnTVQVIDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAG 423
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 468 PEIGVASTKAYTSQFVSLVMFALMMCDDR-ISMQE-RRKEIMLGLKRLPDLIKEVL-SMDDEIQKLATELYHQKSVLIMG 544
Cdd:PTZ00295 424 REVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNyKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKNAKSMFILG 503
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 545 RGYHYATCLEGALKIKEITYMQSEGILAGELKHGPLALVDKL--MPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDK 622
Cdd:PTZ00295 504 KGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKARGAYIIVITDD 583
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158262747 623 EDtETIKNTKRTIKVPhSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTV 680
Cdd:PTZ00295 584 ED-LVKDFADEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
2-284 6.33e-111

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: 333.26  E-value: 6.33e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdl 81
Cdd:cd00714    1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---------SLEVVKAVGKVANLEEKLAEK----- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  82 diEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNnEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00714   61 --PLSGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 162 nresQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtgkdkkgscnlsrv 241
Cdd:cd00714  138 ----GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG--------------------------- 186
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 158262747 242 dsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAV 284
Cdd:cd00714  187 --------------ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
525-679 3.09e-67

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: 217.13  E-value: 3.09e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 525 DEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQN 604
Cdd:cd05009    1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262747 605 ALQQVVARQGRPVVICDKEDTETIKNTkrTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVT 679
Cdd:cd05009   81 LIKEVKARGAKVIVITDDGDAKDLADV--VIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
368-493 7.51e-63

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: 204.65  E-value: 7.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 368 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGIT 447
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 158262747 448 NTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMC 493
Cdd:cd05008   81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB and related proteins with duplicated sugar isomerase (SIS) ...
322-681 4.26e-57

Fructoselysine-6-P-deglycase FrlB and related proteins with duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225132 [Multi-domain]  Cd Length: 340  Bit Score: 196.76  E-value: 4.26e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 322 SSFMQKEIFEQPESVVNTM-RGRVNFDDytvnlggLKDHIKEIQRcRRLILIACGTSYHAGVATRQVLEELTELPVMVEL 400
Cdd:COG2222    2 STLMLREIEQQPAVVARLLeANRAVLAE-------LADFLRKRGI-DRILFVGCGSSLHAATPAKYLLERELGLLVAAIP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 401 ASDFLDRNTPVF-RDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYT 479
Cdd:COG2222   74 ASEFLTNGAKYLgEDSLVIAFSQSGNTPESVAAAELAKEGGALTIALTNEEDSPLARAADYVIPYLAGEEASVAATKSFT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 480 SQFVSLvmfalmmcddrisMQERRK--EIMLGLKRLPDLIKEVL-SMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGA 556
Cdd:COG2222  154 ASLLAL-------------LALLAEydGDAQLLAALPDLPLEAAkALEEDAQEFAEEYADEDRIYTLGSGPLYGAAYEAA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 557 LKIKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTyAKCQNALQQVVARQGRPVVICDKEDTETikntkRTIK 636
Cdd:COG2222  221 LKLKEMQWIHSEAISSGEFRHGPKELVEEGTPVLLFVSEDET-RELDERALKFLKNYGAKVLVIDAKDAAL-----DLID 294
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 158262747 637 VPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 681
Cdd:COG2222  295 QRVRHDLAPPLLSLVVAQRLAYALAVARGHNPDTPRYYGLVKVTR 339
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
2-282 4.14e-51

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: 176.49  E-value: 4.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAYLNYHVPRTRReiLETLIKGLQRLEYRGYDSAGVGIDGGndkdweanackiqlikKKGKVKALDEEVHKQQDMDL 81
Cdd:cd00352    1 CGIFGIVGADGAASLL--LLLLLRGLAALEHRGPDGAGIAVYDG----------------DGLFVEKRAGPVSDVALDLL 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  82 DIEFDVHLGIAHTRWATHGEPNPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00352   63 DEPLKSGVALGHVRLATNGLPSEANAQPFRSE-DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGR 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 162 NREsqdtsFTTLVERVIQQLEGAFALVFKSVHfPGQAVGTRRG---SPLLIGVRSEHklstdhipilyrtgkdkkgscnl 238
Cdd:cd00352  142 EGG-----LFEAVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGITKDG----------------------- 192
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 158262747 239 srvdsttclfpveekavEYYFASDASAVIEHT-NRVIFLEDDDVA 282
Cdd:cd00352  193 -----------------GLVFASEPKALLALPfKGVRRLPPGELL 220
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
362-491 5.45e-38

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: 334514 [Multi-domain]  Cd Length: 131  Bit Score: 137.02  E-value: 5.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  362 EIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSGETADTLMGLRYCKERG 440
Cdd:pfam01380   1 LLAKAKRIYVIGRGTSYAIALELALKLEEIGYIHVEVELAGELKHGpLALVDEDDLVIAISFSGETKDLLALAELAKERG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 158262747  441 ALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALM 491
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHTLYIPASPETGVASTKSITAQLAALDALAVA 131
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
533-664 1.62e-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: 334514 [Multi-domain]  Cd Length: 131  Bit Score: 135.87  E-value: 1.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  533 ELYHQKSVLIMGRGYHYATCLEGALKIKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQnALQQVVAR 612
Cdd:pfam01380   1 LLAKAKRIYVIGRGTSYAIALELALKLEEIGYIHVEVELAGELKHGPLALVDEDDLVIAISFSGETKDLLA-LAELAKER 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158262747  613 QGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLR 664
Cdd:pfam01380  80 GAKIIAITDSPGSPLAREADHTLYIPASPETGVASTKSITAQLAALDALAVA 131
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
2-212 1.17e-20

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: 91.75  E-value: 1.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFA-YLNYHVPRTrreiletLIKGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKVkaldEEVHKQQDMD 80
Cdd:cd00715    1 CGVFGiYGAEDAARL-------TYLGLYALQHRGQESAGIATSDGK---------RFHTHKGMGLV----SDVFDEEKLR 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  81 ldiEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKym 159
Cdd:cd00715   61 ---RLPGNIAIGHVRYSTAGSSSLENAQPFVVNSPLGGIALaHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA-- 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158262747 160 ydnRESQDTSFTTLVERVIQQLEGAFALVFksvhfpgqavGTRRGsplLIGVR 212
Cdd:cd00715  136 ---RSLAKDDLFEAIIDALERVKGAYSLVI----------MTADG---LIAVR 172
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism];
1-214 8.61e-20

Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism];


Pssm-ID: 223112  Cd Length: 470  Bit Score: 92.66  E-value: 8.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYHVPRTRREILEtlikGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKVKaldeEVHKQQDMD 80
Cdd:COG0034    4 MCGVFGIWGHKDNNAAQLTYY----GLYALQHRGQEAAGIAVADGK---------RFHTHKGMGLVS----DVFNERDLL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  81 LdiEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKym 159
Cdd:COG0034   67 R--KLQGNVGIGHVRYSTAGSSSIENAQPFYVNSPGGGIALaHNGNLVNAEELRRELEEEGAIFNTTSDSEVLLHLLA-- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158262747 160 ydnRESQDTSFTTLVERVIQQLEGAFALVfksVHFPGQAVGTR--RG-SPLLIGVRSE 214
Cdd:COG0034  143 ---RELDEDDIFEAVKEVLRRVKGAYALV---ALIKDGLIAVRdpNGiRPLVLGKLGD 194
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
2-212 1.59e-18

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


Pssm-ID: 273461  Cd Length: 442  Bit Score: 88.53  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747    2 CGIFAYlNYHVPRTRREIletlIKGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKVKaldeEVHKQQDMDl 81
Cdd:TIGR01134   1 CGVVGI-YGQEEVAASLT----YYGLYALQHRGQESAGISVFDGN---------RFRLHKGNGLVS----DVFNEEHLQ- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   82 diEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYmy 160
Cdd:TIGR01134  62 --RLKGNVGIGHVRYSTAGSSGLENAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAH-- 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158262747  161 dNRESQDTSFTTlVERVIQQLEGAFALVFKSVHF------PgqaVGTRrgsPLLIGVR 212
Cdd:TIGR01134 138 -NDESKDDLFDA-VARVLERVRGAYALVLMTEDGlvavrdP---HGIR---PLVLGRR 187
PLN02440 PLN02440
amidophosphoribosyltransferase
1-213 5.63e-16

amidophosphoribosyltransferase


Pssm-ID: 215241  Cd Length: 479  Bit Score: 80.88  E-value: 5.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYlnYHVPRTRREILEtlikGLQRLEYRGYDSAG-VGIDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDM 79
Cdd:PLN02440   1 ECGVVGI--FGDPEASRLCYL----GLHALQHRGQEGAGiVTVDGN----------RLQSITGNGLVS----DVFDESKL 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  80 DldiEFDVHLGIAHTRWATHGEPNPVNSHPqrsdknneFI---------VIHNGIITNYKDLKKFLESKGYDFESETDTE 150
Cdd:PLN02440  61 D---QLPGDIAIGHVRYSTAGASSLKNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTE 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262747 151 TIAKLVKymydnrESQDTSFTTLVERVIQQLEGAFALVFKsvhFPGQAVGTR-----RgsPLLIGVRS 213
Cdd:PLN02440 130 VLLHLIA------ISKARPFFSRIVDACEKLKGAYSMVFL---TEDKLVAVRdphgfR--PLVMGRRS 186
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
2-188 5.89e-15

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611  Cd Length: 469  Bit Score: 77.77  E-value: 5.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIF-AYLNyhvprTRREILETLIKGLQRLEYRGYDSAGVGIdggndkdweANACKIQLIKKKGKVkaldEEVHKQQDMD 80
Cdd:PRK05793  15 CGVFgVFSK-----NNIDVASLTYYGLYALQHRGQESAGIAV---------SDGEKIKVHKGMGLV----SEVFSKEKLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  81 ldiEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKym 159
Cdd:PRK05793  77 ---GLKGNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIaHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIA-- 151
                        170       180
                 ....*....|....*....|....*....
gi 158262747 160 ydnRESQdTSFTTLVERVIQQLEGAFALV 188
Cdd:PRK05793 152 ---RSAK-KGLEKALVDAIQAIKGSYALV 176
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
2-160 3.24e-14

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: 72.69  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAYLNyhvpRTRREIL-ETLIKGLQRLEYRG-YDSAGVGIDGGND-------KDweanackIQLIKKKGkvkaLDEE 72
Cdd:cd01907    1 CGIFGIMS----KDGEPFVgALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgKD-------MEVFKGVG----YPED 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  73 VHKQQDMDldiEFDVHLGIAHTRWATHGEPNPVNSHPqrsdknneF-----IVIHNGIITNYKDLKKFLESKGYDFESET 147
Cdd:cd01907   66 IARRYDLE---EYKGYHWIAHTRQPTNSAVWWYGAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFETET 134
                        170
                 ....*....|...
gi 158262747 148 DTETIAKLVKYMY 160
Cdd:cd01907  135 DTEVIAYYLDLLL 147
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
368-459 6.98e-14

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: 68.37  E-value: 6.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 368 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFISQSGETADTLMGLRYCKERGALTVGI 446
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
                         90
                 ....*....|...
gi 158262747 447 TNTVGSSISRETD 459
Cdd:cd05710   81 TDDEDSPLAKLAD 93
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
90-189 1.69e-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: 316080 [Multi-domain]  Cd Length: 130  Bit Score: 67.70  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   90 GIAHTRWATHGEPN----PVNSHpqrsdkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkymydnres 165
Cdd:pfam13522  13 ALGHVRLAIVDLPEagaqPMLSR------DGRLVLVHNGEIYNYGELREELPALGHAFRSRSDTEVLLAL---------- 76
                          90       100
                  ....*....|....*....|....
gi 158262747  166 qdtsFTTLVERVIQQLEGAFALVF 189
Cdd:pfam13522  77 ----YEEWGEDVLERLRGMFAFAI 96
PRK07349 PRK07349
amidophosphoribosyltransferase; Provisional
2-214 1.23e-12

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235998  Cd Length: 500  Bit Score: 70.51  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAylnyhVPRTRREILETLIKGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKV-KALDEEVHKQQDMD 80
Cdd:PRK07349  34 CGVFG-----VYAPGEEVAKLTYFGLYALQHRGQESAGIATFEGD---------KVHLHKDMGLVsQVFDEDILEELPGD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  81 LdiefdvhlGIAHTRWATHGEPNPVNSHPQRSD-KNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 159
Cdd:PRK07349 100 L--------AVGHTRYSTTGSSRKANAQPAVLEtRLGPLALAHNGNLVNTVELREELLARGCELTTTTDSEMIAFAIAQA 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158262747 160 YDnresQDTSFTTLVERVIQQLEGAFALVFKSvhfPGQAVGTRRGS---PLLIGVRSE 214
Cdd:PRK07349 172 VD----AGKDWLEAAISAFQRCQGAFSLVIGT---PEGLMGVRDPNgirPLVIGTLGE 222
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
112-188 4.03e-12

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


Pssm-ID: 338803 [Multi-domain]  Cd Length: 122  Bit Score: 63.28  E-value: 4.03e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262747  112 SDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYdnresqdtsfttlVERVIQQLEGAFALV 188
Cdd:pfam13537  17 VSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW-------------GEDCLDRLNGMFAFA 80
PRK06388 PRK06388
amidophosphoribosyltransferase; Provisional
21-188 1.50e-11

amidophosphoribosyltransferase; Provisional


Pssm-ID: 102351 [Multi-domain]  Cd Length: 474  Bit Score: 66.86  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  21 ETLIKGLQRLEYRGYDSAGVGIDGGNdkdweanacKIQLIKKKGKVKaldeEVHKQQDMDLDiefdVHLGIAHTRWATHG 100
Cdd:PRK06388  33 SPIITALRTLQHRGQESAGMAVFDGR---------KIHLKKGMGLVT----DVFNPATDPIK----GIVGVGHTRYSTAG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 101 EPNPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTET-IAKLVkymydnRESQDTSFTTLVERVI 178
Cdd:PRK06388  96 SKGVENAGPFVINSSLGYIGIsHNGEIVNADELREEMKKEGYIFQSDSDTEVmLAELS------RNISKYGLKEGFERSM 169
                        170
                 ....*....|
gi 158262747 179 QQLEGAFALV 188
Cdd:PRK06388 170 ERLRGAYACA 179
GltB1 COG0067
Glutamate synthase domain 1 [Amino acid transport and metabolism];
79-156 1.60e-11

Glutamate synthase domain 1 [Amino acid transport and metabolism];


Pssm-ID: 223145  Cd Length: 371  Bit Score: 66.21  E-value: 1.60e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262747  79 MDLDIE-FDVHLGIAHTRWATHGEPNPVNSHPQRSdknnefiVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLV 156
Cdd:COG0067  193 LDLDDErYKSAIALVHTRFSTNTFPSWPLAHPFRL-------LVHNGEINTYGGNRNWLEARGYKFESPTDGEVLAKLL 264
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
420-491 5.13e-11

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 64.03  E-value: 5.13e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262747 420 ISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--ALM 491
Cdd:PRK05441 138 IAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstGVM 213
PRK08341 PRK08341
amidophosphoribosyltransferase; Provisional
2-189 6.34e-11

amidophosphoribosyltransferase; Provisional


Pssm-ID: 181395  Cd Length: 442  Bit Score: 64.85  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAYLNYHVPRTRreiletlIKGLQRLEYRGYDSAGVGIdggndkdWEAnacKIQLIKKKGKVkaldEEVHKQQDMDl 81
Cdd:PRK08341   5 CGIFAAYSENAPKKA-------YYALIALQHRGQEGAGISV-------WRH---RIRTVKGHGLV----SEVFKGGSLS- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  82 diEFDVHLGIAHTRWATHGEPNPVNSHPQRSdKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAklVKYMYD 161
Cdd:PRK08341  63 --RLKSNLAIGHVRYSTSGSLSEVQPLEVEC-CGYKIAIAHNGTLTNFLPLRRKYESRGVKFRSSVDTELIG--ISFLWH 137
                        170       180
                 ....*....|....*....|....*...
gi 158262747 162 NRESQDtSFTTLvERVIQQLEGAFALVF 189
Cdd:PRK08341 138 YSETGD-EFEAM-REVFNEVKGAYSVAI 163
PRK07272 PRK07272
amidophosphoribosyltransferase; Provisional
26-186 8.35e-11

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235984  Cd Length: 484  Bit Score: 64.72  E-value: 8.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  26 GLQRLEYRGYDSAG-VGIDGGndkdweanackiQLIKKKGKvkALDEEVHKQQDmDLDiEFDVHLGIAHTRWATHGEPNP 104
Cdd:PRK07272  30 GLHSLQHRGQEGAGiVSNDNG------------KLKGHRDL--GLLSEVFKDPA-DLD-KLTGQAAIGHVRYATAGSASI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 105 VNSHP---QRSDknNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVkymydnRESQDTSFTTLVERVIQQL 181
Cdd:PRK07272  94 ENIQPflfHFHD--MQFGLAHNGNLTNAVSLRKELEKQGAIFHSSSDTEILMHLI------RRSHNPTFMGKLKEALNTV 165

                 ....*
gi 158262747 182 EGAFA 186
Cdd:PRK07272 166 KGGFA 170
PRK07631 PRK07631
amidophosphoribosyltransferase; Provisional
2-186 1.19e-10

amidophosphoribosyltransferase; Provisional


Pssm-ID: 181061  Cd Length: 475  Bit Score: 64.08  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGIDGGNdkdweanackiQLIKKKGKvkALDEEVHKQQDMDl 81
Cdd:PRK07631  12 CGVFGIWGH------EEAAQITYYGLHSLQHRGQEGAGIVVTDGG-----------KLSAHKGL--GLVTEVFQNGELD- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  82 diefDVH--LGIAHTRWATHGEPNPVNSHPQ--RSdKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVK 157
Cdd:PRK07631  72 ----ALKgkAAIGHVRYATAGGGGYENVQPLlfRS-QTGSLALAHNGNLVNATQLKLQLENQGSIFQTTSDTEVLAHLIK 146
                        170       180
                 ....*....|....*....|....*....
gi 158262747 158 ymydnrESQDTSFTTLVERVIQQLEGAFA 186
Cdd:PRK07631 147 ------RSGAPTLKEQIKNALSMLKGAYA 169
PRK06781 PRK06781
amidophosphoribosyltransferase; Provisional
2-186 1.95e-10

amidophosphoribosyltransferase; Provisional


Pssm-ID: 136048  Cd Length: 471  Bit Score: 63.49  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGIDGGNdkdweanackiqlIKKKGKVKALDEEVHKQQDMDl 81
Cdd:PRK06781  12 CGVFGIWGH------ENAAQVSYYGLHSLQHRGQEGAGIVVNNGE-------------KIVGHKGLGLISEVFSRGELE- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  82 diEFDVHLGIAHTRWATHGEPNPVNSHP---QRSDknNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKy 158
Cdd:PRK06781  72 --GLNGKSAIGHVRYATAGGSEVANVQPllfRFSD--HSMALAHNGNLINAKMLRRELEAEGSIFQTSSDTEVLLHLIK- 146
                        170       180
                 ....*....|....*....|....*...
gi 158262747 159 mydnrESQDTSFTTLVERVIQQLEGAFA 186
Cdd:PRK06781 147 -----RSTKDSLIESVKEALNKVKGAFA 169
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
401-492 2.41e-10

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: 61.38  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 401 ASDFLDRNTPvfRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 478
Cdd:cd05007  108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
                         90
                 ....*....|....*.
gi 158262747 479 TSQFVSLVMF--ALMM 492
Cdd:cd05007  186 TAQKLALNMLstAVMI 201
PRK08525 PRK08525
amidophosphoribosyltransferase; Provisional
26-193 3.47e-10

amidophosphoribosyltransferase; Provisional


Pssm-ID: 181456  Cd Length: 445  Bit Score: 62.42  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  26 GLQRLEYRGYDSAGVGIdggndkdweANACKIQLIKKKGKVKaldeEVHKQQDMDLdieFDVHLGIAHTRWATHGEPNPV 105
Cdd:PRK08525  20 ALFAMQHRGQEASGISV---------SNGKKIKTIKGRGLVT----QVFNEDNLKT---LKGEIAIGHNRYSTAGNDSIL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 106 NSHPQRSDKN-NEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnrESQDTSfttLVERVI---QQL 181
Cdd:PRK08525  84 DAQPVFARYDlGEIAIVHNGNLVNKKEVRSRLIQDGAIFQTNMDTENLIHLIA------RSKKES---LKDRIIealKKI 154
                        170
                 ....*....|..
gi 158262747 182 EGAFALVFKSVH 193
Cdd:PRK08525 155 IGAYCLVLLSRS 166
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
2-188 3.60e-10

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: 60.26  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   2 CGIFAYLNYHVPRTRREILETLikgLQRLEYRGYDSAGvgidggndkdweanackiqlikkkgkvkaldeevhkqqdmdl 81
Cdd:cd00712    1 CGIAGIIGLDGASVDRATLERM---LDALAHRGPDGSG------------------------------------------ 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  82 dIEFDVHLGIAHTRWATHGepnPVNSH-PQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkYM- 159
Cdd:cd00712   36 -IWIDEGVALGHRRLSIID---LSGGAqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL--YEe 108
                        170       180
                 ....*....|....*....|....*....
gi 158262747 160 YDnresqdtsfttlvERVIQQLEGAFALV 188
Cdd:cd00712  109 WG-------------EDCLERLNGMFAFA 124
PRK09123 PRK09123
amidophosphoribosyltransferase; Provisional
88-212 4.29e-10

amidophosphoribosyltransferase; Provisional


Pssm-ID: 236384  Cd Length: 479  Bit Score: 62.22  E-value: 4.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  88 HLGIAHTRWATHGEPNPVNSHPQRSD-KNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnRESQ 166
Cdd:PRK09123  87 NRAIGHVRYSTTGETILRNVQPLFAElEFGGLAIAHNGNLTNALTLRRELIRRGAIFQSTSDTEVILHLIA-----RSRK 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 158262747 167 DtsftTLVERVI---QQLEGAFALVFKsvhfpgqavgTRRGsplLIGVR 212
Cdd:PRK09123 162 A----SFLDRFIdalRQVEGAYSLVAL----------TNTK---LIGAR 193
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
369-447 1.66e-09

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: 54.69  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 369 LILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFISQSGETADTLMGLRYCKERGALTVGI 446
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80

                 .
gi 158262747 447 T 447
Cdd:cd04795   81 T 81
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
360-493 1.67e-09

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


Pssm-ID: 223865 [Multi-domain]  Cd Length: 202  Bit Score: 58.05  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 360 IKEIQRCRRLILIA-CGTSYHAG---VATrqvleeL--TELPVMVELASDFLDRNTPVF-RDDVCFFISQSGETADTLMG 432
Cdd:COG0794   32 VELILECKGKVFVTgVGKSGLIGkkfAAR------LasTGTPAFFVGPAEALHGDLGMItPGDVVIAISGSGETKELLNL 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262747 433 LRYCKERGALTVGITNTVGSSISRETDCGVHINAGPE---IGVASTkayTSQFVSLVMF-ALMMC 493
Cdd:COG0794  106 APKAKRLGAKLIAITSNPDSSLAKAADVVLVIPVKTEacpLGLAPT---TSTTLTLALGdALAGT 167
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism];
1-152 2.87e-09

Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism];


Pssm-ID: 223444 [Multi-domain]  Cd Length: 542  Bit Score: 59.73  E-value: 2.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYHVPRTRREILETLIKglqRLEYRGYDSAGVGIDGGndkdweanackiqlikkkgkvkaldeevhkqqdmd 80
Cdd:COG0367    1 MCGIAGILNFKNLIDAKSIIEEMTK---LLRHRGPDDSGVWISLN----------------------------------- 42
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262747  81 ldiefdvhLGIAHTRWATHGepnPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETI 152
Cdd:COG0367   43 --------ALLGHRRLSIVD---LSGGRQPMIKEGGKYAIVYNGEIYNVEELRKELREAGYEFRTYSDTEVI 103
frlB PRK11382
fructoselysine-6-P-deglycase; Provisional
368-672 3.52e-09

fructoselysine-6-P-deglycase; Provisional


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 58.86  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 368 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFI--SQSGETADTLMGLRYCKERGALTVG 445
Cdd:PRK11382  46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 446 ITNTVGSSISRETDCGVHINAGPEIGVASTKAYTsqfVSLVMFAlmmcddRISMQERRKEIMLGLKRLPDLIKEVLSMDD 525
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMIT------RLAPNAEIGKIKNDLKQLPNALGHLVRTWE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 526 EIQKLATELYHQKSVL-------IMGRGYHyatclEGALKIKEITYMQSEGILAGELKHGPLALVDKLMPVIMIIMRDHT 598
Cdd:PRK11382 196 EKGRQLGELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDES 270
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262747 599 YAKCQNALQQVVARQGRPVVICDKEDTETIKntkrtikvphsvDCLQGILSVIPLQLLAFHLAVLRGYDVDFPR 672
Cdd:PRK11382 271 RHTTERAINFVKQRTDNVIVIDYAEISQGLH------------PWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
MurQ COG2103
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ...
414-491 4.66e-09

N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225014 [Multi-domain]  Cd Length: 298  Bit Score: 58.07  E-value: 4.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 414 DDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--A 489
Cdd:COG2103  130 KDVVVGIAASGRTPYVIGALEYARQRGATTIGIACNPGSAISRIADIAIEPVVGPEVLTGSTrlKAGTAQKLVLNMLstG 209

                 ..
gi 158262747 490 LM 491
Cdd:COG2103  210 VM 211
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
360-487 6.23e-09

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: 54.54  E-value: 6.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 360 IKEIQRCRRLILIACGTSYHAG--VATRqvleeLTELPVMVELASD---FLDRNTPVFRDDVCFFISQSGETADTLMGLR 434
Cdd:cd05013    7 VDLLAKARRIYIFGVGSSGLVAeyLAYK-----LLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAE 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158262747 435 YCKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM 487
Cdd:cd05013   82 IAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
367-493 7.83e-09

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: 54.09  E-value: 7.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 367 RRLILIACGTSYHAG---VATRQVleelTELPvmvelaSDFLDrntP----------VFRDDVCFFISQSGETADTLMGL 433
Cdd:cd05014    1 GKVVVTGVGKSGHIArkiAATLSS----TGTP------AFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLL 67
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262747 434 RYCKERGALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFVSLVMF-ALMMC 493
Cdd:cd05014   68 PHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALGdALAVA 128
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
413-487 2.70e-07

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


Pssm-ID: 224651 [Multi-domain]  Cd Length: 281  Bit Score: 52.30  E-value: 2.70e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262747 413 RDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEigVASTKAYTSQFVSLVM 487
Cdd:COG1737  177 PGDVVIAISFSGYTREIVEAAELAKERGAKVIAITDSADSPLAKLADIVLLVPVAEE--SFFRSPISSRIAQLAL 249
TIGR00274 TIGR00274
N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling ...
407-492 4.41e-07

N-acetylmuramic acid 6-phosphate etherase; This protein, MurQ, is involved in recycling components of the bacterial murein sacculus turned over during cell growth. The cell wall metabolite anhydro-N-acetylmuramic acid (anhMurNAc) is converted by a kinase, AnmK, to MurNAc-phosphate, then converted to N-acetylglucosamine-phosphate by this etherase, called MurQ. This family of proteins is similar to the C-terminal half of a number of vertebrate glucokinase regulator proteins and contains a Prosite pattern which is shared by this group of proteins in a region of local similarity. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 272991 [Multi-domain]  Cd Length: 291  Bit Score: 51.77  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  407 RNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVS 484
Cdd:TIGR00274 120 QNIHLTKNDVVVGIAASGRTPYVIAGLQYARSLGALTISIACNPKSAMSEIADIAIETIVGPEILTGSSrlKAGTAQKMV 199
                          90
                  ....*....|
gi 158262747  485 LVMF--ALMM 492
Cdd:TIGR00274 200 LNMLstASMI 209
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
1-188 4.86e-06

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 49.71  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYhvpRTRREILETLIKGL-QRLEYRGYDSAGVGIdggndkdweanackiqlikkkgkvkaldeevhkqqdm 79
Cdd:PTZ00077   1 MCGILAIFNS---KGERHELRRKALELsKRLRHRGPDWSGIIV------------------------------------- 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  80 dLDIEFDVHLGIAHTRWAThgePNPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYm 159
Cdd:PTZ00077  41 -LENSPGTYNILAHERLAI---VDLSDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKE- 115
                        170       180
                 ....*....|....*....|....*....
gi 158262747 160 YDNREsqdtsfttlverVIQQLEGAFALV 188
Cdd:PTZ00077 116 YGPKD------------FWNHLDGMFATV 132
asnB PRK09431
asparagine synthetase B; Provisional
1-273 5.17e-06

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 49.52  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   1 MCGIFAYLNYH--VPRTRREILEtlikGLQRLEYRGYDSAGVGIDGGndkdweanackiqlikkkgkvkaldeevhkqqd 78
Cdd:PRK09431   1 MCGIFGILDIKtdADELRKKALE----MSRLMRHRGPDWSGIYASDN--------------------------------- 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  79 mdldiefdvhlGI-AHTRWA----THGEPNPVNShpqrsDKNNefIVIHNGIITNYKDLKKFLESKgYDFESETDTETIA 153
Cdd:PRK09431  44 -----------AIlGHERLSivdvNGGAQPLYNE-----DGTH--VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVIL 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 154 KLvkYmydnrESQDTSFttlvervIQQLEGAFALVfksvhfpgqavgtrrgspLLIGVRSEHKLSTDHIPI--LYrTGKD 231
Cdd:PRK09431 105 AL--Y-----QEKGPDF-------LDDLDGMFAFA------------------LYDSEKDAYLIARDPIGIipLY-YGYD 151
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 158262747 232 KKGscnlsrvdsttclfpveekavEYYFASDASAVIEHTNRV 273
Cdd:PRK09431 152 EHG---------------------NLYFASEMKALVPVCKTI 172
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
120-189 6.07e-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: 48.87  E-value: 6.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  120 VIHNGIITNYKDLKKFLESKGYDFESETDTETIakLVKYMYDNresqdtsfttlvERVIQQLEGAFALVF 189
Cdd:TIGR01536  70 IVFNGEIYNHEELREELEAKGYTFQTDSDTEVI--LHLYEEWG------------EECVDRLDGMFAFAL 125
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
414-488 2.66e-05

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 46.22  E-value: 2.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262747 414 DDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF 488
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
88-155 4.10e-05

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 lucosamine-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 somwhat 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: 45.46  E-value: 4.10e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262747  88 HLGIAHTRWATHGEPNPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-ESETDTETIAKL 155
Cdd:cd01908   81 PLVLAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFAL 146
trio_amidotrans TIGR03104
asparagine synthase family amidotransferase; Members of this protein family are closely ...
120-154 1.13e-04

asparagine synthase family amidotransferase; Members of this protein family are closely related to several isoforms of asparagine synthetase (glutamine amidotransferase) and typically have been given this name in genome annotation to date. Each is part of a conserved three-gene cassette sparsely distributed across at least twenty different species known so far, including alpha, beta, and gamma Proteobacteria, Mycobacterium, and Prosthecochloris, which is a member of the Chlorobi. The other two members of the cassette are a probable protease and a member of the GNAT family of acetyltransferases.


Pssm-ID: 274430 [Multi-domain]  Cd Length: 589  Bit Score: 45.08  E-value: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 158262747  120 VIHNGIITNYKDLKKFLESKGYDFESETDTETIAK 154
Cdd:TIGR03104  72 LVFNGCIYNYRELRAELEALGYRFFSDGDTEVILK 106
YafJ COG0121
Predicted glutamine amidotransferase [General function prediction only];
88-142 1.74e-04

Predicted glutamine amidotransferase [General function prediction only];


Pssm-ID: 223199  Cd Length: 252  Bit Score: 43.53  E-value: 1.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 158262747  88 HLGIAHTRWATHGEPNPVNSHP-QRSDKNNEFIVIHNGIITNYKDL-KKFLESKGYD 142
Cdd:COG0121   71 ELVIAHVRKATQGEVSLSNTHPfTRELWGYIWLFAHNGQLDKFKLLeGRKLEPVGYT 127
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
540-622 8.06e-04

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: 38.51  E-value: 8.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 540 VLIMGRGYHYATCLEGALKIKEITYMQSEGILAGELKHGP-LALVDKLMPVIMIIMRdHTYAKCQNALQQVVARQGRPVV 618
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYS-GRTEELLAALEIAKELGIPVIA 79

                 ....
gi 158262747 619 ICDK 622
Cdd:cd04795   80 ITDA 83
PRK07847 PRK07847
amidophosphoribosyltransferase; Provisional
26-189 3.95e-03

amidophosphoribosyltransferase; Provisional


Pssm-ID: 236113  Cd Length: 510  Bit Score: 39.95  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  26 GLQRLEYRGYDSAGVGIdggndkdweANACKIQLIKKKGKV-KALDEEVhkqqdmdLDiEFDVHLGIAHTRWATHGEPNP 104
Cdd:PRK07847  43 GLYALQHRGQEAAGIAV---------SDGSQILVFKDLGLVsQVFDEQT-------LA-SLQGHVAIGHCRYSTTGASTW 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 105 VNSHPQ-RSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDF-----ESETDTETIAKLVKYmydnRESQDTSFTTLVErV 177
Cdd:PRK07847 106 ENAQPTfRATAAGGGVALgHNGNLVNTAELAARARDRGLIRgrdpaGATTDTDLVTALLAH----GAADSTLEQAALE-L 180
                        170
                 ....*....|..
gi 158262747 178 IQQLEGAFALVF 189
Cdd:PRK07847 181 LPTVRGAFCLVF 192
GATase_4 pfam13230
Glutamine amidotransferases class-II; This family captures members that are not found in ...
91-175 4.30e-03

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


Pssm-ID: 315813  Cd Length: 272  Bit Score: 39.22  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747   91 IAHTRWATHGEPNPVNSHP-QRSDKNNEFIVIHNGiitNYKDLKKFLeSKGYDFESETDTETI-----AKLVKYMYDNRE 164
Cdd:pfam13230  75 IAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNG---DLKGYKPRL-SGRFQPVGSTDSELAfcwllDELRARFPGARP 150
                          90
                  ....*....|.
gi 158262747  165 SQDTSFTTLVE 175
Cdd:pfam13230 151 SAGELFRALAE 161
PRK11337 PRK11337
DNA-binding transcriptional repressor RpiR; Provisional
414-459 5.56e-03

DNA-binding transcriptional repressor RpiR; Provisional


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 38.97  E-value: 5.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 158262747 414 DDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETD 459
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLAD 233
PRK09246 PRK09246
amidophosphoribosyltransferase; Provisional
26-188 7.13e-03

amidophosphoribosyltransferase; Provisional


Pssm-ID: 236427  Cd Length: 501  Bit Score: 39.39  E-value: 7.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747  26 GLQRLEYRGYDSAG-VGIDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDMdLDIEFDVhlGIAHTRWATHG---- 100
Cdd:PRK09246  20 ALTVLQHRGQDAAGiVTIDGN----------RFRLRKANGLVR----DVFRTRHM-RRLQGNM--GIGHVRYPTAGssss 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262747 101 -EPNP--VNShPqrsdknneF-IV-IHNGIITNYKDLKKFLeskgydFE-------SETDTET--------IAKLVKYmy 160
Cdd:PRK09246  83 aEAQPfyVNS-P--------YgITlAHNGNLTNAEELRKEL------FEkdrrhinTTSDSEVllnvfaheLQKFRGL-- 145
                        170       180
                 ....*....|....*....|....*...
gi 158262747 161 dnRESQDTSFTTlVERVIQQLEGAFALV 188
Cdd:PRK09246 146 --PLTPEDIFAA-VAAVHRRVRGAYAVV 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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