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Conserved domains on  [gi|1240630904|gb|ASY71163|]
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Glucosamine-6-phosphate deaminase [isomerizing], alternative [Sinorhizobium fredii CCBAU 83666]

Protein Classification

SIS domain-containing protein( domain architecture ID 11454870)

SIS (sugar isomerase) domain-containing protein such as Bacillus subtilis fructosamine deglycase FrlB, which catalyzes the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid

CATH:  3.40.50.10490
EC:  3.5.-.-
Gene Ontology:  GO:0097367|GO:0005975|GO:0016787
PubMed:  10203754
SCOP:  4000802

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 6-339 1.50e-112

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


:

Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 330.32  E-value: 1.50e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   6 RREIDEIPEAAARLLDRSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVASLGPSLASIYGAELK 85
Cdd:COG2222     1 AREIAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  86 LGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGE 165
Cdd:COG2222    81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 166 WTGDAGLKRAVADLPNQFAKAVKLNWQDFA-ADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPV 244
Cdd:COG2222   161 WGGDDALLAALDALPAALEAALAADWPAAAlAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 245 ALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATSARAQKAKRLPFVETGHPITDALALILPFYGFVEAWSRSRG 324
Cdd:COG2222   241 SLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALALARG 320

                         330
                  ....*....|....*
gi 1240630904 325 LNPDAPASLKKVTET 339
Cdd:COG2222   321 LDPDTPRHLNKVVKT 335
 
Name Accession Description Interval E-value
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 6-339 1.50e-112

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


Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 330.32  E-value: 1.50e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   6 RREIDEIPEAAARLLDRSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVASLGPSLASIYGAELK 85
Cdd:COG2222     1 AREIAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  86 LGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGE 165
Cdd:COG2222    81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 166 WTGDAGLKRAVADLPNQFAKAVKLNWQDFA-ADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPV 244
Cdd:COG2222   161 WGGDDALLAALDALPAALEAALAADWPAAAlAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 245 ALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATSARAQKAKRLPFVETGHPITDALALILPFYGFVEAWSRSRG 324
Cdd:COG2222   241 SLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALALARG 320

                         330
                  ....*....|....*
gi 1240630904 325 LNPDAPASLKKVTET 339
Cdd:COG2222   321 LDPDTPRHLNKVVKT 335
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 191-338 2.54e-41

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: 141.63  E-value: 2.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 191 WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEASVTEIA 270
Cdd:cd05009     3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1240630904 271 DGMSAKGAVVHATSARAQkAKRLPFVETGHPITD----ALALILPFYGFVEAWSRSRGLNPDAPASLKKVTE 338
Cdd:cd05009    83 KEVKARGAKVIVITDDGD-AKDLADVVIRVPATVeelsPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
5-261 1.68e-36

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 138.64  E-value: 1.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   5 MRREIDEIPEAAARLLD-RSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVAslgPSLASIYG-A 82
Cdd:PRK00331  254 MLKEIYEQPEAIRDTLEgRLDELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVE---VEIASEFRyR 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  83 ELKLG-GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVA--G 159
Cdd:PRK00331  331 DPVLSpKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVlyL 410

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 160 LAV-LGEWTG------DAGLKRAVADLPNQFAKAVKLN--WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMH 230
Cdd:PRK00331  411 LALaLAKARGtlsaeeEADLVHELRELPALIEQVLDLKeqIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIH 490

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1240630904 231 AEAYSAAEVLHGPVALVGARFPVLVLAARDA 261
Cdd:PRK00331  491 AEGYAAGELKHGPIALIDEGMPVVAIAPNDE 521
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 5-337 5.88e-36

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: 137.00  E-value: 5.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   5 MRREIDEIPEAAARLLdrsATALAAAGAALRAKDPAFLVT-------IARGSSDHAALFLKYAIELQAGRPVAslgPSLA 77
Cdd:TIGR01135 253 MLKEIYEQPRALRDTL---EGRIEENGGVFEELGAEELLKnidriqiVACGTSYHAGLVAKYLIERLAGIPVE---VEIA 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  78 SiygaELKLGGAA------AIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKS 151
Cdd:TIGR01135 327 S----EFRYRKPVvdkdtlVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKA 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 152 YVNSIVAgLAVLGEWTGDA----------GLKRAVADLPNQFAKAVKLNWQ--DFAADLGEVESLYVLGRGPALAIASEA 219
Cdd:TIGR01135 403 FTTQLTV-LYLLALALAKArgtlsaeeeaELVDALRRLPDLVEQVLLADESiaELAERYADKRNFLFLGRGLGYPIALEG 481

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 220 ALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATS------ARAQKAKRL 293
Cdd:TIGR01135 482 ALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFApeddetIASVADDVI 561

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1240630904 294 PFVETGHPITDALALIlPFYGFVEAWSRSRGLNPDAPASL-KKVT 337
Cdd:TIGR01135 562 KLPEVEELLAPIVYTI-PLQLLAYHIALAKGTDVDKPRNLaKSVT 605
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 42-163 1.11e-12

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 64.24  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  42 LVTIARGSSDHAALFLKYAIELQAGRPVASlgpslasIYGAELKLGGAA-------AIAISQSGKSPDIVAMAEAATRAG 114
Cdd:pfam01380   8 IFVIGRGTSYAIALELALKFEEIGYKVVEV-------ELASELRHGVLAlvdeddlVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1240630904 115 AVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVL 163
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALA 129
 
Name Accession Description Interval E-value
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 6-339 1.50e-112

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


Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 330.32  E-value: 1.50e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   6 RREIDEIPEAAARLLDRSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVASLGPSLASIYGAELK 85
Cdd:COG2222     1 AREIAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  86 LGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGE 165
Cdd:COG2222    81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 166 WTGDAGLKRAVADLPNQFAKAVKLNWQDFA-ADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPV 244
Cdd:COG2222   161 WGGDDALLAALDALPAALEAALAADWPAAAlAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 245 ALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATSARAQKAKRLPFVETGHPITDALALILPFYGFVEAWSRSRG 324
Cdd:COG2222   241 SLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALALARG 320

                         330
                  ....*....|....*
gi 1240630904 325 LNPDAPASLKKVTET 339
Cdd:COG2222   321 LDPDTPRHLNKVVKT 335
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 191-338 2.54e-41

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: 141.63  E-value: 2.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 191 WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEASVTEIA 270
Cdd:cd05009     3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1240630904 271 DGMSAKGAVVHATSARAQkAKRLPFVETGHPITD----ALALILPFYGFVEAWSRSRGLNPDAPASLKKVTE 338
Cdd:cd05009    83 KEVKARGAKVIVITDDGD-AKDLADVVIRVPATVeelsPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 5-261 3.15e-40

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


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 149.01  E-value: 3.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   5 MRREIDEIPEAAARLLDRSATALAAAGAALRAKDPAFLVTIAR------GSSDHAALFLKYAIELQAGRPVAslgPSLAS 78
Cdd:COG0449   254 MLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRiyivacGTSYHAGLVGKYLIEELARIPVE---VEIAS 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  79 --IYGAELKLGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSI 156
Cdd:COG0449   331 efRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQL 410

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 157 VAgLAVLGEWTG----------DAGLKRAVADLPNQFAKAVKLNWQ--DFAADLGEVESLYVLGRGPALAIASEAALKFK 224
Cdd:COG0449   411 AA-LYLLALYLArargtlsaeeEAELLEELRKLPEKIEEVLDLEEQieELAEKYADARNALFLGRGINYPVALEGALKLK 489

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1240630904 225 ETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDA 261
Cdd:COG0449   490 EISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDE 526
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
5-261 1.68e-36

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 138.64  E-value: 1.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   5 MRREIDEIPEAAARLLD-RSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVAslgPSLASIYG-A 82
Cdd:PRK00331  254 MLKEIYEQPEAIRDTLEgRLDELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVE---VEIASEFRyR 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  83 ELKLG-GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVA--G 159
Cdd:PRK00331  331 DPVLSpKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVlyL 410

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 160 LAV-LGEWTG------DAGLKRAVADLPNQFAKAVKLN--WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMH 230
Cdd:PRK00331  411 LALaLAKARGtlsaeeEADLVHELRELPALIEQVLDLKeqIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIH 490

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1240630904 231 AEAYSAAEVLHGPVALVGARFPVLVLAARDA 261
Cdd:PRK00331  491 AEGYAAGELKHGPIALIDEGMPVVAIAPNDE 521
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 5-337 5.88e-36

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: 137.00  E-value: 5.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   5 MRREIDEIPEAAARLLdrsATALAAAGAALRAKDPAFLVT-------IARGSSDHAALFLKYAIELQAGRPVAslgPSLA 77
Cdd:TIGR01135 253 MLKEIYEQPRALRDTL---EGRIEENGGVFEELGAEELLKnidriqiVACGTSYHAGLVAKYLIERLAGIPVE---VEIA 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  78 SiygaELKLGGAA------AIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKS 151
Cdd:TIGR01135 327 S----EFRYRKPVvdkdtlVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKA 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 152 YVNSIVAgLAVLGEWTGDA----------GLKRAVADLPNQFAKAVKLNWQ--DFAADLGEVESLYVLGRGPALAIASEA 219
Cdd:TIGR01135 403 FTTQLTV-LYLLALALAKArgtlsaeeeaELVDALRRLPDLVEQVLLADESiaELAERYADKRNFLFLGRGLGYPIALEG 481

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 220 ALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATS------ARAQKAKRL 293
Cdd:TIGR01135 482 ALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFApeddetIASVADDVI 561

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1240630904 294 PFVETGHPITDALALIlPFYGFVEAWSRSRGLNPDAPASL-KKVT 337
Cdd:TIGR01135 562 KLPEVEELLAPIVYTI-PLQLLAYHIALAKGTDVDKPRNLaKSVT 605
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 41-166 2.01e-35

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: 125.30  E-value: 2.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  41 FLVTIARGSSDHAALFLKYAIELQAGRPVASLGPSlASIYGAELKLGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIAL 120
Cdd:cd05008     1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAAS-EFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1240630904 121 TNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGEW 166
Cdd:cd05008    80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALAL 125
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 5-337 2.76e-31

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 124.09  E-value: 2.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904   5 MRREIDEIPEAA-----ARLLdRSATALAAAGAALRAKDpaFLVTIAR---------GSSDHAALFLKYAIELQAGRPVA 70
Cdd:PLN02981  318 MQKEIHEQPESLtttmrGRLI-RGGSGKAKRVLLGGLKD--HLKTIRRsrrivfigcGTSYNAALAARPILEELSGVPVT 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  71 SlgpSLAS--------IYGAElklggaAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGP 142
Cdd:PLN02981  395 M---ELASdlldrqgpIYRED------TAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGA 465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 143 ELAVAATKSYVNSIVA----GLAvLGEWTGDAGLKR-----AVADLPNQFAKAVKLNWQ--DFAADLGEVESLYVLGRGP 211
Cdd:PLN02981  466 EIGVASTKAYTSQIVAmtmlALA-LGEDSISSRSRReaiidGLFDLPNKVREVLKLDQEmkELAELLIDEQSLLVFGRGY 544

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 212 ALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAA---EASVTE--IADG-----MSAKGAVVH 281
Cdd:PLN02981  545 NYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACfskQQSVIQqlRARKgrlivICSKGDASS 624

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1240630904 282 ATSARAQKAKRLPFVETG-HPITDALALILPFYGFveawSRSRGLNPDAPASL-KKVT 337
Cdd:PLN02981  625 VCPSGGCRVIEVPQVEDClQPVINIVPLQLLAYHL----TVLRGHNVDQPRNLaKSVT 678
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 42-337 1.08e-29

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 119.36  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  42 LVTIARGSSDHAALFLKYAIE-LQAGRPVASLGPSLASIYGAELKLGGAaaIAISQSGKSPDIVAMAEAATRAGAVSIAL 120
Cdd:PTZ00295  325 LILVGCGTSYYAALFAASIMQkLKCFNTVQVIDASELTLYRLPDEDAGV--IFISQSGETLDVVRALNLADELNLPKISV 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 121 TNTLPSPIAEACSHPLDILAGPELAVAATKSYvNSIVAGLAVLGEW-----------TGDAGLKRAVADLPNQFAKAVKL 189
Cdd:PTZ00295  403 VNTVGSLIARSTDCGVYLNAGREVAVASTKAF-TSQVTVLSLIALWfaqnkeyscsnYKCSSLINSLHRLPTYIGMTLKS 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 190 N---WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGAR--FPVLVLAARDAAEA 264
Cdd:PTZ00295  482 CeeqCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKE 561

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1240630904 265 SVTEIADGMSAKGAVVHATSARAQKAK----RLPFVETGHPITDALALIlPFYGFVEAWSRSRGLNPDAPASLKK-VT 337
Cdd:PTZ00295  562 LMINAAEQVKARGAYIIVITDDEDLVKdfadEIILIPSNGPLTALLAVI-PLQLLAYEIAILRGINPDKPRGLAKtVT 638
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 92-335 9.44e-22

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 96.10  E-value: 9.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGEWTGD-- 169
Cdd:PTZ00394  406 FFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDsv 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 170 ------AGLKRAVADLPNQFAKAVKLN---WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVL 240
Cdd:PTZ00394  486 rlqerrNEIIRGLAELPAAISECLKIThdpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELK 565

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 241 HGPVALVGARFPVLVLAARDAA-EASVTEIADGMSAKGAVV-HATSARAQ-KAKRLPFVETGHpITDALALI---LPFYG 314
Cdd:PTZ00394  566 HGPLALIDETSPVLAMCTHDKHfGLSKSAVQQVKARGGAVVvFATEVDAElKAAASEIVLVPK-TVDCLQCVvnvIPFQL 644

                         250       260
                  ....*....|....*....|.
gi 1240630904 315 FVEAWSRSRGLNPDAPASLKK 335
Cdd:PTZ00394  645 LAYYMALLRGNNVDCPRNLAK 665
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 42-163 1.11e-12

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 64.24  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  42 LVTIARGSSDHAALFLKYAIELQAGRPVASlgpslasIYGAELKLGGAA-------AIAISQSGKSPDIVAMAEAATRAG 114
Cdd:pfam01380   8 IFVIGRGTSYAIALELALKFEEIGYKVVEV-------ELASELRHGVLAlvdeddlVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1240630904 115 AVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVL 163
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALA 129
frlB PRK11382
fructoselysine 6-phosphate deglycase;
90-262 2.90e-08

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 54.62  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  90 AAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGP--ELAVAATKSYVNSIVAGLAVLGEWt 167
Cdd:PRK11382   95 AVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNAEI- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 168 gdAGLKRAVADLPNQFAKAVKlNWQDFAADLGEVES----LYVLGRGPALAIA-SEAALKFKETSGMHAEAYSAAEVLHG 242
Cdd:PRK11382  174 --GKIKNDLKQLPNALGHLVR-TWEEKGRQLGELASqwpmIYTVAAGPLRPLGyKEGIVTLMEFTWTHGCVIESGEFRHG 250

                         170       180
                  ....*....|....*....|
gi 1240630904 243 PVALVGARFPVLVLAARDAA 262
Cdd:PRK11382  251 PLEIVEPGVPFLFLLGNDES 270
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 45-163 3.60e-08

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: 51.85  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  45 IARGSSDHAALFLKYAIeLQAGRPV-ASLGPSLASIYGAELKlGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNT 123
Cdd:cd05013    19 FGVGSSGLVAEYLAYKL-LRLGKPVvLLSDPHLQLMSAANLT-PGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDS 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1240630904 124 LPSPIAEACSHPLDILAGPELavaATKSYVNSIVAGLAVL 163
Cdd:cd05013    97 ANSPLAKLADIVLLVSSEEGD---FRSSAFSSRIAQLALI 133
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 45-163 1.35e-07

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 52.24  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  45 IARGSSDHAALFLKYAIeLQAGRPVASLGPSLASIYGAELKLG-GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNT 123
Cdd:COG1737   140 FGVGASAPVAEDLAYKL-LRLGKNVVLLDGDGHLQAESAALLGpGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDS 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1240630904 124 LPSPIAEACSHPLDIlagPELAVAATKSYVNSIVAGLAVL 163
Cdd:COG1737   219 PLSPLAKLADVVLYV---PSEEPTLRSSAFSSRVAQLALI 255
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 203-260 2.71e-07

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 48.83  E-value: 2.71e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1240630904 203 SLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARD 260
Cdd:pfam01380   7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSG 64
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
88-141 2.11e-05

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 45.46  E-value: 2.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1240630904  88 GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAG 141
Cdd:PRK15482  183 GDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSG 236
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 92-144 2.39e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 42.46  E-value: 2.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1240630904  92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPEL 144
Cdd:PRK05441  136 VGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEV 188
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
88-130 2.77e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 42.05  E-value: 2.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1240630904  88 GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAE 130
Cdd:PRK11337  188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAK 230
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 92-162 3.01e-04

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: 41.74  E-value: 3.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1240630904  92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPEL--------AVAATKSYVNSIVAGLAV 162
Cdd:cd05007   123 IGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVvagstrlkAGTAQKLALNMLSTAVMI 201
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 91-134 4.37e-04

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: 39.48  E-value: 4.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1240630904  91 AIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSH 134
Cdd:cd05710    51 VILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADY 94
SIS_AgaS_like cd05010
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ...
 207-330 2.19e-03

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


Pssm-ID: 240143 [Multi-domain]  Cd Length: 151  Bit Score: 37.99  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 207 LGRGPALAIASEAALKFKE-TSG-MHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEAS-----VTEI-ADGMSAKGA 278
Cdd:cd05010     4 LGSGPLAGLAREAALKVLElTAGkVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQydldlLKELrRDGIAARVI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1240630904 279 VVHATSARAQKAKRLPFVETGHPITDAlALILPFYGFVE----AWSRSRGLNPDAP 330
Cdd:cd05010    84 AISPESDAGIEDNSHYYLPGSRDLDDV-YLAFPYILYAQlfalFNSIALGLTPDNP 138
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 92-170 2.47e-03

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


Pssm-ID: 440557 [Multi-domain]  Cd Length: 317  Bit Score: 39.19  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904  92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPE---LAVAATksyvNSIVAGLAVlgewtG 168
Cdd:COG0794    96 IAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREacpLNLAPT----TSTTATLAL-----G 166


                  ..
gi 1240630904 169 DA 170
Cdd:COG0794   167 DA 168
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 88-138 3.40e-03

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 37.91  E-value: 3.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1240630904  88 GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDI 138
Cdd:PRK13937  107 GDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLIV 157
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 92-130 6.25e-03

Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.


Pssm-ID: 240138 [Multi-domain]  Cd Length: 179  Bit Score: 37.17  E-value: 6.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1240630904  92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAE 130
Cdd:cd05005    80 IAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAK 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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