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Conserved domains on  [gi|1386706836|gb|AWH38901|]
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tagatose-6-phosphate ketose isomerase [Stenotrophomonas sp. ZAC14D1_NAIMI4_6]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
agaS_fam super family cl31250
putative sugar isomerase, AgaS family; Some members of this protein family are found in ...
20-382 5.80e-131

putative sugar isomerase, AgaS family; Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases.


The actual alignment was detected with superfamily member TIGR02815:

Pssm-ID: 131862 [Multi-domain]  Cd Length: 372  Bit Score: 380.30  E-value: 5.80e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  20 TATEIAQQPALWEALAQDLSRARDRLQAFLGDSLNDPNQRVLFTGAGSSGFIAEMVADAINAQWPAEVRVVHTTSLLTHP 99
Cdd:TIGR02815   5 TAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGLNVSAVPTTDLVSNP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 100 ALYLQRDRPTLLVSFGRSGSSPESVAAVDRVRADVADARFLDITCNADGELARRGAGRSDTFTLLMPSASCDRAFAMTSS 179
Cdd:TIGR02815  85 RQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRSFAMTSS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 180 LTCMLLAALTMFDRSPWEARSARLKQIAALGREGLAQWDAPVAALAQRPFNRVIYLASGPLEALARECALKVLELTAGRV 259
Cdd:TIGR02815 165 FSCMTLATLAVLGPETIESQTEERFADAALCILESGQWDFSEGVLGYAPWERIVYLGSGGLQGLARESALKVLELTAGKV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 260 LALANTPLGFRHGPKSTLDGDTLVVVLRSVQPLARRYEQDLLEELRRDGVAGQVLAIGPHADIGADDEYTLTVPAL---D 336
Cdd:TIGR02815 245 MAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPSrhfI 324
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1386706836 337 DPWLAPVWLGFAQLFALQRSAALGLTPDNPFPDGTVNRVVQGVTIH 382
Cdd:TIGR02815 325 DVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIH 370
 
Name Accession Description Interval E-value
agaS_fam TIGR02815
putative sugar isomerase, AgaS family; Some members of this protein family are found in ...
20-382 5.80e-131

putative sugar isomerase, AgaS family; Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases.


Pssm-ID: 131862 [Multi-domain]  Cd Length: 372  Bit Score: 380.30  E-value: 5.80e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  20 TATEIAQQPALWEALAQDLSRARDRLQAFLGDSLNDPNQRVLFTGAGSSGFIAEMVADAINAQWPAEVRVVHTTSLLTHP 99
Cdd:TIGR02815   5 TAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGLNVSAVPTTDLVSNP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 100 ALYLQRDRPTLLVSFGRSGSSPESVAAVDRVRADVADARFLDITCNADGELARRGAGRSDTFTLLMPSASCDRAFAMTSS 179
Cdd:TIGR02815  85 RQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRSFAMTSS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 180 LTCMLLAALTMFDRSPWEARSARLKQIAALGREGLAQWDAPVAALAQRPFNRVIYLASGPLEALARECALKVLELTAGRV 259
Cdd:TIGR02815 165 FSCMTLATLAVLGPETIESQTEERFADAALCILESGQWDFSEGVLGYAPWERIVYLGSGGLQGLARESALKVLELTAGKV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 260 LALANTPLGFRHGPKSTLDGDTLVVVLRSVQPLARRYEQDLLEELRRDGVAGQVLAIGPHADIGADDEYTLTVPAL---D 336
Cdd:TIGR02815 245 MAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPSrhfI 324
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1386706836 337 DPWLAPVWLGFAQLFALQRSAALGLTPDNPFPDGTVNRVVQGVTIH 382
Cdd:TIGR02815 325 DVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIH 370
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
21-379 9.84e-94

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: 284.10  E-value: 9.84e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  21 ATEIAQQPALWEALaqdLSRARDRLQAFLGDSLNDPNQRVLFTGAGSSGFIAEMVADAINAQWPAEVRVVHTTSLLTHPA 100
Cdd:COG2222     1 AREIAQQPEAWRRA---LAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 101 lYLqRDRPTLLVSFGRSGSSPESVAAVDRVRAdvADARFLDITCNADGELARRGAGrsdtfTLLMPsASCDRAFAMTSSL 180
Cdd:COG2222    78 -YL-KLEGTLVVAISRSGNSPEVVAALELAKA--RGARTLAITNNPDSPLAEAADR-----VLPLP-AGPEKSVAATKSF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 181 TCMLLAALTMFD-RSPWEARSARLKQIAALGREGLAQWDAPVAALAQRPFNRVIYLASGPLEALARECALKVLELTAGRv 259
Cdd:COG2222   148 TTMLLALLALLAaWGGDDALLAALDALPAALEAALAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELSAGH- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 260 lALANTPLGFRHGPKSTLDGDTLVVVLRSVQPlARRYEQDLLEELRRDGvaGQVLAIGPhadiGADDEYTL-TVPALDDP 338
Cdd:COG2222   227 -AEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRALG--ARVVAIGA----EDDAAITLpAIPDLHDA 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1386706836 339 WLAPVWLGFAQLFALQRSAALGLTPDNPFPdgtVNRVVQGV 379
Cdd:COG2222   299 LDPLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
SIS_AgaS_like cd05010
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ...
232-379 4.08e-80

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: 242.53  E-value: 4.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 232 VIYLASGPLEALARECALKVLELTAGRVLALANTPLGFRHGPKSTLDGDTLVVVLRSVQPLARRYEQDLLEELRRDGVAG 311
Cdd:cd05010     1 VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386706836 312 QVLAIGPHADIGADDEYTLTVPA---LDDPWLAPVWLGFAQLFALQRSAALGLTPDNPFPDGTVNRVVQGV 379
Cdd:cd05010    81 RVIAISPESDAGIEDNSHYYLPGsrdLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
59-188 2.75e-05

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: 43.44  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  59 RVLFTGAGSSGFIAEMVADAInAQWPAEVRVVHTTSLLTH-PALYLQRDRPTLLVSFgrSGSSPESVAAVDRVRADVADA 137
Cdd:pfam01380   7 RIFVIGRGTSYAIALELALKF-EEIGYKVVEVELASELRHgVLALVDEDDLVIAISY--SGETKDLLAAAELAKARGAKI 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1386706836 138 rfLDITCNADGELARrgagRSD-TFTLLMPSASCdRAFAMTSSLTCMLLAAL 188
Cdd:pfam01380  84 --IAITDSPGSPLAR----EADhVLYINAGPETG-VASTKSITAQLAALDAL 128
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
55-245 4.94e-05

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 44.97  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  55 DPNQRVLFTGAGSSGFIAEMVADAINAQWPAEVRVVHTTSLlthPALylqRDRPTLLVSFGRSGSSPESVAAVDRVRAdv 134
Cdd:PRK08674   32 EKIDNIVISGMGGSGIGGDLLRILLFDELKVPVFVNRDYTL---PAF---VDEKTLVIAVSYSGNTEETLSAVEQALK-- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 135 ADARFLDITcnADGELARRGAGRSdTFTLLMPSASCDRAfamtsSLTCMLLAALTMFDRSPW--------EARSARLKQI 206
Cdd:PRK08674  104 RGAKIIAIT--SGGKLKEMAKEHG-LPVIIVPGGYQPRA-----ALGYLFTPLLKILEKLGLipdksaevLETKIVLSEL 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1386706836 207 AALGREGLAQWDAPVAALAQRPFNR--VIYlASGPLEALAR 245
Cdd:PRK08674  176 AEGLKEKVPTLKNLAKRLAGKLYGRipVIY-GSGLTLAVAY 215
 
Name Accession Description Interval E-value
agaS_fam TIGR02815
putative sugar isomerase, AgaS family; Some members of this protein family are found in ...
20-382 5.80e-131

putative sugar isomerase, AgaS family; Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases.


Pssm-ID: 131862 [Multi-domain]  Cd Length: 372  Bit Score: 380.30  E-value: 5.80e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  20 TATEIAQQPALWEALAQDLSRARDRLQAFLGDSLNDPNQRVLFTGAGSSGFIAEMVADAINAQWPAEVRVVHTTSLLTHP 99
Cdd:TIGR02815   5 TAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGLNVSAVPTTDLVSNP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 100 ALYLQRDRPTLLVSFGRSGSSPESVAAVDRVRADVADARFLDITCNADGELARRGAGRSDTFTLLMPSASCDRAFAMTSS 179
Cdd:TIGR02815  85 RQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRSFAMTSS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 180 LTCMLLAALTMFDRSPWEARSARLKQIAALGREGLAQWDAPVAALAQRPFNRVIYLASGPLEALARECALKVLELTAGRV 259
Cdd:TIGR02815 165 FSCMTLATLAVLGPETIESQTEERFADAALCILESGQWDFSEGVLGYAPWERIVYLGSGGLQGLARESALKVLELTAGKV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 260 LALANTPLGFRHGPKSTLDGDTLVVVLRSVQPLARRYEQDLLEELRRDGVAGQVLAIGPHADIGADDEYTLTVPAL---D 336
Cdd:TIGR02815 245 MAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPSrhfI 324
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1386706836 337 DPWLAPVWLGFAQLFALQRSAALGLTPDNPFPDGTVNRVVQGVTIH 382
Cdd:TIGR02815 325 DVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIH 370
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
21-379 9.84e-94

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: 284.10  E-value: 9.84e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  21 ATEIAQQPALWEALaqdLSRARDRLQAFLGDSLNDPNQRVLFTGAGSSGFIAEMVADAINAQWPAEVRVVHTTSLLTHPA 100
Cdd:COG2222     1 AREIAQQPEAWRRA---LAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 101 lYLqRDRPTLLVSFGRSGSSPESVAAVDRVRAdvADARFLDITCNADGELARRGAGrsdtfTLLMPsASCDRAFAMTSSL 180
Cdd:COG2222    78 -YL-KLEGTLVVAISRSGNSPEVVAALELAKA--RGARTLAITNNPDSPLAEAADR-----VLPLP-AGPEKSVAATKSF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 181 TCMLLAALTMFD-RSPWEARSARLKQIAALGREGLAQWDAPVAALAQRPFNRVIYLASGPLEALARECALKVLELTAGRv 259
Cdd:COG2222   148 TTMLLALLALLAaWGGDDALLAALDALPAALEAALAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELSAGH- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 260 lALANTPLGFRHGPKSTLDGDTLVVVLRSVQPlARRYEQDLLEELRRDGvaGQVLAIGPhadiGADDEYTL-TVPALDDP 338
Cdd:COG2222   227 -AEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRALG--ARVVAIGA----EDDAAITLpAIPDLHDA 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1386706836 339 WLAPVWLGFAQLFALQRSAALGLTPDNPFPdgtVNRVVQGV 379
Cdd:COG2222   299 LDPLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
SIS_AgaS_like cd05010
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ...
232-379 4.08e-80

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: 242.53  E-value: 4.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 232 VIYLASGPLEALARECALKVLELTAGRVLALANTPLGFRHGPKSTLDGDTLVVVLRSVQPLARRYEQDLLEELRRDGVAG 311
Cdd:cd05010     1 VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386706836 312 QVLAIGPHADIGADDEYTLTVPA---LDDPWLAPVWLGFAQLFALQRSAALGLTPDNPFPDGTVNRVVQGV 379
Cdd:cd05010    81 RVIAISPESDAGIEDNSHYYLPGsrdLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
59-191 3.02e-20

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: 85.63  E-value: 3.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  59 RVLFTGAGSSGFIAEMVADAINAQWPAEVRVVhttslLTHPALYLQ--RDRPTLLVSFGRSGSSPESVAAVDRVRADVAd 136
Cdd:cd05008     1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVE-----AASEFRYRRplLDEDTLVIAISQSGETADTLAALRLAKEKGA- 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1386706836 137 arFLDITCNADGELARRGAGRSdTFTLLMPSASCDRAFAMTSSLTCMLLAALTMF 191
Cdd:cd05008    75 --KTVAITNVVGSTLAREADYV-LYLRAGPEISVAATKAFTSQLLALLLLALALA 126
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
221-366 1.41e-15

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: 73.45  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 221 VAALAQR--PFNRVIYLASGPLEALARECALKVLELTagRVLALAnTPLG-FRHGPKSTLDGDTLVVVLRSVQPLARRYE 297
Cdd:cd05009     3 IKELAEKlkEAKSFYVLGRGPNYGTALEGALKLKETS--YIHAEA-YSAGeFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386706836 298 QdLLEELRRDGvaGQVLAIGPHADIGADDEYTLTVPALDDPWLAPVWLGFAQLFALQRSAALGLTPDNP 366
Cdd:cd05009    80 S-LIKEVKARG--AKVIVITDDGDAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKP 145
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
59-190 9.12e-06

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: 44.84  E-value: 9.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  59 RVLFTGAGSSGFIAEmvadainaqwpaevRVVHTTSLLTHPALYL-------------QRDRPTLLVSfgRSGSSPESVA 125
Cdd:cd05014     2 KVVVTGVGKSGHIAR--------------KIAATLSSTGTPAFFLhptealhgdlgmvTPGDVVIAIS--NSGETDELLN 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386706836 126 AVDRVRAdvADARFLDITCNADGELARrgagRSDtFTLLMPSAS--CDRAFAMTSSLTCMLLA--ALTM 190
Cdd:cd05014    66 LLPHLKR--RGAPIIAITGNPNSTLAK----LSD-VVLDLPVEEeaCPLGLAPTTSTTAMLALgdALAV 127
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
59-188 2.75e-05

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: 43.44  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  59 RVLFTGAGSSGFIAEMVADAInAQWPAEVRVVHTTSLLTH-PALYLQRDRPTLLVSFgrSGSSPESVAAVDRVRADVADA 137
Cdd:pfam01380   7 RIFVIGRGTSYAIALELALKF-EEIGYKVVEVELASELRHgVLALVDEDDLVIAISY--SGETKDLLAAAELAKARGAKI 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1386706836 138 rfLDITCNADGELARrgagRSD-TFTLLMPSASCdRAFAMTSSLTCMLLAAL 188
Cdd:pfam01380  84 --IAITDSPGSPLAR----EADhVLYINAGPETG-VASTKSITAQLAALDAL 128
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
55-245 4.94e-05

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 44.97  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836  55 DPNQRVLFTGAGSSGFIAEMVADAINAQWPAEVRVVHTTSLlthPALylqRDRPTLLVSFGRSGSSPESVAAVDRVRAdv 134
Cdd:PRK08674   32 EKIDNIVISGMGGSGIGGDLLRILLFDELKVPVFVNRDYTL---PAF---VDEKTLVIAVSYSGNTEETLSAVEQALK-- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 135 ADARFLDITcnADGELARRGAGRSdTFTLLMPSASCDRAfamtsSLTCMLLAALTMFDRSPW--------EARSARLKQI 206
Cdd:PRK08674  104 RGAKIIAIT--SGGKLKEMAKEHG-LPVIIVPGGYQPRA-----ALGYLFTPLLKILEKLGLipdksaevLETKIVLSEL 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1386706836 207 AALGREGLAQWDAPVAALAQRPFNR--VIYlASGPLEALAR 245
Cdd:PRK08674  176 AEGLKEKVPTLKNLAKRLAGKLYGRipVIY-GSGLTLAVAY 215
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
230-353 8.60e-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. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 39.20  E-value: 8.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386706836 230 NRVIYLASGPLEALARECALKVLELtaGRVLALANTPLGFRHGPKSTLDGDTLVVVLrSVQPLARRYeQDLLEELRRDGV 309
Cdd:pfam01380   6 KRIFVIGRGTSYAIALELALKFEEI--GYKVVEVELASELRHGVLALVDEDDLVIAI-SYSGETKDL-LAAAELAKARGA 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1386706836 310 AGQVLAIGPHADIGADDEYTLTVPALDDPWLAPVWLGFAQLFAL 353
Cdd:pfam01380  82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAAL 125
 
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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