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Conserved domains on  [gi|1731571511|gb|TYK95433|]
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SIS domain-containing protein [Streptococcus dysgalactiae]

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 ...
17-389 7.15e-144

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: 413.42  E-value: 7.15e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  17 TTKEIKQQPALWQETMTSFDITKEALVSFLKAVYESANgnrVRVIFTGAGTSEYVGNTICPYLNKVGNRQryfFDSIAST 96
Cdd:TIGR02815   5 TAREIRQQPALWRRLLTIIQALRPALNAFLEPLLAREN---LRIVLTGAGTSAFIGDALAPWLASHTGLN---VSAVPTT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  97 DLVAAPEYYLAEEETVLLVSFARSGNSPESVAAVNLINQLVPNSYHLIITCAKDGELAKKAQQDDHSFLYLMPEAANDAG 176
Cdd:TIGR02815  79 DLVSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 177 FAMTGSFTCMMLAALLIFDDATDLSQKQSYVADmvfAGQAILDQE---ERLQELADLGFERLVYLGSASLANLTQEAQLK 253
Cdd:TIGR02815 159 FAMTSSFSCMTLATLAVLGPETIESQTEERFAD---AALCILESGqwdFSEGVLGYAPWERIVYLGSGGLQGLARESALK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 254 MLELTAGQVATVYESSMGFRHGPKSFINMDTLVIGFVNSDPYVRQYDLEILEEVRADGIALKTLALL-QKGPTNFSGDQF 332
Cdd:TIGR02815 236 VLELTAGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISaESSDIVAAGDHF 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1731571511 333 LLEASQLLPDAYLAFPMILVAQMLALLTAITVGNRPDTPSATGTVNRVVKGVTIHPY 389
Cdd:TIGR02815 316 ILPPSRHFIDVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
 
Name Accession Description Interval E-value
agaS_fam TIGR02815
putative sugar isomerase, AgaS family; Some members of this protein family are found in ...
17-389 7.15e-144

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: 413.42  E-value: 7.15e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  17 TTKEIKQQPALWQETMTSFDITKEALVSFLKAVYESANgnrVRVIFTGAGTSEYVGNTICPYLNKVGNRQryfFDSIAST 96
Cdd:TIGR02815   5 TAREIRQQPALWRRLLTIIQALRPALNAFLEPLLAREN---LRIVLTGAGTSAFIGDALAPWLASHTGLN---VSAVPTT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  97 DLVAAPEYYLAEEETVLLVSFARSGNSPESVAAVNLINQLVPNSYHLIITCAKDGELAKKAQQDDHSFLYLMPEAANDAG 176
Cdd:TIGR02815  79 DLVSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 177 FAMTGSFTCMMLAALLIFDDATDLSQKQSYVADmvfAGQAILDQE---ERLQELADLGFERLVYLGSASLANLTQEAQLK 253
Cdd:TIGR02815 159 FAMTSSFSCMTLATLAVLGPETIESQTEERFAD---AALCILESGqwdFSEGVLGYAPWERIVYLGSGGLQGLARESALK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 254 MLELTAGQVATVYESSMGFRHGPKSFINMDTLVIGFVNSDPYVRQYDLEILEEVRADGIALKTLALL-QKGPTNFSGDQF 332
Cdd:TIGR02815 236 VLELTAGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISaESSDIVAAGDHF 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1731571511 333 LLEASQLLPDAYLAFPMILVAQMLALLTAITVGNRPDTPSATGTVNRVVKGVTIHPY 389
Cdd:TIGR02815 316 ILPPSRHFIDVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
19-384 1.17e-97

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: 294.11  E-value: 1.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  19 KEIKQQPALWQETmtsFDITKEALVSFLKAVYESANGnrvRVIFTGAGTSEYVGNTICPYLNKVGNRqryFFDSIASTDL 98
Cdd:COG2222     2 REIAQQPEAWRRA---LAALAAAIAALLARLRAKPPR---RVVLVGAGSSDHAAQAAAYLLERLLGI---PVAALAPSEL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  99 VAAPEYYLaeEETVLLVSFARSGNSPESVAAVNLINQLvpNSYHLIITCAKDGELAKKAQQddhsfLYLMPeAANDAGFA 178
Cdd:COG2222    73 VVYPAYLK--LEGTLVVAISRSGNSPEVVAALELAKAR--GARTLAITNNPDSPLAEAADR-----VLPLP-AGPEKSVA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 179 MTGSFTCMMLAALLIFDDATDLSQKQSYVADMVFAGQAILDQ-EERLQELADLGFERLVYLGSASLANLTQEAQLKMLEL 257
Cdd:COG2222   143 ATKSFTTMLLALLALLAAWGGDDALLAALDALPAALEAALAAdWPAAALAALADAERVVFLGRGPLYGLAREAALKLKEL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 258 TAGQvaTVYESSMGFRHGPKSFINMDTLVIGFVNSDPyVRQYDLEILEEVRADGiaLKTLALLQKGPTNFSgdqflLEAS 337
Cdd:COG2222   223 SAGH--AEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRALG--ARVVAIGAEDDAAIT-----LPAI 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1731571511 338 QLLPDAYLAFPMILVAQMLALLTAITVGNRPDTPSAtgtVNRVVKGV 384
Cdd:COG2222   293 PDLHDALDPLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
SIS_AgaS_like cd05010
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ...
236-384 8.50e-75

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: 229.05  E-value: 8.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 236 VYLGSASLANLTQEAQLKMLELTAGQVATVYESSMGFRHGPKSFINMDTLVIGFVNSDPYVRQYDLEILEEVRADGIALK 315
Cdd:cd05010     2 VYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAAR 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 316 TLALLQKGPTNFSGDQFL-LEASQLLPDAYLAFPMILVAQMLALLTAITVGNRPDTPSATGTVNRVVKGV 384
Cdd:cd05010    82 VIAISPESDAGIEDNSHYyLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
17-371 7.66e-09

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 57.34  E-value: 7.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  17 TTKEIKQQPALWQETMTS----FDITKEALVSFLKAVYESANgNRVRVIFTGAGTSEYVGNTICPYLNKVGNrqryfFDS 92
Cdd:PTZ00295  279 TLKEIFEQPIALSRALNNggrlSGYNNRVKLGGLDQYLEELL-NIKNLILVGCGTSYYAALFAASIMQKLKC-----FNT 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  93 IASTDlvaAPEY----YLAEEETVLLVSfaRSGNSPESVAAVNLINQL------VPNSYH-LIITCAKDGelakkaqqdd 161
Cdd:PTZ00295  353 VQVID---ASELtlyrLPDEDAGVIFIS--QSGETLDVVRALNLADELnlpkisVVNTVGsLIARSTDCG---------- 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 162 hsfLYLmpEAANDAGFAMTGSFT----CMMLAALLIFD--DATDLSQK-QSYVADM----VFAGQAILDQEERLQELAD- 229
Cdd:PTZ00295  418 ---VYL--NAGREVAVASTKAFTsqvtVLSLIALWFAQnkEYSCSNYKcSSLINSLhrlpTYIGMTLKSCEEQCKRIAEk 492
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 230 LGFERLVY-LGSASLANLTQEAQLKMLELTAGQVATVYESSMgfRHGPKSFINMD--TLVIGFVNSDPYvRQYDLEILEE 306
Cdd:PTZ00295  493 LKNAKSMFiLGKGLGYPIALEGALKIKEITYIHAEGFSGGAL--KHGPFALIDKEknTPVILIILDDEH-KELMINAAEQ 569
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731571511 307 VRADGIALKTLALLQKGPTNFSGDQFLLEASQLLpDAYLAfpmILVAQMLALLTAITVGNRPDTP 371
Cdd:PTZ00295  570 VKARGAYIIVITDDEDLVKDFADEIILIPSNGPL-TALLA---VIPLQLLAYEIAILRGINPDKP 630
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
59-193 2.26e-06

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: 46.52  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  59 RVIFTGAGTSEYVGNTICPYLNKVGNRQRYFFDSIASTDLVAAPeyyLAEEETVLLVSFarSGNSPESVAAVNLINQLVP 138
Cdd:pfam01380   7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLAL---VDEDDLVIAISY--SGETKDLLAAAELAKARGA 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1731571511 139 NSyhLIITCAKDGELAKKAqqdDHSfLYLMPEAANDAGFAMTGSFTCMMLAALLI 193
Cdd:pfam01380  82 KI--IAITDSPGSPLAREA---DHV-LYINAGPETGVASTKSITAQLAALDALAV 130
 
Name Accession Description Interval E-value
agaS_fam TIGR02815
putative sugar isomerase, AgaS family; Some members of this protein family are found in ...
17-389 7.15e-144

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: 413.42  E-value: 7.15e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  17 TTKEIKQQPALWQETMTSFDITKEALVSFLKAVYESANgnrVRVIFTGAGTSEYVGNTICPYLNKVGNRQryfFDSIAST 96
Cdd:TIGR02815   5 TAREIRQQPALWRRLLTIIQALRPALNAFLEPLLAREN---LRIVLTGAGTSAFIGDALAPWLASHTGLN---VSAVPTT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  97 DLVAAPEYYLAEEETVLLVSFARSGNSPESVAAVNLINQLVPNSYHLIITCAKDGELAKKAQQDDHSFLYLMPEAANDAG 176
Cdd:TIGR02815  79 DLVSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 177 FAMTGSFTCMMLAALLIFDDATDLSQKQSYVADmvfAGQAILDQE---ERLQELADLGFERLVYLGSASLANLTQEAQLK 253
Cdd:TIGR02815 159 FAMTSSFSCMTLATLAVLGPETIESQTEERFAD---AALCILESGqwdFSEGVLGYAPWERIVYLGSGGLQGLARESALK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 254 MLELTAGQVATVYESSMGFRHGPKSFINMDTLVIGFVNSDPYVRQYDLEILEEVRADGIALKTLALL-QKGPTNFSGDQF 332
Cdd:TIGR02815 236 VLELTAGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISaESSDIVAAGDHF 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1731571511 333 LLEASQLLPDAYLAFPMILVAQMLALLTAITVGNRPDTPSATGTVNRVVKGVTIHPY 389
Cdd:TIGR02815 316 ILPPSRHFIDVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
19-384 1.17e-97

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: 294.11  E-value: 1.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  19 KEIKQQPALWQETmtsFDITKEALVSFLKAVYESANGnrvRVIFTGAGTSEYVGNTICPYLNKVGNRqryFFDSIASTDL 98
Cdd:COG2222     2 REIAQQPEAWRRA---LAALAAAIAALLARLRAKPPR---RVVLVGAGSSDHAAQAAAYLLERLLGI---PVAALAPSEL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  99 VAAPEYYLaeEETVLLVSFARSGNSPESVAAVNLINQLvpNSYHLIITCAKDGELAKKAQQddhsfLYLMPeAANDAGFA 178
Cdd:COG2222    73 VVYPAYLK--LEGTLVVAISRSGNSPEVVAALELAKAR--GARTLAITNNPDSPLAEAADR-----VLPLP-AGPEKSVA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 179 MTGSFTCMMLAALLIFDDATDLSQKQSYVADMVFAGQAILDQ-EERLQELADLGFERLVYLGSASLANLTQEAQLKMLEL 257
Cdd:COG2222   143 ATKSFTTMLLALLALLAAWGGDDALLAALDALPAALEAALAAdWPAAALAALADAERVVFLGRGPLYGLAREAALKLKEL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 258 TAGQvaTVYESSMGFRHGPKSFINMDTLVIGFVNSDPyVRQYDLEILEEVRADGiaLKTLALLQKGPTNFSgdqflLEAS 337
Cdd:COG2222   223 SAGH--AEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRALG--ARVVAIGAEDDAAIT-----LPAI 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1731571511 338 QLLPDAYLAFPMILVAQMLALLTAITVGNRPDTPSAtgtVNRVVKGV 384
Cdd:COG2222   293 PDLHDALDPLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
SIS_AgaS_like cd05010
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ...
236-384 8.50e-75

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: 229.05  E-value: 8.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 236 VYLGSASLANLTQEAQLKMLELTAGQVATVYESSMGFRHGPKSFINMDTLVIGFVNSDPYVRQYDLEILEEVRADGIALK 315
Cdd:cd05010     2 VYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAAR 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 316 TLALLQKGPTNFSGDQFL-LEASQLLPDAYLAFPMILVAQMLALLTAITVGNRPDTPSATGTVNRVVKGV 384
Cdd:cd05010    82 VIAISPESDAGIEDNSHYyLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
59-194 1.18e-24

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: 97.57  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  59 RVIFTGAGTSEYVGNTICPYLNKVGNRqryffdsiaSTDLVAAPEYYLAE---EETVLLVSFARSGNSPESVAAVNLINQ 135
Cdd:cd05008     1 RILIVGCGTSYHAALVAKYLLERLAGI---------PVEVEAASEFRYRRpllDEDTLVIAISQSGETADTLAALRLAKE 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1731571511 136 LVPnsYHLIITCAKDGELAKKAqqDDHSFLYLMPEAANDAGFAMTGSFTCMMLAALLIF 194
Cdd:cd05008    72 KGA--KTVAITNVVGSTLAREA--DYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
222-371 5.01e-10

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: 57.66  E-value: 5.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 222 ERLQELADL--GFERLVYLGS-ASLAnLTQEAQLKMLElTAGQVATVYeSSMGFRHGPKSFINMDTLVIGFVNSDPyVRQ 298
Cdd:cd05009     1 EDIKELAEKlkEAKSFYVLGRgPNYG-TALEGALKLKE-TSYIHAEAY-SAGEFKHGPIALVDEGTPVIFLAPEDR-LEE 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731571511 299 YDLEILEEVRADGiaLKTLALLQKGPTNFSGDQFLLeasqlLP---DAYLAFPMILVAQMLALLTAITVGNRPDTP 371
Cdd:cd05009    77 KLESLIKEVKARG--AKVIVITDDGDAKDLADVVIR-----VPatvEELSPLLYIVPLQLLAYHLAVARGIDPDKP 145
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
17-371 7.66e-09

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 57.34  E-value: 7.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  17 TTKEIKQQPALWQETMTS----FDITKEALVSFLKAVYESANgNRVRVIFTGAGTSEYVGNTICPYLNKVGNrqryfFDS 92
Cdd:PTZ00295  279 TLKEIFEQPIALSRALNNggrlSGYNNRVKLGGLDQYLEELL-NIKNLILVGCGTSYYAALFAASIMQKLKC-----FNT 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  93 IASTDlvaAPEY----YLAEEETVLLVSfaRSGNSPESVAAVNLINQL------VPNSYH-LIITCAKDGelakkaqqdd 161
Cdd:PTZ00295  353 VQVID---ASELtlyrLPDEDAGVIFIS--QSGETLDVVRALNLADELnlpkisVVNTVGsLIARSTDCG---------- 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 162 hsfLYLmpEAANDAGFAMTGSFT----CMMLAALLIFD--DATDLSQK-QSYVADM----VFAGQAILDQEERLQELAD- 229
Cdd:PTZ00295  418 ---VYL--NAGREVAVASTKAFTsqvtVLSLIALWFAQnkEYSCSNYKcSSLINSLhrlpTYIGMTLKSCEEQCKRIAEk 492
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 230 LGFERLVY-LGSASLANLTQEAQLKMLELTAGQVATVYESSMgfRHGPKSFINMD--TLVIGFVNSDPYvRQYDLEILEE 306
Cdd:PTZ00295  493 LKNAKSMFiLGKGLGYPIALEGALKIKEITYIHAEGFSGGAL--KHGPFALIDKEknTPVILIILDDEH-KELMINAAEQ 569
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731571511 307 VRADGIALKTLALLQKGPTNFSGDQFLLEASQLLpDAYLAfpmILVAQMLALLTAITVGNRPDTP 371
Cdd:PTZ00295  570 VKARGAYIIVITDDEDLVKDFADEIILIPSNGPL-TALLA---VIPLQLLAYEIAILRGINPDKP 630
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
59-193 2.26e-06

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: 46.52  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  59 RVIFTGAGTSEYVGNTICPYLNKVGNRQRYFFDSIASTDLVAAPeyyLAEEETVLLVSFarSGNSPESVAAVNLINQLVP 138
Cdd:pfam01380   7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLAL---VDEDDLVIAISY--SGETKDLLAAAELAKARGA 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1731571511 139 NSyhLIITCAKDGELAKKAqqdDHSfLYLMPEAANDAGFAMTGSFTCMMLAALLI 193
Cdd:pfam01380  82 KI--IAITDSPGSPLAREA---DHV-LYINAGPETGVASTKSITAQLAALDALAV 130
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
59-187 1.93e-05

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: 43.69  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511  59 RVIFTGAGTSEYVGNTICPYLNKVGNRQrYFFDSI--ASTDLVAapeyyLAEEETVLLVSfaRSGNSPESvaaVNLINQL 136
Cdd:cd05014     2 KVVVTGVGKSGHIARKIAATLSSTGTPA-FFLHPTeaLHGDLGM-----VTPGDVVIAIS--NSGETDEL---LNLLPHL 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1731571511 137 VPNSYHLI-ITCAKDGELAKKAqqdDHSFLYLMPEAANDAGFAMTGSFTCMM 187
Cdd:cd05014    71 KRRGAPIIaITGNPNSTLAKLS---DVVLDLPVEEEACPLGLAPTTSTTAML 119
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
234-363 8.17e-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: 8.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731571511 234 RLVYLGSASLANLTQEAQLKMLELTaGQVATVYESSmGFRHGPKSFINMDTLVIGFVNSDpYVRQYdLEILEEVRADGIa 313
Cdd:pfam01380   7 RIFVIGRGTSYAIALELALKFEEIG-YKVVEVELAS-ELRHGVLALVDEDDLVIAISYSG-ETKDL-LAAAELAKARGA- 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1731571511 314 lKTLALlqkgpTNFSGDQFLLEASQLL-----PDAYLAFPMILVAQMLALLTAIT 363
Cdd:pfam01380  82 -KIIAI-----TDSPGSPLAREADHVLyinagPETGVASTKSITAQLAALDALAV 130
 
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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