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Conserved domains on  [gi|1469305103|ref|WP_117646616|]
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MULTISPECIES: SIS domain-containing protein [unclassified Collinsella]

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
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 27-149 1.55e-44

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: 148.49  E-value: 1.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  27 SVAFVGCGASMSDLYPAKYFLANNTdKLNVQIFTANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVS 106
Cdd:cd05710     1 NVFFVGCGGSLADMYPAKYFLKKES-KLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1469305103 107 LTNKAGSALTVDADHVIVHGFHANyaAKCEKPGYAIALALEIL 149
Cdd:cd05710    80 LTDDEDSPLAKLADYVIVYGFEID--AVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 28-324 3.78e-33

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: 125.01  E-value: 3.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  28 VAFVGCGASMSDLYPAKYFLANNTDkLNVQIFTANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVSL 107
Cdd:COG2222    37 VVLVGAGSSDHAAQAAAYLLERLLG-IPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 108 TNKAGSALTVDADHVIVHGFHANYAAKCEKPGYAIALALEILQQTEGYDhyEDMITGLTNVFDLCENAAQhcKKLAKKFA 187
Cdd:COG2222   116 TNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAAWGGD--DALLAALDALPAALEAALA--ADWPAAAL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 188 EDFKDDKMIYFMASGASEKMAYShAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVFFMSDGATRPMDARALTFLE 267
Cdd:COG2222   192 AALADAERVVFLGRGPLYGLARE-AALKLKELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELR 270

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1469305103 268 RMGAKVALIDSKDYGLAD-AVPASVITYFNPLLHLAVMREYGNQIAEARQHPLTMRRY 324
Cdd:COG2222   271 ALGARVVAIGAEDDAAITlPAIPDLHDALDPLLLLVVAQRLALALALARGLDPDTPRH 328
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 27-149 1.55e-44

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: 148.49  E-value: 1.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  27 SVAFVGCGASMSDLYPAKYFLANNTdKLNVQIFTANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVS 106
Cdd:cd05710     1 NVFFVGCGGSLADMYPAKYFLKKES-KLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1469305103 107 LTNKAGSALTVDADHVIVHGFHANyaAKCEKPGYAIALALEIL 149
Cdd:cd05710    80 LTDDEDSPLAKLADYVIVYGFEID--AVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 28-324 3.78e-33

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: 125.01  E-value: 3.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  28 VAFVGCGASMSDLYPAKYFLANNTDkLNVQIFTANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVSL 107
Cdd:COG2222    37 VVLVGAGSSDHAAQAAAYLLERLLG-IPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 108 TNKAGSALTVDADHVIVHGFHANYAAKCEKPGYAIALALEILQQTEGYDhyEDMITGLTNVFDLCENAAQhcKKLAKKFA 187
Cdd:COG2222   116 TNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAAWGGD--DALLAALDALPAALEAALA--ADWPAAAL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 188 EDFKDDKMIYFMASGASEKMAYShAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVFFMSDGATRPMDARALTFLE 267
Cdd:COG2222   192 AALADAERVVFLGRGPLYGLARE-AALKLKELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELR 270

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1469305103 268 RMGAKVALIDSKDYGLAD-AVPASVITYFNPLLHLAVMREYGNQIAEARQHPLTMRRY 324
Cdd:COG2222   271 ALGARVVAIGAEDDAAITlPAIPDLHDALDPLLLLVVAQRLALALALARGLDPDTPRH 328
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 181-327 1.15e-21

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: 89.63  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 181 KLAKKFAEDFKDDKMIYFMASGASEKMAYShAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVFFMSDGATRPMDA 260
Cdd:cd05009     1 EDIKELAEKLKEAKSFYVLGRGPNYGTALE-GALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469305103 261 RALTFLERMGAKVALIDSKDYGLADA-----VPAsVITYFNPLLHLAVMREYGNQIAEAR-QHPLTMRRYMWK 327
Cdd:cd05009    80 SLIKEVKARGAKVIVITDDGDAKDLAdvvirVPA-TVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKS 151
frlB PRK11382
fructoselysine 6-phosphate deglycase;
16-277 4.89e-16

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 77.73  E-value: 4.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  16 VADVLSNHEIHSVAFVGCGASMSDLYPAKYfLANNTDKLNVQIFTANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANK 95
Cdd:PRK11382   35 IVEEMVKRDIDRIYFVACGSPLNAAQTAKH-LADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  96 TAKKHNCPVVSLTNKAGSALTVDADHVIvhgfhaNYAAKCEKPGYAI---ALALEILqqTEGYDHYEdmITGLTNVFDLC 172
Cdd:PRK11382  114 LGRACGALTAAFTKRADSPITSAAEFSI------DYQADCIWEIHLLlcySVVLEMI--TRLAPNAE--IGKIKNDLKQL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 173 ENAAQHCKKL----AKKFAEDFKDDKMIYFMASGASEKMAYSHAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVF 248
Cdd:PRK11382  184 PNALGHLVRTweekGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLF 263

                         250       260
                  ....*....|....*....|....*....
gi 1469305103 249 FMSDGATRPMDARALTFLERMGAKVALID 277
Cdd:PRK11382  264 LLGNDESRHTTERAINFVKQRTDNVIVID 292
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 24-237 8.53e-10

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 59.65  E-value: 8.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  24 EIHSVAFVGCGASmsdlYPAKYFLANNTDKLN----VQIFTANEFN-YDTPswvNEHTFVITCSLGGSTPETVEANKTAK 98
Cdd:PTZ00295  321 NIKNLILVGCGTS----YYAALFAASIMQKLKcfntVQVIDASELTlYRLP---DEDAGVIFISQSGETLDVVRALNLAD 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  99 KHNCPVVSLTNKAGSAL--TVDAdhvivhGFHANY-------AAKC--EKPGYAIALALEILQQTEGY---DHYEDMITG 164
Cdd:PTZ00295  394 ELNLPKISVVNTVGSLIarSTDC------GVYLNAgrevavaSTKAftSQVTVLSLIALWFAQNKEYScsnYKCSSLINS 467

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469305103 165 LTNVFDLCENAAQHCKKLAKKFAEDFKDDKMIYFMASGASEKMAYsHAAFLFTEMQWIDAAAYNTGEYFHGPF 237
Cdd:PTZ00295  468 LHRLPTYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIAL-EGALKIKEITYIHAEGFSGGALKHGPF 539
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 16-124 3.82e-07

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 50.70  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  16 VADVLSNHEihSVAFVGCGASMSdlyPAKYFlannTDKL-----NVQIFTAN-EFNYDTPSWVNEHTFVITCSLGGSTPE 89
Cdd:COG1737   127 AVDLLAKAR--RIYIFGVGASAP---VAEDL----AYKLlrlgkNVVLLDGDgHLQAESAALLGPGDVVIAISFSGYTRE 197

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1469305103  90 TVEANKTAKKHNCPVVSLTNKAGSALTVDADHVIV 124
Cdd:COG1737   198 TLEAARLAKERGAKVIAITDSPLSPLAKLADVVLY 232
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 26-123 3.04e-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: 45.75  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  26 HSVAFVGCGASmsdlYPAKYFLANNTDKLNVQIF---TANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNC 102
Cdd:pfam01380   6 KRIFVIGRGTS----YAIALELALKFEEIGYKVVeveLASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81

                          90       100
                  ....*....|....*....|.
gi 1469305103 103 PVVSLTNKAGSALTVDADHVI 123
Cdd:pfam01380  82 KIIAITDSPGSPLAREADHVL 102
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 194-321 2.53e-03

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: 37.66  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 194 KMIYFMASGASEKMAySHAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVFFMSDGATRPMDaRALTFLERMGAKV 273
Cdd:pfam01380   6 KRIFVIGRGTSYAIA-LELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLL-AAAELAKARGAKI 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1469305103 274 ALIdskdyglADAVPASVITYFNPLLHLAVMREYGNQIAEARQHPLTM 321
Cdd:pfam01380  84 IAI-------TDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAA 124
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 27-149 1.55e-44

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: 148.49  E-value: 1.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  27 SVAFVGCGASMSDLYPAKYFLANNTdKLNVQIFTANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVS 106
Cdd:cd05710     1 NVFFVGCGGSLADMYPAKYFLKKES-KLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1469305103 107 LTNKAGSALTVDADHVIVHGFHANyaAKCEKPGYAIALALEIL 149
Cdd:cd05710    80 LTDDEDSPLAKLADYVIVYGFEID--AVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 28-324 3.78e-33

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: 125.01  E-value: 3.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  28 VAFVGCGASMSDLYPAKYFLANNTDkLNVQIFTANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVSL 107
Cdd:COG2222    37 VVLVGAGSSDHAAQAAAYLLERLLG-IPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 108 TNKAGSALTVDADHVIVHGFHANYAAKCEKPGYAIALALEILQQTEGYDhyEDMITGLTNVFDLCENAAQhcKKLAKKFA 187
Cdd:COG2222   116 TNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAAWGGD--DALLAALDALPAALEAALA--ADWPAAAL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 188 EDFKDDKMIYFMASGASEKMAYShAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVFFMSDGATRPMDARALTFLE 267
Cdd:COG2222   192 AALADAERVVFLGRGPLYGLARE-AALKLKELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELR 270

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1469305103 268 RMGAKVALIDSKDYGLAD-AVPASVITYFNPLLHLAVMREYGNQIAEARQHPLTMRRY 324
Cdd:COG2222   271 ALGARVVAIGAEDDAAITlPAIPDLHDALDPLLLLVVAQRLALALALARGLDPDTPRH 328
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 181-327 1.15e-21

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: 89.63  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 181 KLAKKFAEDFKDDKMIYFMASGASEKMAYShAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVFFMSDGATRPMDA 260
Cdd:cd05009     1 EDIKELAEKLKEAKSFYVLGRGPNYGTALE-GALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469305103 261 RALTFLERMGAKVALIDSKDYGLADA-----VPAsVITYFNPLLHLAVMREYGNQIAEAR-QHPLTMRRYMWK 327
Cdd:cd05009    80 SLIKEVKARGAKVIVITDDGDAKDLAdvvirVPA-TVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKS 151
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 28-124 5.61e-18

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: 78.69  E-value: 5.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  28 VAFVGCGASMSDLYPAKYFLANNTdKLNVQIFTANEFNYDTPSwVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVSL 107
Cdd:cd05008     2 ILIVGCGTSYHAALVAKYLLERLA-GIPVEVEAASEFRYRRPL-LDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAI 79

                          90
                  ....*....|....*..
gi 1469305103 108 TNKAGSALTVDADHVIV 124
Cdd:cd05008    80 TNVVGSTLAREADYVLY 96
frlB PRK11382
fructoselysine 6-phosphate deglycase;
16-277 4.89e-16

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 77.73  E-value: 4.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  16 VADVLSNHEIHSVAFVGCGASMSDLYPAKYfLANNTDKLNVQIFTANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANK 95
Cdd:PRK11382   35 IVEEMVKRDIDRIYFVACGSPLNAAQTAKH-LADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  96 TAKKHNCPVVSLTNKAGSALTVDADHVIvhgfhaNYAAKCEKPGYAI---ALALEILqqTEGYDHYEdmITGLTNVFDLC 172
Cdd:PRK11382  114 LGRACGALTAAFTKRADSPITSAAEFSI------DYQADCIWEIHLLlcySVVLEMI--TRLAPNAE--IGKIKNDLKQL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 173 ENAAQHCKKL----AKKFAEDFKDDKMIYFMASGASEKMAYSHAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVF 248
Cdd:PRK11382  184 PNALGHLVRTweekGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLF 263

                         250       260
                  ....*....|....*....|....*....
gi 1469305103 249 FMSDGATRPMDARALTFLERMGAKVALID 277
Cdd:PRK11382  264 LLGNDESRHTTERAINFVKQRTDNVIVID 292
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 24-237 8.53e-10

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 59.65  E-value: 8.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  24 EIHSVAFVGCGASmsdlYPAKYFLANNTDKLN----VQIFTANEFN-YDTPswvNEHTFVITCSLGGSTPETVEANKTAK 98
Cdd:PTZ00295  321 NIKNLILVGCGTS----YYAALFAASIMQKLKcfntVQVIDASELTlYRLP---DEDAGVIFISQSGETLDVVRALNLAD 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  99 KHNCPVVSLTNKAGSAL--TVDAdhvivhGFHANY-------AAKC--EKPGYAIALALEILQQTEGY---DHYEDMITG 164
Cdd:PTZ00295  394 ELNLPKISVVNTVGSLIarSTDC------GVYLNAgrevavaSTKAftSQVTVLSLIALWFAQNKEYScsnYKCSSLINS 467

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469305103 165 LTNVFDLCENAAQHCKKLAKKFAEDFKDDKMIYFMASGASEKMAYsHAAFLFTEMQWIDAAAYNTGEYFHGPF 237
Cdd:PTZ00295  468 LHRLPTYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIAL-EGALKIKEITYIHAEGFSGGALKHGPF 539
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
7-198 2.35e-09

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 58.52  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103   7 IDLNLPKQIVADVLSNheIHSVAFVGCG----ASMSdlypAKYFLANNTdKLNVQIFTANEFNYDTPsWVNEHTFVITCS 82
Cdd:PRK00331  273 LDELGEGELADEDLKK--IDRIYIVACGtsyhAGLV----AKYLIESLA-GIPVEVEIASEFRYRDP-VLSPKTLVIAIS 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  83 LGGSTPETVEANKTAKKHNCPVVSLTNKAGSALTVDADHVIVhgFHAnyaakcekpG------------------YAIAL 144
Cdd:PRK00331  345 QSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLY--THA---------GpeigvastkaftaqlavlYLLAL 413

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469305103 145 ALEILQQTEGYDHYEDMITGLTNVFDLCENAAQHcKKLAKKFAEDFKDDKMIYF 198
Cdd:PRK00331  414 ALAKARGTLSAEEEADLVHELRELPALIEQVLDL-KEQIEELAEDFADARNALF 466
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 1-209 3.63e-09

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 57.30  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103   1 MCQMYEIDLNLPKQI-------VADVLSN--HEIHSVAFVGCGAS------MSDLYpakyflannTDKLNVQIFTANefN 65
Cdd:PRK08674    1 PMGMLEEYLNWPEQFeealeiaISLDLEEdlEKIDNIVISGMGGSgiggdlLRILL---------FDELKVPVFVNR--D 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  66 YDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVSLTnkAGSALTVDA-----DHVIV-HGFHANYAAkcekpG 139
Cdd:PRK08674   70 YTLPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAIT--SGGKLKEMAkehglPVIIVpGGYQPRAAL-----G 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469305103 140 YAIALALEILQQTEGYDHYEDMITGLTNVF-DLCEN---AAQHCKKLAKKFAEDFKDD-KMIYfmASGASEKMAY 209
Cdd:PRK08674  143 YLFTPLLKILEKLGLIPDKSAEVLETKIVLsELAEGlkeKVPTLKNLAKRLAGKLYGRiPVIY--GSGLTLAVAY 215
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 16-124 4.37e-09

RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.


Pssm-ID: 240144 [Multi-domain]  Cd Length: 139  Bit Score: 54.16  E-value: 4.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  16 VADVLSNHEihSVAFVGCGASMSdlyPAKYFlANNTDKLNVQIFTANEFNYDTPSWVN--EHTFVITCSLGGSTPETVEA 93
Cdd:cd05013     6 AVDLLAKAR--RIYIFGVGSSGL---VAEYL-AYKLLRLGKPVVLLSDPHLQLMSAANltPGDVVIAISFSGETKETVEA 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1469305103  94 NKTAKKHNCPVVSLTNKAGSALTVDADHVIV 124
Cdd:cd05013    80 AEIAKERGAKVIAITDSANSPLAKLADIVLL 110
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 16-124 3.82e-07

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 50.70  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  16 VADVLSNHEihSVAFVGCGASMSdlyPAKYFlannTDKL-----NVQIFTAN-EFNYDTPSWVNEHTFVITCSLGGSTPE 89
Cdd:COG1737   127 AVDLLAKAR--RIYIFGVGASAP---VAEDL----AYKLlrlgkNVVLLDGDgHLQAESAALLGPGDVVIAISFSGYTRE 197

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1469305103  90 TVEANKTAKKHNCPVVSLTNKAGSALTVDADHVIV 124
Cdd:COG1737   198 TLEAARLAKERGAKVIAITDSPLSPLAKLADVVLY 232
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 72-123 2.52e-06

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: 47.90  E-value: 2.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1469305103  72 VNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVSLTNKAGSALTVDADHVI 123
Cdd:cd05007   116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAI 167
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 26-123 3.04e-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: 45.75  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  26 HSVAFVGCGASmsdlYPAKYFLANNTDKLNVQIF---TANEFNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHNC 102
Cdd:pfam01380   6 KRIFVIGRGTS----YAIALELALKFEEIGYKVVeveLASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81

                          90       100
                  ....*....|....*....|.
gi 1469305103 103 PVVSLTNKAGSALTVDADHVI 123
Cdd:pfam01380  82 KIIAITDSPGSPLAREADHVL 102
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 28-108 5.35e-06

The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.


Pssm-ID: 240148 [Multi-domain]  Cd Length: 119  Bit Score: 44.95  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  28 VAFVGCGAS------MSDLYPakyflanntDKLNVQIFTANefNYDTPSWVNEHTFVITCSLGGSTPETVEANKTAKKHN 101
Cdd:cd05017     2 IVILGMGGSgiggdlLESLLL---------DEAKIPVYVVK--DYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERG 70


                  ....*..
gi 1469305103 102 CPVVSLT 108
Cdd:cd05017    71 AKIVAIT 77
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 72-123 5.98e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 40.92  E-value: 5.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1469305103  72 VNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVSLTNKAGSALTVDADHVI 123
Cdd:PRK05441  129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAI 180
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 68-124 6.03e-04

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: 40.25  E-value: 6.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469305103  68 TPSwVNEHTFVITCSLGGSTPETVEANKTAKKHNCPVVSLTNKAGSALTVDADHVIV 124
Cdd:cd05005    70 TPA-IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 78-128 1.00e-03

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: 38.68  E-value: 1.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1469305103  78 VITCSLGGSTPETVEANKTAKKHNCPVVSLTNKAGSALTVDADHVIVHGFH 128
Cdd:cd05014    51 VIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVE 101
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 14-291 2.06e-03

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 39.86  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  14 QIVADVLSNHEIhsvAFVGCGASMSDLYPAKyFLANNTDKLNVQIFTANEFnYDTPSWVNEHTFVITCSLGGSTPETVEA 93
Cdd:PTZ00394  346 QSIRAILTSRRI---LFIACGTSLNSCLAVR-PLFEELVPLPISVENASDF-LDRRPRIQRDDVCFFVSQSGETADTLMA 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103  94 NKTAKKHNCPVVSLTNKAGSALTVDADHVIV--HGFHANYAAKCEKPGYAIALALEILQQTEGYDHYE----DMITGLTN 167
Cdd:PTZ00394  421 LQLCKEAGAMCVGITNVVGSSISRLTHYAIHlnAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQerrnEIIRGLAE 500

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 168 VfdlcENAAQHCKKL----AKKFAEDFKDDKMIYFMASGASEKMAYsHAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEG 243
Cdd:PTZ00394  501 L----PAAISECLKIthdpVKALAARLKESSSILVLGRGYDLATAM-EAALKVKELSYVHTEGIHSGELKHGPLALIDET 575

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469305103 244 KPYV--------FFMSDGATRPMDARAltflermGAKVALIDSKDYGLADA------VPASV 291
Cdd:PTZ00394  576 SPVLamcthdkhFGLSKSAVQQVKARG-------GAVVVFATEVDAELKAAaseivlVPKTV 630
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 194-321 2.53e-03

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: 37.66  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469305103 194 KMIYFMASGASEKMAySHAAFLFTEMQWIDAAAYNTGEYFHGPFEVSTEGKPYVFFMSDGATRPMDaRALTFLERMGAKV 273
Cdd:pfam01380   6 KRIFVIGRGTSYAIA-LELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLL-AAAELAKARGAKI 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1469305103 274 ALIdskdyglADAVPASVITYFNPLLHLAVMREYGNQIAEARQHPLTM 321
Cdd:pfam01380  84 IAI-------TDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAA 124
 
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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