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Conserved domains on  [gi|505377911|ref|WP_015565013|]
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MULTISPECIES: SIS domain-containing protein [Faecalibacterium]

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 ...
 24-146 4.35e-42

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: 141.94  E-value: 4.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  24 NVAFVGCGASKAELYPAKYFLANCSKkLRVAHYTANEFNYDTPDWLGDTTVVITASLGGSTPETVKANSVAKAAGATVVS 103
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 505377911 104 VTHAAGSALTKEADYTIVHGFEANyaAKLEKMGYVLALAVEIL 146
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGFEID--AVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 7-321 1.09e-31

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: 121.16  E-value: 1.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   7 ANVKSIVADIVAKHNvENVAFVGCGASKAELYPAKYFLANCSKkLRVAHYTANEFNYDTPDWLGDTTVVITASLGGSTPE 86
Cdd:COG2222   20 AAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLG-IPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSPE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  87 TVKANSVAKAAGATVVSVTHAAGSALTKEADYTIVHGF--EANYAAklEKmGYVLALAVeiLQQVEGFDKYDKMIEGLTN 164
Cdd:COG2222   98 VVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAgpEKSVAA--TK-SFTTMLLA--LLALLAAWGGDDALLAALD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 165 VFEAAENAANSARKSAKEFAEkYKDAPVVYVMSSGASMEVAYSTSIClMMEMQWVNSGSFHSGEFFHGPFEIVDKDVPFI 244
Cdd:COG2222  173 ALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALK-LKELSAGHAEAYSAAEFRHGPKSLVDPGTLVV 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 245 LLMNDGKTRPVDARALTFLHRFDALTTVVDAKDYG---LGNAVDSSVItyFNPLMHTAVFRVYAEELSYVRQHPLTLRRY 321
Cdd:COG2222  251 VLASEDPTRELDLDLAAELRALGARVVAIGAEDDAaitLPAIPDLHDA--LDPLLLLVVAQRLALALALARGLDPDTPRH 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 ...
 24-146 4.35e-42

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: 141.94  E-value: 4.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  24 NVAFVGCGASKAELYPAKYFLANCSKkLRVAHYTANEFNYDTPDWLGDTTVVITASLGGSTPETVKANSVAKAAGATVVS 103
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 505377911 104 VTHAAGSALTKEADYTIVHGFEANyaAKLEKMGYVLALAVEIL 146
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGFEID--AVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 7-321 1.09e-31

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: 121.16  E-value: 1.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   7 ANVKSIVADIVAKHNvENVAFVGCGASKAELYPAKYFLANCSKkLRVAHYTANEFNYDTPDWLGDTTVVITASLGGSTPE 86
Cdd:COG2222   20 AAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLG-IPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSPE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  87 TVKANSVAKAAGATVVSVTHAAGSALTKEADYTIVHGF--EANYAAklEKmGYVLALAVeiLQQVEGFDKYDKMIEGLTN 164
Cdd:COG2222   98 VVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAgpEKSVAA--TK-SFTTMLLA--LLALLAAWGGDDALLAALD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 165 VFEAAENAANSARKSAKEFAEkYKDAPVVYVMSSGASMEVAYSTSIClMMEMQWVNSGSFHSGEFFHGPFEIVDKDVPFI 244
Cdd:COG2222  173 ALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALK-LKELSAGHAEAYSAAEFRHGPKSLVDPGTLVV 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 245 LLMNDGKTRPVDARALTFLHRFDALTTVVDAKDYG---LGNAVDSSVItyFNPLMHTAVFRVYAEELSYVRQHPLTLRRY 321
Cdd:COG2222  251 VLASEDPTRELDLDLAAELRALGARVVAIGAEDDAaitLPAIPDLHDA--LDPLLLLVVAQRLALALALARGLDPDTPRH 328
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 178-326 1.35e-27

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: 105.04  E-value: 1.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 178 KSAKEFAEKYKDAPVVYVMSSGASMEVAYSTSICLMmEMQWVNSGSFHSGEFFHGPFEIVDKDVPFILLMNDGKTRPVDA 257
Cdd:cd05009    1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLK-ETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505377911 258 RALTFLHRFDALTTVVDAKDYGLGNAVDS----SVITYFNPLMHTAVFRVYAEELSYVR-QHPLTLRRYMWKLE 326
Cdd:cd05009   80 SLIKEVKARGAKVIVITDDGDAKDLADVVirvpATVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKSVT 153
frlB PRK11382
fructoselysine 6-phosphate deglycase;
5-281 3.69e-24

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 100.85  E-value: 3.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   5 DLANVKSIVADIVaKHNVENVAFVGCGASKAELYPAKYfLANCSKKLRVAHYTANEFNYDTPDWLGDTTVVITASLGGST 84
Cdd:PRK11382  28 DVPLVHAIVEEMV-KRDIDRIYFVACGSPLNAAQTAKH-LADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  85 PETVKANSVAKAAGATVVSVTHAAGSALTKEADYTIvhGFEANYAAKLEKMgYVLALAVEILQQVEGFDKYDKMIEGLTN 164
Cdd:PRK11382 106 EEVIKALELGRACGALTAAFTKRADSPITSAAEFSI--DYQADCIWEIHLL-LCYSVVLEMITRLAPNAEIGKIKNDLKQ 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 165 VFEAAENAANSARKSAKEFAEKYKDAPVVYVMSSGASMEVAYSTSICLMMEMQWVNSGSFHSGEFFHGPFEIVDKDVPFI 244
Cdd:PRK11382 183 LPNALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFL 262

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 505377911 245 LLMNDGKTRPVDARALTFLHRFDALTTVVDAKDYGLG 281
Cdd:PRK11382 263 FLLGNDESRHTTERAINFVKQRTDNVIVIDYAEISQG 299
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 21-249 2.94e-10

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 61.19  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  21 NVENVAFVGCGASkaelYPAKYFLANCSKKLR----VAHYTANEFN-YDTPDwlGDTTVV-ITASlgGSTPETVKANSVA 94
Cdd:PTZ00295 321 NIKNLILVGCGTS----YYAALFAASIMQKLKcfntVQVIDASELTlYRLPD--EDAGVIfISQS--GETLDVVRALNLA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  95 KAAGATVVSVTHAAGSALTKEADYTI-VH-GFEANYAAKLEKMGYVLAL---AVEILQQVEGFDKYDKM---IEGLTNVF 166
Cdd:PTZ00295 393 DELNLPKISVVNTVGSLIARSTDCGVyLNaGREVAVASTKAFTSQVTVLsliALWFAQNKEYSCSNYKCsslINSLHRLP 472

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 167 EAAENAANSARKSAKEFAEKYKDAPVVYVMSSGASMEVAYSTSIcLMMEMQWVNSGSFHSGEFFHGPFEIVDKD--VPFI 244
Cdd:PTZ00295 473 TYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGAL-KIKEITYIHAEGFSGGALKHGPFALIDKEknTPVI 551


                 ....*
gi 505377911 245 LLMND 249
Cdd:PTZ00295 552 LIILD 556
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 3-121 4.69e-10

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 59.56  E-value: 4.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   3 NIDLANVKSIVADIVAKHNVEnvaFVGCGASKAelyPAKYFlancSKKLRVAHYTANEFNYDTPDW------LGDTTVVI 76
Cdd:COG1737  118 LLDEEALERAVDLLAKARRIY---IFGVGASAP---VAEDL----AYKLLRLGKNVVLLDGDGHLQaesaalLGPGDVVI 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 505377911  77 TASLGGSTPETVKANSVAKAAGATVVSVTHAAGSALTKEADYTIV 121
Cdd:COG1737  188 AISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLY 232
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 20-120 3.03e-07

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 48.83  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   20 HNVENVAFVGCGASkaelYPAKYFLANCSKKLRVAH---YTANEFNYDTPDWLGDTTVVITASLGGSTPETVKANSVAKA 96
Cdd:pfam01380   3 AKAKRIFVIGRGTS----YAIALELALKFEEIGYKVvevELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKA 78

                          90       100
                  ....*....|....*....|....
gi 505377911   97 AGATVVSVTHAAGSALTKEADYTI 120
Cdd:pfam01380  79 RGAKIIAITDSPGSPLAREADHVL 102
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 24-146 4.35e-42

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: 141.94  E-value: 4.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  24 NVAFVGCGASKAELYPAKYFLANCSKkLRVAHYTANEFNYDTPDWLGDTTVVITASLGGSTPETVKANSVAKAAGATVVS 103
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 505377911 104 VTHAAGSALTKEADYTIVHGFEANyaAKLEKMGYVLALAVEIL 146
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGFEID--AVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 7-321 1.09e-31

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: 121.16  E-value: 1.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   7 ANVKSIVADIVAKHNvENVAFVGCGASKAELYPAKYFLANCSKkLRVAHYTANEFNYDTPDWLGDTTVVITASLGGSTPE 86
Cdd:COG2222   20 AAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLG-IPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSPE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  87 TVKANSVAKAAGATVVSVTHAAGSALTKEADYTIVHGF--EANYAAklEKmGYVLALAVeiLQQVEGFDKYDKMIEGLTN 164
Cdd:COG2222   98 VVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAgpEKSVAA--TK-SFTTMLLA--LLALLAAWGGDDALLAALD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 165 VFEAAENAANSARKSAKEFAEkYKDAPVVYVMSSGASMEVAYSTSIClMMEMQWVNSGSFHSGEFFHGPFEIVDKDVPFI 244
Cdd:COG2222  173 ALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALK-LKELSAGHAEAYSAAEFRHGPKSLVDPGTLVV 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 245 LLMNDGKTRPVDARALTFLHRFDALTTVVDAKDYG---LGNAVDSSVItyFNPLMHTAVFRVYAEELSYVRQHPLTLRRY 321
Cdd:COG2222  251 VLASEDPTRELDLDLAAELRALGARVVAIGAEDDAaitLPAIPDLHDA--LDPLLLLVVAQRLALALALARGLDPDTPRH 328
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 178-326 1.35e-27

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: 105.04  E-value: 1.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 178 KSAKEFAEKYKDAPVVYVMSSGASMEVAYSTSICLMmEMQWVNSGSFHSGEFFHGPFEIVDKDVPFILLMNDGKTRPVDA 257
Cdd:cd05009    1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLK-ETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505377911 258 RALTFLHRFDALTTVVDAKDYGLGNAVDS----SVITYFNPLMHTAVFRVYAEELSYVR-QHPLTLRRYMWKLE 326
Cdd:cd05009   80 SLIKEVKARGAKVIVITDDGDAKDLADVVirvpATVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKSVT 153
frlB PRK11382
fructoselysine 6-phosphate deglycase;
5-281 3.69e-24

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 100.85  E-value: 3.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   5 DLANVKSIVADIVaKHNVENVAFVGCGASKAELYPAKYfLANCSKKLRVAHYTANEFNYDTPDWLGDTTVVITASLGGST 84
Cdd:PRK11382  28 DVPLVHAIVEEMV-KRDIDRIYFVACGSPLNAAQTAKH-LADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  85 PETVKANSVAKAAGATVVSVTHAAGSALTKEADYTIvhGFEANYAAKLEKMgYVLALAVEILQQVEGFDKYDKMIEGLTN 164
Cdd:PRK11382 106 EEVIKALELGRACGALTAAFTKRADSPITSAAEFSI--DYQADCIWEIHLL-LCYSVVLEMITRLAPNAEIGKIKNDLKQ 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 165 VFEAAENAANSARKSAKEFAEKYKDAPVVYVMSSGASMEVAYSTSICLMMEMQWVNSGSFHSGEFFHGPFEIVDKDVPFI 244
Cdd:PRK11382 183 LPNALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFL 262

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 505377911 245 LLMNDGKTRPVDARALTFLHRFDALTTVVDAKDYGLG 281
Cdd:PRK11382 263 FLLGNDESRHTTERAINFVKQRTDNVIVIDYAEISQG 299
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 24-121 4.85e-15

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: 70.60  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  24 NVAFVGCGASKAELYPAKYFLANCSKkLRVAHYTANEFNYDTPDwLGDTTVVITASLGGSTPETVKANSVAKAAGATVVS 103
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAG-IPVEVEAASEFRYRRPL-LDEDTLVIAISQSGETADTLAALRLAKEKGAKTVA 78

                         90
                 ....*....|....*...
gi 505377911 104 VTHAAGSALTKEADYTIV 121
Cdd:cd05008   79 ITNVVGSTLAREADYVLY 96
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 13-121 2.60e-10

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: 57.62  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  13 VADIVAKHnvENVAFVGCGASKAelyPAKYFlancSKKLRVAHYTAneFNYDTPDW-------LGDTTVVITASLGGSTP 85
Cdd:cd05013    6 AVDLLAKA--RRIYIFGVGSSGL---VAEYL----AYKLLRLGKPV--VLLSDPHLqlmsaanLTPGDVVIAISFSGETK 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505377911  86 ETVKANSVAKAAGATVVSVTHAAGSALTKEADYTIV 121
Cdd:cd05013   75 ETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLL 110
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 21-249 2.94e-10

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 61.19  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  21 NVENVAFVGCGASkaelYPAKYFLANCSKKLR----VAHYTANEFN-YDTPDwlGDTTVV-ITASlgGSTPETVKANSVA 94
Cdd:PTZ00295 321 NIKNLILVGCGTS----YYAALFAASIMQKLKcfntVQVIDASELTlYRLPD--EDAGVIfISQS--GETLDVVRALNLA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  95 KAAGATVVSVTHAAGSALTKEADYTI-VH-GFEANYAAKLEKMGYVLAL---AVEILQQVEGFDKYDKM---IEGLTNVF 166
Cdd:PTZ00295 393 DELNLPKISVVNTVGSLIARSTDCGVyLNaGREVAVASTKAFTSQVTVLsliALWFAQNKEYSCSNYKCsslINSLHRLP 472

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 167 EAAENAANSARKSAKEFAEKYKDAPVVYVMSSGASMEVAYSTSIcLMMEMQWVNSGSFHSGEFFHGPFEIVDKD--VPFI 244
Cdd:PTZ00295 473 TYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGAL-KIKEITYIHAEGFSGGALKHGPFALIDKEknTPVI 551


                 ....*
gi 505377911 245 LLMND 249
Cdd:PTZ00295 552 LIILD 556
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 3-121 4.69e-10

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 59.56  E-value: 4.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   3 NIDLANVKSIVADIVAKHNVEnvaFVGCGASKAelyPAKYFlancSKKLRVAHYTANEFNYDTPDW------LGDTTVVI 76
Cdd:COG1737  118 LLDEEALERAVDLLAKARRIY---IFGVGASAP---VAEDL----AYKLLRLGKNVVLLDGDGHLQaesaalLGPGDVVI 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 505377911  77 TASLGGSTPETVKANSVAKAAGATVVSVTHAAGSALTKEADYTIV 121
Cdd:COG1737  188 AISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLY 232
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 71-244 4.77e-10

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 60.66  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  71 DTTVVITASlgGSTPETVKANSVAKAAGATVVSVTHAAGSALTKEADYTIV--HGFEANYAAKLEKMGYVLALAVEIL-- 146
Cdd:PTZ00394 403 DVCFFVSQS--GETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHlnAGVEVGVASTKAYTSQVVVLTLVALll 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 147 --QQVEGFDKYDKMIEGLTNVFEAAENAANSARKSAKEFAEKYKDAPVVYVMSSGASMEVAYSTSIcLMMEMQWVNSGSF 224
Cdd:PTZ00394 481 ssDSVRLQERRNEIIRGLAELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATAMEAAL-KVKELSYVHTEGI 559

                        170       180
                 ....*....|....*....|
gi 505377911 225 HSGEFFHGPFEIVDKDVPFI 244
Cdd:PTZ00394 560 HSGELKHGPLALIDETSPVL 579
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 68-121 1.55e-07

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: 50.65  E-value: 1.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505377911  68 WLGDTT--------VVITASLGGSTPETVKANSVAKAAGATVVSVTHAAGSALTKEADYTIV 121
Cdd:cd05005   64 VVGETTtpaigpgdLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 20-120 3.03e-07

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 48.83  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911   20 HNVENVAFVGCGASkaelYPAKYFLANCSKKLRVAH---YTANEFNYDTPDWLGDTTVVITASLGGSTPETVKANSVAKA 96
Cdd:pfam01380   3 AKAKRIFVIGRGTS----YAIALELALKFEEIGYKVvevELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKA 78

                          90       100
                  ....*....|....*....|....
gi 505377911   97 AGATVVSVTHAAGSALTKEADYTI 120
Cdd:pfam01380  79 RGAKIIAITDSPGSPLAREADHVL 102
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
21-120 1.96e-06

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 49.27  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  21 NVENVAFVGCGASK-AELYpAKYF---LAncskKLRVAHYTANEFNYDTPdWLGDTTVVITASLGGSTPETVKANSVAKA 96
Cdd:PRK00331 288 KIDRIYIVACGTSYhAGLV-AKYLiesLA----GIPVEVEIASEFRYRDP-VLSPKTLVIAISQSGETADTLAALRLAKE 361

                         90       100
                 ....*....|....*....|....
gi 505377911  97 AGATVVSVTHAAGSALTKEADYTI 120
Cdd:PRK00331 362 LGAKTLAICNVPGSTIARESDAVL 385
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 62-206 1.27e-05

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 46.13  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  62 NYDTPDWLGDTTVVITASLGGSTPETVKANSVAKAAGATVVSVThaAGSALTKEAD------YTIVHGFEANYAaklekM 135
Cdd:PRK08674  69 DYTLPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAIT--SGGKLKEMAKehglpvIIVPGGYQPRAA-----L 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505377911 136 GYVLALAVEILQQVEGFDKYDKMIEGLTNVFEAAENAANSARKSAKEFAEK-----YKDAPVVYvmSSGASMEVAY 206
Cdd:PRK08674 142 GYLFTPLLKILEKLGLIPDKSAEVLETKIVLSELAEGLKEKVPTLKNLAKRlagklYGRIPVIY--GSGLTLAVAY 215
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 25-246 1.67e-05

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 46.28  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  25 VAFVGCGASKAELYPAKYFLANCSKkLRVAHYTANEF-NYDTPDWLGDTTVVITASlgGSTPETVKANSVAKAAGATVVS 103
Cdd:PLN02981 366 IVFIGCGTSYNAALAARPILEELSG-VPVTMELASDLlDRQGPIYREDTAVFVSQS--GETADTLRALEYAKENGALCVG 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911 104 VTHAAGSALTKEADYTiVH---GFEAN------YAAKLEKMgYVLALAV---EILQQvegfDKYDKMIEGLTNVfEAAEN 171
Cdd:PLN02981 443 ITNTVGSAISRGTHCG-VHinaGAEIGvastkaYTSQIVAM-TMLALALgedSISSR----SRREAIIDGLFDL-PNKVR 515

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505377911 172 AANSARKSAKEFAEKYKDAPVVYVMSSGASmevaYSTSI---CLMMEMQWVNSGSFHSGEFFHGPFEIVDKDVPFILL 246
Cdd:PLN02981 516 EVLKLDQEMKELAELLIDEQSLLVFGRGYN----YATALegaLKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVI 589
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
69-148 4.90e-05

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 44.37  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  69 LGDTTVVITASLGGSTPETVKANSVAKAAGATVVSVTHAAGSALTKEADYTI------VHGFEANYAAKLEKMGYVLALA 142
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVIcstaqgSPLLGENAAARIAQLNILDAFF 264


                 ....*.
gi 505377911 143 VEILQQ 148
Cdd:PRK11337 265 VSVAQL 270
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 70-120 5.44e-05

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: 44.05  E-value: 5.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505377911  70 GDTTVVITASlgGSTPETVKANSVAKAAGATVVSVTHAAGSALTKEADYTI 120
Cdd:cd05007  119 RDVVIGIAAS--GRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAI 167
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 70-120 1.49e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 42.85  E-value: 1.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505377911  70 GDTTVVITASlgGSTPETVKANSVAKAAGATVVSVTHAAGSALTKEADYTI 120
Cdd:PRK05441 132 KDVVVGIAAS--GRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAI 180
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
70-120 1.85e-03

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 39.30  E-value: 1.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505377911  70 GDTTVVITASlgGSTPETVKANSVAKAAGATVVSVTHAAGSALTKEADYTI 120
Cdd:PRK15482 183 GDVQIAISYS--GSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTL 231
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 24-105 4.97e-03

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: 36.47  E-value: 4.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505377911  24 NVAFVGCGASKAelyPAKYFLANCSKKLRVAHYTANefNYDTPDWLGDTTVVITASLGGSTPETVKANSVAKAAGATVVS 103
Cdd:cd05017    1 NIVILGMGGSGI---GGDLLESLLLDEAKIPVYVVK--DYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVA 75


                 ..
gi 505377911 104 VT 105
Cdd:cd05017   76 IT 77
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 73-121 6.46e-03

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 37.71  E-value: 6.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505377911  73 TVVITASLGGSTpetVKANSVAKAAGATVVSVT--HAAGSALTKEADYTIV 121
Cdd:PRK13771 165 TVLVTGAGGGVG---IHAIQVAKALGAKVIAVTssESKAKIVSKYADYVIV 212
 
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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