NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488982184|ref|WP_002893003|]
View 

MULTISPECIES: SIS domain-containing protein [Klebsiella]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 23-148 1.19e-46

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: 153.89  E-value: 1.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  23 RVWFVGCGGSLTGFWPGKYFLDCEAKkLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQKGAATIG 102
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488982184 103 LVYTPGTPLCEHSDYTIEYCWarypeTVDPTQQKAAYSLWLALEVL 148
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGF-----EIDAVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 4-326 2.39e-39

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: 141.57  E-value: 2.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184   4 AHQNAHTIIRDILSK---QHIERVWFVGCGGSltgfW----PGKYFLdCEAKKLAVGYVTSNEFVHATPNALGKNSVVIL 76
Cdd:COG2222   14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  77 ASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIeycwarypeTVDPTQQKA-------AYSLWLALEVLA 149
Cdd:COG2222   89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL---------PLPAGPEKSvaatksfTTMLLALLALLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 150 QTEGyahyDEmvSAFASFESVVRGAQQQVQADARHFAE-AWKSEKVIYMMGSGPSFGAAHqESICILLEMQWINSASIHS 228
Cdd:COG2222  160 AWGG----DD--ALLAALDALPAALEAALAADWPAAALaALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 229 GEYFHGPFEITETGTPFILLKSSGRTRPLDDRAIRFIERYQGKLQIIDVEKVGIDAL--HASVREYFCGLLHNCVLDVYN 306
Cdd:COG2222  233 AEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLpaIPDLHDALDPLLLLVVAQRLA 312

                        330       340
                 ....*....|....*....|
gi 488982184 307 LALATARNHPLTTRRYMWKV 326
Cdd:COG2222  313 LALALARGLDPDTPRHLNKV 332
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 23-148 1.19e-46

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: 153.89  E-value: 1.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  23 RVWFVGCGGSLTGFWPGKYFLDCEAKkLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQKGAATIG 102
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488982184 103 LVYTPGTPLCEHSDYTIEYCWarypeTVDPTQQKAAYSLWLALEVL 148
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGF-----EIDAVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 4-326 2.39e-39

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: 141.57  E-value: 2.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184   4 AHQNAHTIIRDILSK---QHIERVWFVGCGGSltgfW----PGKYFLdCEAKKLAVGYVTSNEFVHATPNALGKNSVVIL 76
Cdd:COG2222   14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  77 ASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIeycwarypeTVDPTQQKA-------AYSLWLALEVLA 149
Cdd:COG2222   89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL---------PLPAGPEKSvaatksfTTMLLALLALLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 150 QTEGyahyDEmvSAFASFESVVRGAQQQVQADARHFAE-AWKSEKVIYMMGSGPSFGAAHqESICILLEMQWINSASIHS 228
Cdd:COG2222  160 AWGG----DD--ALLAALDALPAALEAALAADWPAAALaALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 229 GEYFHGPFEITETGTPFILLKSSGRTRPLDDRAIRFIERYQGKLQIIDVEKVGIDAL--HASVREYFCGLLHNCVLDVYN 306
Cdd:COG2222  233 AEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLpaIPDLHDALDPLLLLVVAQRLA 312

                        330       340
                 ....*....|....*....|
gi 488982184 307 LALATARNHPLTTRRYMWKV 326
Cdd:COG2222  313 LALALARGLDPDTPRHLNKV 332
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 181-327 9.55e-32

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: 116.21  E-value: 9.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 181 DARHFAEAWKSEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITETGTPFILLKSSGRTRPLDDR 260
Cdd:cd05009    2 DIKELAEKLKEAKSFYVLGRGPNYGTA-LEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488982184 261 AIRFIERYQGKLQIIDVEKVGIDA-----LHASVREYFCGLLHNCVLDVYNLALATAR-NHPLTTRRYMWKVE 327
Cdd:cd05009   81 LIKEVKARGAKVIVITDDGDAKDLadvviRVPATVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKSVT 153
frlB PRK11382
fructoselysine 6-phosphate deglycase;
9-280 1.74e-26

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 107.01  E-value: 1.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184   9 HTIIRDILsKQHIERVWFVGCGGSLTGFWPGKYFLDcEAKKLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVE 88
Cdd:PRK11382  33 HAIVEEMV-KRDIDRIYFVACGSPLNAAQTAKHLAD-RFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  89 AARIARQKGAATIGLVYTPGTPLCEHSDYTIEYcwarYPETVDPTQQKAAYSLwlALEVLAQTEGYAHYDEMVSAFASFE 168
Cdd:PRK11382 111 ALELGRACGALTAAFTKRADSPITSAAEFSIDY----QADCIWEIHLLLCYSV--VLEMITRLAPNAEIGKIKNDLKQLP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 169 SVVRGAQQQVQADARHFAEAWKSEKVIYMMGSGPSFGAAHQESICILLEMQWINSASIHSGEYFHGPFEITETGTPFILL 248
Cdd:PRK11382 185 NALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFL 264

                        250       260       270
                 ....*....|....*....|....*....|..
gi 488982184 249 KSSGRTRPLDDRAIRFIERYQGKLQIIDVEKV 280
Cdd:PRK11382 265 LGNDESRHTTERAINFVKQRTDNVIVIDYAEI 296
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 15-119 3.96e-11

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: 59.62  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184   15 ILSKQHieRVWFVGCGGSLTGFWPGKYFLDCEAKKLAVGYVTSnEFVHATPNALGKNSVVILASQQGNTAETVEAARIAR 94
Cdd:pfam01380   1 LLAKAK--RIFVIGRGTSYAIALELALKFEEIGYKVVEVELAS-ELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAK 77

                          90       100
                  ....*....|....*....|....*
gi 488982184   95 QKGAATIGLVYTPGTPLCEHSDYTI 119
Cdd:pfam01380  78 ARGAKIIAITDSPGSPLAREADHVL 102
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 22-121 4.23e-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: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  22 ERVWFVGCGGSltgFWPGKYFldceAKKL------AVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQ 95
Cdd:COG1737  135 RRIYIFGVGAS---APVAEDL----AYKLlrlgknVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKE 207

                         90       100
                 ....*....|....*....|....*.
gi 488982184  96 KGAATIGLVYTPGTPLCEHSDYTIEY 121
Cdd:COG1737  208 RGAKVIAITDSPLSPLAKLADVVLYV 233
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 14-248 1.86e-09

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 58.88  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  14 DILSKQHIErvwFVGCGGSLTGFWPGKYFLdceaKKLA----VGYVTSNEF-VHATPNalgKNSVVILASQQGNTAETVE 88
Cdd:PTZ00295 318 ELLNIKNLI---LVGCGTSYYAALFAASIM----QKLKcfntVQVIDASELtLYRLPD---EDAGVIFISQSGETLDVVR 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  89 AARIARQKGAATIGLVYTPGTPLCEHSDYTIEYCWAR---YPETVDPTQQKAAYSLwLALEVLAQTEGYAHYD---EMVS 162
Cdd:PTZ00295 388 ALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGRevaVASTKAFTSQVTVLSL-IALWFAQNKEYSCSNYkcsSLIN 466

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 163 AFASFESVVRGAQQQVQADARHFAEAWKSEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEI--TE 240
Cdd:PTZ00295 467 SLHRLPTYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIA-LEGALKIKEITYIHAEGFSGGALKHGPFALidKE 545


                 ....*...
gi 488982184 241 TGTPFILL 248
Cdd:PTZ00295 546 KNTPVILI 553
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 23-148 1.19e-46

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: 153.89  E-value: 1.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  23 RVWFVGCGGSLTGFWPGKYFLDCEAKkLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQKGAATIG 102
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488982184 103 LVYTPGTPLCEHSDYTIEYCWarypeTVDPTQQKAAYSLWLALEVL 148
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGF-----EIDAVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 4-326 2.39e-39

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: 141.57  E-value: 2.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184   4 AHQNAHTIIRDILSK---QHIERVWFVGCGGSltgfW----PGKYFLdCEAKKLAVGYVTSNEFVHATPNALGKNSVVIL 76
Cdd:COG2222   14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  77 ASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIeycwarypeTVDPTQQKA-------AYSLWLALEVLA 149
Cdd:COG2222   89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL---------PLPAGPEKSvaatksfTTMLLALLALLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 150 QTEGyahyDEmvSAFASFESVVRGAQQQVQADARHFAE-AWKSEKVIYMMGSGPSFGAAHqESICILLEMQWINSASIHS 228
Cdd:COG2222  160 AWGG----DD--ALLAALDALPAALEAALAADWPAAALaALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 229 GEYFHGPFEITETGTPFILLKSSGRTRPLDDRAIRFIERYQGKLQIIDVEKVGIDAL--HASVREYFCGLLHNCVLDVYN 306
Cdd:COG2222  233 AEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLpaIPDLHDALDPLLLLVVAQRLA 312

                        330       340
                 ....*....|....*....|
gi 488982184 307 LALATARNHPLTTRRYMWKV 326
Cdd:COG2222  313 LALALARGLDPDTPRHLNKV 332
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 181-327 9.55e-32

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: 116.21  E-value: 9.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 181 DARHFAEAWKSEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITETGTPFILLKSSGRTRPLDDR 260
Cdd:cd05009    2 DIKELAEKLKEAKSFYVLGRGPNYGTA-LEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488982184 261 AIRFIERYQGKLQIIDVEKVGIDA-----LHASVREYFCGLLHNCVLDVYNLALATAR-NHPLTTRRYMWKVE 327
Cdd:cd05009   81 LIKEVKARGAKVIVITDDGDAKDLadvviRVPATVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKSVT 153
frlB PRK11382
fructoselysine 6-phosphate deglycase;
9-280 1.74e-26

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 107.01  E-value: 1.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184   9 HTIIRDILsKQHIERVWFVGCGGSLTGFWPGKYFLDcEAKKLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVE 88
Cdd:PRK11382  33 HAIVEEMV-KRDIDRIYFVACGSPLNAAQTAKHLAD-RFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  89 AARIARQKGAATIGLVYTPGTPLCEHSDYTIEYcwarYPETVDPTQQKAAYSLwlALEVLAQTEGYAHYDEMVSAFASFE 168
Cdd:PRK11382 111 ALELGRACGALTAAFTKRADSPITSAAEFSIDY----QADCIWEIHLLLCYSV--VLEMITRLAPNAEIGKIKNDLKQLP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 169 SVVRGAQQQVQADARHFAEAWKSEKVIYMMGSGPSFGAAHQESICILLEMQWINSASIHSGEYFHGPFEITETGTPFILL 248
Cdd:PRK11382 185 NALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFL 264

                        250       260       270
                 ....*....|....*....|....*....|..
gi 488982184 249 KSSGRTRPLDDRAIRFIERYQGKLQIIDVEKV 280
Cdd:PRK11382 265 LGNDESRHTTERAINFVKQRTDNVIVIDYAEI 296
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 23-147 7.17e-16

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: 72.91  E-value: 7.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  23 RVWFVGCGGSL-TGFwPGKYFLDcEAKKLAVGYVTSNEFVHATPNaLGKNSVVILASQQGNTAETVEAARIARQKGAATI 101
Cdd:cd05008    1 RILIVGCGTSYhAAL-VAKYLLE-RLAGIPVEVEAASEFRYRRPL-LDEDTLVIAISQSGETADTLAALRLAKEKGAKTV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488982184 102 GLVYTPGTPLCEHSDYTIeYCWARYPETVDPTqqKAAYS-----LWLALEV 147
Cdd:cd05008   78 AITNVVGSTLAREADYVL-YLRAGPEISVAAT--KAFTSqllalLLLALAL 125
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 11-279 2.33e-12

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 67.60  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  11 IIRDILSKQhieRVWFVGCGGSLTGFWPGKYFLDcEAKKLAVGYVTSNEFVHATPNaLGKNSVVILASQQGNTAETVEAA 90
Cdd:PTZ00394 347 SIRAILTSR---RILFIACGTSLNSCLAVRPLFE-ELVPLPISVENASDFLDRRPR-IQRDDVCFFVSQSGETADTLMAL 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  91 RIARQKGAATIGLVYTPGTPLCEHSDYTIEYcwaRYPETVDPTQQKAAYSLWLALEVLA------QTEGYAHYDEMVSAF 164
Cdd:PTZ00394 422 QLCKEAGAMCVGITNVVGSSISRLTHYAIHL---NAGVEVGVASTKAYTSQVVVLTLVAlllssdSVRLQERRNEIIRGL 498

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 165 ASFESVVRGAQQQVQADARHFAEAWKSEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITETGTP 244
Cdd:PTZ00394 499 AELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATA-MEAALKVKELSYVHTEGIHSGELKHGPLALIDETSP 577

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488982184 245 FILLKSSGRTRPLDDRAIRFIERYQGKLQIIDVEK 279
Cdd:PTZ00394 578 VLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEV 612
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 15-119 3.96e-11

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: 59.62  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184   15 ILSKQHieRVWFVGCGGSLTGFWPGKYFLDCEAKKLAVGYVTSnEFVHATPNALGKNSVVILASQQGNTAETVEAARIAR 94
Cdd:pfam01380   1 LLAKAK--RIFVIGRGTSYAIALELALKFEEIGYKVVEVELAS-ELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAK 77

                          90       100
                  ....*....|....*....|....*
gi 488982184   95 QKGAATIGLVYTPGTPLCEHSDYTI 119
Cdd:pfam01380  78 ARGAKIIAITDSPGSPLAREADHVL 102
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 22-121 6.57e-11

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: 59.55  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  22 ERVWFVGCGGSltgFWPGKYFldceAKKL-----AVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQK 96
Cdd:cd05013   14 RRIYIFGVGSS---GLVAEYL----AYKLlrlgkPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86

                         90       100
                 ....*....|....*....|....*
gi 488982184  97 GAATIGLVYTPGTPLCEHSDYTIEY 121
Cdd:cd05013   87 GAKVIAITDSANSPLAKLADIVLLV 111
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 22-121 4.23e-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: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  22 ERVWFVGCGGSltgFWPGKYFldceAKKL------AVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQ 95
Cdd:COG1737  135 RRIYIFGVGAS---APVAEDL----AYKLlrlgknVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKE 207

                         90       100
                 ....*....|....*....|....*.
gi 488982184  96 KGAATIGLVYTPGTPLCEHSDYTIEY 121
Cdd:COG1737  208 RGAKVIAITDSPLSPLAKLADVVLYV 233
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 14-248 1.86e-09

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 58.88  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  14 DILSKQHIErvwFVGCGGSLTGFWPGKYFLdceaKKLA----VGYVTSNEF-VHATPNalgKNSVVILASQQGNTAETVE 88
Cdd:PTZ00295 318 ELLNIKNLI---LVGCGTSYYAALFAASIM----QKLKcfntVQVIDASELtLYRLPD---EDAGVIFISQSGETLDVVR 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  89 AARIARQKGAATIGLVYTPGTPLCEHSDYTIEYCWAR---YPETVDPTQQKAAYSLwLALEVLAQTEGYAHYD---EMVS 162
Cdd:PTZ00295 388 ALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGRevaVASTKAFTSQVTVLSL-IALWFAQNKEYSCSNYkcsSLIN 466

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184 163 AFASFESVVRGAQQQVQADARHFAEAWKSEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEI--TE 240
Cdd:PTZ00295 467 SLHRLPTYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIA-LEGALKIKEITYIHAEGFSGGALKHGPFALidKE 545


                 ....*...
gi 488982184 241 TGTPFILL 248
Cdd:PTZ00295 546 KNTPVILI 553
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 64-120 9.03e-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: 48.34  E-value: 9.03e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488982184  64 TPnALGKNSVVILASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIE 120
Cdd:cd05005   70 TP-AIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 68-120 4.20e-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: 47.52  E-value: 4.20e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488982184  68 LGKNSVVILASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIE 120
Cdd:cd05007  116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIA 168
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 73-120 9.42e-06

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 46.53  E-value: 9.42e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488982184  73 VVILASQQGNTAETVEAARIARQKGAATIGLVyTPGTPLCEHSDYTIE 120
Cdd:PRK11302 178 VVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPLAREATLALT 224
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
68-119 2.23e-05

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 45.52  E-value: 2.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488982184  68 LGKNSVVILASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTI 119
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 23-101 2.60e-05

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: 43.02  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  23 RVWFVGCGGSltgFWPGKYFLDCEAKKLAVgyvtsNEFVHAT---PNALGKNSVVILASQQGNTAETVEAARIARQKGAA 99
Cdd:cd05017    1 NIVILGMGGS---GIGGDLLESLLLDEAKI-----PVYVVKDytlPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAK 72


                 ..
gi 488982184 100 TI 101
Cdd:cd05017   73 IV 74
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 68-120 7.98e-05

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 43.62  E-value: 7.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488982184  68 LGKNSVVILASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIE 120
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIE 181
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
12-120 4.46e-04

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 41.22  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  12 IRDILSKQHIERVWFVGcGGSLTGfwpgkyfLDCEAKKLAVGYVTSNE---FVHAT-PNALGKNSVVILASQQGNTAETV 87
Cdd:PRK15482 128 IIEVISKAPFIQITGLG-GSALVG-------RDLSFKLMKIGYRVACEadtHVQATvSQALKKGDVQIAISYSGSKKEIV 199

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488982184  88 EAARIARQKGAATIGLVYTPGTPLCEHSDYTIE 120
Cdd:PRK15482 200 LCAEAARKQGATVIAITSLADSPLRRLAHFTLD 232
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 21-101 8.54e-04

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 40.74  E-value: 8.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  21 IERVWFVGCGGSLTGfwpGKYFLDCEAKKLAVGYVTSNEFVhaTPNALGKNSVVILASQQGNTAETVEAARIARQKGAAT 100
Cdd:PRK08674  34 IDNIVISGMGGSGIG---GDLLRILLFDELKVPVFVNRDYT--LPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKI 108


                 .
gi 488982184 101 I 101
Cdd:PRK08674 109 I 109
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 60-119 1.57e-03

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


Pssm-ID: 440557 [Multi-domain]  Cd Length: 317  Bit Score: 39.57  E-value: 1.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488982184  60 FVHATpNA----LG---KNSVVILASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTI 119
Cdd:COG0794   75 FLHPA-EAshgdLGmitPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVL 140
PRK02947 PRK02947
sugar isomerase domain-containing protein;
68-119 2.90e-03

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 38.70  E-value: 2.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488982184  68 LGKNSVVILASQQGNTAETVEAARIARQKGAATIGLV-----------YTPGTPLCEHSDYTI 119
Cdd:PRK02947 104 IRPGDVLIVVSNSGRNPVPIEMALEAKERGAKVIAVTslaysasvasrHSSGKRLAEVADVVL 166
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 23-120 3.08e-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: 37.14  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  23 RVWFVGCGGSltgfwpGKYfldceAKKLA-----VG----YVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIA 93
Cdd:cd05014    2 KVVVTGVGKS------GHI-----ARKIAatlssTGtpafFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHL 70

                         90       100
                 ....*....|....*....|....*..
gi 488982184  94 RQKGAATIGLVYTPGTPLCEHSDYTIE 120
Cdd:cd05014   71 KRRGAPIIAITGNPNSTLAKLSDVVLD 97
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 10-105 3.62e-03

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 38.95  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488982184  10 TIIRDILSKQHIERVwFVGCGGSLTGFW--PGKYfldceakklAVGYVTSNEFV------------HATPNALGKNSVVI 75
Cdd:PRK12778 507 TITIEELEEEGFKGI-FIASGAGLPNFMniPGEN---------SNGVMSSNEYLtrvnlmdaaspdSDTPIKFGKKVAVV 576

                         90       100       110
                 ....*....|....*....|....*....|
gi 488982184  76 LAsqqGNTAetVEAARIARQKGAATIGLVY 105
Cdd:PRK12778 577 GG---GNTA--MDSARTAKRLGAERVTIVY 601
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 26-101 4.89e-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.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 35.81  E-value: 4.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488982184  26 FVGCGGSLTgfwPGKYF--LDCEAKKLAVGYVTSNEFVHATPNALG-KNSVVILASQQGNTAETVEAARIARQKGAATI 101
Cdd:cd04795    3 VIGIGGSGA---IAAYFalELLELTGIEVVALIATELEHASLLSLLrKGDVVIALSYSGRTEELLAALEIAKELGIPVI 78
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH