NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1367558326|gb|PSJ50025|]
View 

SIS domain-containing protein [Klebsiella pneumoniae]

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 1.31e-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: 153.50  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  23 RVWFVGCGGSLTGFWPGKYFLDCEAKkLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQKGAATIG 102
Cdd:cd05710     1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1367558326 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 4.49e-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: 140.80  E-value: 4.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326   4 AHQNAHTIIRDILSK---QHIERVWFVGCGGSltgfW----PGKYFLdCEAKKLAVGYVTSNEFVHATPNALGKNSVVIL 76
Cdd:COG2222    14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  77 ASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIeycwarypeTVDPTQQKA-------AYSLWLALEVLA 149
Cdd:COG2222    89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL---------PLPAGPEKSvaatksfTTMLLALLALLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 150 QTEGyahyDEmvSAFASFESVVRGAQQQVQADARHFAE-AWKTEKVIYMMGSGPSFGAAHqESICILLEMQWINSASIHS 228
Cdd:COG2222   160 AWGG----DD--ALLAALDALPAALEAALAADWPAAALaALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 229 GEYFHGPFEITETGTPFILLKSSGRTRPLDDRAIRFIERYQGKLQIIDVEKVGIDAL--HASVREYFCGLLHNCVLDVYN 306
Cdd:COG2222   233 AEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLpaIPDLHDALDPLLLLVVAQRLA 312

                         330       340
                  ....*....|....*....|
gi 1367558326 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 1.31e-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: 153.50  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  23 RVWFVGCGGSLTGFWPGKYFLDCEAKkLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQKGAATIG 102
Cdd:cd05710     1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1367558326 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 4.49e-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: 140.80  E-value: 4.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326   4 AHQNAHTIIRDILSK---QHIERVWFVGCGGSltgfW----PGKYFLdCEAKKLAVGYVTSNEFVHATPNALGKNSVVIL 76
Cdd:COG2222    14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  77 ASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIeycwarypeTVDPTQQKA-------AYSLWLALEVLA 149
Cdd:COG2222    89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL---------PLPAGPEKSvaatksfTTMLLALLALLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 150 QTEGyahyDEmvSAFASFESVVRGAQQQVQADARHFAE-AWKTEKVIYMMGSGPSFGAAHqESICILLEMQWINSASIHS 228
Cdd:COG2222   160 AWGG----DD--ALLAALDALPAALEAALAADWPAAALaALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 229 GEYFHGPFEITETGTPFILLKSSGRTRPLDDRAIRFIERYQGKLQIIDVEKVGIDAL--HASVREYFCGLLHNCVLDVYN 306
Cdd:COG2222   233 AEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLpaIPDLHDALDPLLLLVVAQRLA 312

                         330       340
                  ....*....|....*....|
gi 1367558326 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 5.75e-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: 116.59  E-value: 5.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 181 DARHFAEAWKTEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITETGTPFILLKSSGRTRPLDDR 260
Cdd:cd05009     2 DIKELAEKLKEAKSFYVLGRGPNYGTA-LEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367558326 261 AIRFIERYQGKLQIIDVEKVGIDA-----LHASVREYFCGLLHNCVLDVYNLALATAR-NHPLTTRRYMWKVE 327
Cdd:cd05009    81 LIKEVKARGAKVIVITDDGDAKDLadvviRVPATVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKSVT 153
frlB PRK11382
fructoselysine 6-phosphate deglycase;
9-280 2.11e-26

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 107.01  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326   9 HTIIRDILsKQHIERVWFVGCGGSLTGFWPGKYFLDcEAKKLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVE 88
Cdd:PRK11382   33 HAIVEEMV-KRDIDRIYFVACGSPLNAAQTAKHLAD-RFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIK 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  89 AARIARQKGAATIGLVYTPGTPLCEHSDYTIEYcwarYPETVDPTQQKAAYSLwlALEVLAQTEGYAHYDEMVSAFASFE 168
Cdd:PRK11382  111 ALELGRACGALTAAFTKRADSPITSAAEFSIDY----QADCIWEIHLLLCYSV--VLEMITRLAPNAEIGKIKNDLKQLP 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 169 SVVRGAQQQVQADARHFAEAWKTEKVIYMMGSGPSFGAAHQESICILLEMQWINSASIHSGEYFHGPFEITETGTPFILL 248
Cdd:PRK11382  185 NALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFL 264

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1367558326 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 3.77e-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: 60.01  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  15 ILSKQHieRVWFVGCGGSLTGFWPGKYFLDCEAKKLAVGYVTSnEFVHATPNALGKNSVVILASQQGNTAETVEAARIAR 94
Cdd:pfam01380   1 LLAKAK--RIFVIGRGTSYAIALELALKFEEIGYKVVEVELAS-ELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAK 77

                          90       100
                  ....*....|....*....|....*
gi 1367558326  95 QKGAATIGLVYTPGTPLCEHSDYTI 119
Cdd:pfam01380  78 ARGAKIIAITDSPGSPLAREADHVL 102
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 22-121 4.35e-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: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  22 ERVWFVGCGGSltgFWPGKYFldceAKKL------AVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQ 95
Cdd:COG1737   135 RRIYIFGVGAS---APVAEDL----AYKLlrlgknVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKE 207

                          90       100
                  ....*....|....*....|....*.
gi 1367558326  96 KGAATIGLVYTPGTPLCEHSDYTIEY 121
Cdd:COG1737   208 RGAKVIAITDSPLSPLAKLADVVLYV 233
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 14-248 1.76e-09

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 58.88  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  14 DILSKQHIErvwFVGCGGSLTGFWPGKYFLdceaKKLA----VGYVTSNEF-VHATPNalgKNSVVILASQQGNTAETVE 88
Cdd:PTZ00295  318 ELLNIKNLI---LVGCGTSYYAALFAASIM----QKLKcfntVQVIDASELtLYRLPD---EDAGVIFISQSGETLDVVR 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  89 AARIARQKGAATIGLVYTPGTPLCEHSDYTIEYCWAR---YPETVDPTQQKAAYSLwLALEVLAQTEGYAHYD---EMVS 162
Cdd:PTZ00295  388 ALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGRevaVASTKAFTSQVTVLSL-IALWFAQNKEYSCSNYkcsSLIN 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 163 AFASFESVVRGAQQQVQADARHFAEAWKTEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEI--TE 240
Cdd:PTZ00295  467 SLHRLPTYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIA-LEGALKIKEITYIHAEGFSGGALKHGPFALidKE 545


                  ....*...
gi 1367558326 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 1.31e-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: 153.50  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  23 RVWFVGCGGSLTGFWPGKYFLDCEAKkLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQKGAATIG 102
Cdd:cd05710     1 NVFFVGCGGSLADMYPAKYFLKKESK-LPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1367558326 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 4.49e-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: 140.80  E-value: 4.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326   4 AHQNAHTIIRDILSK---QHIERVWFVGCGGSltgfW----PGKYFLdCEAKKLAVGYVTSNEFVHATPNALGKNSVVIL 76
Cdd:COG2222    14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  77 ASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTIeycwarypeTVDPTQQKA-------AYSLWLALEVLA 149
Cdd:COG2222    89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL---------PLPAGPEKSvaatksfTTMLLALLALLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 150 QTEGyahyDEmvSAFASFESVVRGAQQQVQADARHFAE-AWKTEKVIYMMGSGPSFGAAHqESICILLEMQWINSASIHS 228
Cdd:COG2222   160 AWGG----DD--ALLAALDALPAALEAALAADWPAAALaALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 229 GEYFHGPFEITETGTPFILLKSSGRTRPLDDRAIRFIERYQGKLQIIDVEKVGIDAL--HASVREYFCGLLHNCVLDVYN 306
Cdd:COG2222   233 AEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLpaIPDLHDALDPLLLLVVAQRLA 312

                         330       340
                  ....*....|....*....|
gi 1367558326 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 5.75e-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: 116.59  E-value: 5.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 181 DARHFAEAWKTEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITETGTPFILLKSSGRTRPLDDR 260
Cdd:cd05009     2 DIKELAEKLKEAKSFYVLGRGPNYGTA-LEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367558326 261 AIRFIERYQGKLQIIDVEKVGIDA-----LHASVREYFCGLLHNCVLDVYNLALATAR-NHPLTTRRYMWKVE 327
Cdd:cd05009    81 LIKEVKARGAKVIVITDDGDAKDLadvviRVPATVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKSVT 153
frlB PRK11382
fructoselysine 6-phosphate deglycase;
9-280 2.11e-26

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 107.01  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326   9 HTIIRDILsKQHIERVWFVGCGGSLTGFWPGKYFLDcEAKKLAVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVE 88
Cdd:PRK11382   33 HAIVEEMV-KRDIDRIYFVACGSPLNAAQTAKHLAD-RFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIK 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  89 AARIARQKGAATIGLVYTPGTPLCEHSDYTIEYcwarYPETVDPTQQKAAYSLwlALEVLAQTEGYAHYDEMVSAFASFE 168
Cdd:PRK11382  111 ALELGRACGALTAAFTKRADSPITSAAEFSIDY----QADCIWEIHLLLCYSV--VLEMITRLAPNAEIGKIKNDLKQLP 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 169 SVVRGAQQQVQADARHFAEAWKTEKVIYMMGSGPSFGAAHQESICILLEMQWINSASIHSGEYFHGPFEITETGTPFILL 248
Cdd:PRK11382  185 NALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFL 264

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1367558326 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 7.24e-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: 7.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  23 RVWFVGCGGSL-TGFwPGKYFLDcEAKKLAVGYVTSNEFVHATPNaLGKNSVVILASQQGNTAETVEAARIARQKGAATI 101
Cdd:cd05008     1 RILIVGCGTSYhAAL-VAKYLLE-RLAGIPVEVEAASEFRYRRPL-LDEDTLVIAISQSGETADTLAALRLAKEKGAKTV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1367558326 102 GLVYTPGTPLCEHSDYTIeYCWARYPETVDPTqqKAAYS-----LWLALEV 147
Cdd:cd05008    78 AITNVVGSTLAREADYVL-YLRAGPEISVAAT--KAFTSqllalLLLALAL 125
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 11-279 2.95e-12

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 67.21  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  11 IIRDILSKQhieRVWFVGCGGSLTGFWPGKYFLDcEAKKLAVGYVTSNEFVHATPNaLGKNSVVILASQQGNTAETVEAA 90
Cdd:PTZ00394  347 SIRAILTSR---RILFIACGTSLNSCLAVRPLFE-ELVPLPISVENASDFLDRRPR-IQRDDVCFFVSQSGETADTLMAL 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  91 RIARQKGAATIGLVYTPGTPLCEHSDYTIEYcwaRYPETVDPTQQKAAYSLWLALEVLA------QTEGYAHYDEMVSAF 164
Cdd:PTZ00394  422 QLCKEAGAMCVGITNVVGSSISRLTHYAIHL---NAGVEVGVASTKAYTSQVVVLTLVAlllssdSVRLQERRNEIIRGL 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 165 ASFESVVRGAQQQVQADARHFAEAWKTEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITETGTP 244
Cdd:PTZ00394  499 AELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATA-MEAALKVKELSYVHTEGIHSGELKHGPLALIDETSP 577

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1367558326 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 3.77e-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: 60.01  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  15 ILSKQHieRVWFVGCGGSLTGFWPGKYFLDCEAKKLAVGYVTSnEFVHATPNALGKNSVVILASQQGNTAETVEAARIAR 94
Cdd:pfam01380   1 LLAKAK--RIFVIGRGTSYAIALELALKFEEIGYKVVEVELAS-ELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAK 77

                          90       100
                  ....*....|....*....|....*
gi 1367558326  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 6.02e-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: 6.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  22 ERVWFVGCGGSltgFWPGKYFldceAKKL-----AVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQK 96
Cdd:cd05013    14 RRIYIFGVGSS---GLVAEYL----AYKLlrlgkPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86

                          90       100
                  ....*....|....*....|....*
gi 1367558326  97 GAATIGLVYTPGTPLCEHSDYTIEY 121
Cdd:cd05013    87 GAKVIAITDSANSPLAKLADIVLLV 111
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 22-121 4.35e-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: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  22 ERVWFVGCGGSltgFWPGKYFldceAKKL------AVGYVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIARQ 95
Cdd:COG1737   135 RRIYIFGVGAS---APVAEDL----AYKLlrlgknVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKE 207

                          90       100
                  ....*....|....*....|....*.
gi 1367558326  96 KGAATIGLVYTPGTPLCEHSDYTIEY 121
Cdd:COG1737   208 RGAKVIAITDSPLSPLAKLADVVLYV 233
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 14-248 1.76e-09

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 58.88  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  14 DILSKQHIErvwFVGCGGSLTGFWPGKYFLdceaKKLA----VGYVTSNEF-VHATPNalgKNSVVILASQQGNTAETVE 88
Cdd:PTZ00295  318 ELLNIKNLI---LVGCGTSYYAALFAASIM----QKLKcfntVQVIDASELtLYRLPD---EDAGVIFISQSGETLDVVR 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  89 AARIARQKGAATIGLVYTPGTPLCEHSDYTIEYCWAR---YPETVDPTQQKAAYSLwLALEVLAQTEGYAHYD---EMVS 162
Cdd:PTZ00295  388 ALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGRevaVASTKAFTSQVTVLSL-IALWFAQNKEYSCSNYkcsSLIN 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326 163 AFASFESVVRGAQQQVQADARHFAEAWKTEKVIYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEI--TE 240
Cdd:PTZ00295  467 SLHRLPTYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIA-LEGALKIKEITYIHAEGFSGGALKHGPFALidKE 545


                  ....*...
gi 1367558326 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 1367558326  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 4.28e-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: 47.13  E-value: 4.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1367558326  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 1367558326  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 1367558326  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 2.63e-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: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367558326  23 RVWFVGCGGSltgFWPGKYFLDCEAKKLAVgyvtsNEFVHAT---PNALGKNSVVILASQQGNTAETVEAARIARQKGAA 99
Cdd:cd05017     1 NIVILGMGGS---GIGGDLLESLLLDEAKI-----PVYVVKDytlPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAK 72


                  ..
gi 1367558326 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 1367558326  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 1367558326  12 IRDILSKQHIERVWFVGcGGSLTGfwpgkyfLDCEAKKLAVGYVTSNE---FVHAT-PNALGKNSVVILASQQGNTAETV 87
Cdd:PRK15482  128 IIEVISKAPFIQITGLG-GSALVG-------RDLSFKLMKIGYRVACEadtHVQATvSQALKKGDVQIAISYSGSKKEIV 199

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1367558326  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 1367558326  21 IERVWFVGCGGSLTGfwpGKYFLDCEAKKLAVGYVTSNEFVhaTPNALGKNSVVILASQQGNTAETVEAARIARQKGAAT 100
Cdd:PRK08674   34 IDNIVISGMGGSGIG---GDLLRILLFDELKVPVFVNRDYT--LPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKI 108


                  .
gi 1367558326 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 1367558326  60 FVHATpNA----LG---KNSVVILASQQGNTAETVEAARIARQKGAATIGLVYTPGTPLCEHSDYTI 119
Cdd:COG0794    75 FLHPA-EAshgdLGmitPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVL 140
PRK02947 PRK02947
sugar isomerase domain-containing protein;
68-119 2.83e-03

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 38.70  E-value: 2.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367558326  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 1367558326  23 RVWFVGCGGSltgfwpGKYfldceAKKLA-----VG----YVTSNEFVHATPNALGKNSVVILASQQGNTAETVEAARIA 93
Cdd:cd05014     2 KVVVTGVGKS------GHI-----ARKIAatlssTGtpafFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHL 70

                          90       100
                  ....*....|....*....|....*..
gi 1367558326  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 1367558326  10 TIIRDILSKQHIERVwFVGCGGSLTGFW--PGKYfldceakklAVGYVTSNEFV------------HATPNALGKNSVVI 75
Cdd:PRK12778  507 TITIEELEEEGFKGI-FIASGAGLPNFMniPGEN---------SNGVMSSNEYLtrvnlmdaaspdSDTPIKFGKKVAVV 576

                          90       100       110
                  ....*....|....*....|....*....|
gi 1367558326  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 4.74e-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: 4.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1367558326  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