|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11557 |
PRK11557 |
MurR/RpiR family transcriptional regulator; |
5-282 |
0e+00 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 517.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 5 TRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALASAPTPQSVP 84
Cdd:PRK11557 1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 85 VHNQIRGDDPLRLVGEKLIKDNVAAMHASLDVNTEEKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGINAVSE 164
Cdd:PRK11557 81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 165 QDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAITGFNPNALQQQATLCLYTIAEEQATRSAAISS 244
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 503996404 245 TSAQMMLTDLLFMGLVQQDLEHAPERIRHSEALVKKLV 282
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
1-281 |
7.52e-82 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 247.92 E-value: 7.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 1 MNCLTRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALASapTP 80
Cdd:COG1737 5 MSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAE--GL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 81 QSVPVHNQIRGDDPLRLVGEKLIKDNVAAMHASLDVNTEEKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGIN 160
Cdd:COG1737 83 SSYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 161 AVS-EQDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAITGFNPNALQQQATLCLYTIAEEQATRS 239
Cdd:COG1737 163 VVLlDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503996404 240 AAISSTSAQMMLTDLLFMGLVQQDLEHAPERIRHSEALVKKL 281
Cdd:COG1737 243 SAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
120-258 |
5.33e-35 |
|
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: 123.11 E-value: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 120 EKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGINAVSEQDMHALLATVQAMSPDDLLLAISYSGERREINMAA 199
Cdd:cd05013 1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 503996404 200 GEALRVGSQILAITGFNPNALQQQATLCLYTIAEEQATRSAAISSTSAQMMLTDLLFMG 258
Cdd:cd05013 81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
|
|
| HTH_6 |
pfam01418 |
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ... |
1-76 |
1.93e-27 |
|
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best characterized member of this family is Swiss:P39266. RpiR is a regulator of the expression of rpiB gene.
Pssm-ID: 334531 [Multi-domain] Cd Length: 77 Bit Score: 101.25 E-value: 1.93e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996404 1 MNCLTRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALAS 76
Cdd:pfam01418 1 MGLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
|
|
| G6PI_arch |
TIGR02128 |
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ... |
134-213 |
4.26e-04 |
|
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member of the larger PGI superfamily and only distantly related to other glucose-6-phosphate isomerases. The family is limited to the archaea.
Pssm-ID: 273988 [Multi-domain] Cd Length: 308 Bit Score: 41.27 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 134 RVIITGIGASGLVARNFS-WKLMKIGINAVSEQDMHALLATVQAmspDDLLLAISYSGERREINMAAGEALRVGSQILAI 212
Cdd:TIGR02128 23 EIVICGMGGSGIAGRIISiLLLEKSFQGPVFVVKDYRLPRFVDG---KTLLIAVSYSGNTEETLSAVEEAKKKGAKVIAI 99
|
.
gi 503996404 213 T 213
Cdd:TIGR02128 100 T 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11557 |
PRK11557 |
MurR/RpiR family transcriptional regulator; |
5-282 |
0e+00 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 517.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 5 TRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALASAPTPQSVP 84
Cdd:PRK11557 1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 85 VHNQIRGDDPLRLVGEKLIKDNVAAMHASLDVNTEEKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGINAVSE 164
Cdd:PRK11557 81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 165 QDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAITGFNPNALQQQATLCLYTIAEEQATRSAAISS 244
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 503996404 245 TSAQMMLTDLLFMGLVQQDLEHAPERIRHSEALVKKLV 282
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
1-281 |
7.52e-82 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 247.92 E-value: 7.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 1 MNCLTRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALASapTP 80
Cdd:COG1737 5 MSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAE--GL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 81 QSVPVHNQIRGDDPLRLVGEKLIKDNVAAMHASLDVNTEEKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGIN 160
Cdd:COG1737 83 SSYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 161 AVS-EQDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAITGFNPNALQQQATLCLYTIAEEQATRS 239
Cdd:COG1737 163 VVLlDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503996404 240 AAISSTSAQMMLTDLLFMGLVQQDLEHAPERIRHSEALVKKL 281
Cdd:COG1737 243 SAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| PRK15482 |
PRK15482 |
HTH-type transcriptional regulator MurR; |
1-281 |
3.85e-58 |
|
HTH-type transcriptional regulator MurR;
Pssm-ID: 185379 [Multi-domain] Cd Length: 285 Bit Score: 187.60 E-value: 3.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 1 MNCLTRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALASA--- 77
Cdd:PRK15482 1 MLYLTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMALIGEYSASrek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 78 PTPQSVPVHNQIRGDDPLRLVGEKLIKDNVAAMHASLDVNTEEKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKI 157
Cdd:PRK15482 81 TNATALHLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 158 GINAVSEQDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAITGFNPNALQQQATLCLYTIAEEQAT 237
Cdd:PRK15482 161 GYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEW 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 503996404 238 RSAAISSTSAQMMLTDLLFMGLVQQDLEHAPERIRHSEALVKKL 281
Cdd:PRK15482 241 RSSSMSTRTAQNSVTDLLFVGLVQLNDVESLKMIQRSSELTQRL 284
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
120-258 |
5.33e-35 |
|
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: 123.11 E-value: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 120 EKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGINAVSEQDMHALLATVQAMSPDDLLLAISYSGERREINMAA 199
Cdd:cd05013 1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 503996404 200 GEALRVGSQILAITGFNPNALQQQATLCLYTIAEEQATRSAAISSTSAQMMLTDLLFMG 258
Cdd:cd05013 81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
6-279 |
5.71e-34 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 124.87 E-value: 5.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 6 RIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALASAPTPqsvpV 85
Cdd:PRK11337 18 YIRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSEQV----L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 86 HNQIRGDDPLRLVGEKLIKDNVAAMHASLDVNTEEKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGINAVSEQ 165
Cdd:PRK11337 94 HSELSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 166 DMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAITGFNPNALQQQATLCLYTIAEEQATRSAAISST 245
Cdd:PRK11337 174 DAHIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLGENAAAR 253
|
250 260 270
....*....|....*....|....*....|....
gi 503996404 246 SAQMMLTDLLFMGLVQQDLEHAPERIRHSEALVK 279
Cdd:PRK11337 254 IAQLNILDAFFVSVAQLNIEQAEINLQKTGAAVD 287
|
|
| PRK14101 |
PRK14101 |
bifunctional transcriptional regulator/glucokinase; |
4-279 |
3.76e-30 |
|
bifunctional transcriptional regulator/glucokinase;
Pssm-ID: 184507 [Multi-domain] Cd Length: 638 Bit Score: 119.25 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 4 LTRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALaSAPTPQSv 83
Cdd:PRK14101 344 FERIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGL-TGTIPMS- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 84 pvHNQIRGDDPLRLVGEKLIKDNVAAMHASLDVNTEEKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGINAVS 163
Cdd:PRK14101 422 --HSQVHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 164 EQDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAITGFNpNALQQQATLCLYTIAEEQATRSAAIS 243
Cdd:PRK14101 500 YGDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSSN-TPLAKRATVALETDHIEMRESQLSMI 578
|
250 260 270
....*....|....*....|....*....|....*.
gi 503996404 244 STSAQMMLTDLLFMGLVqqdLEHAPERIRHSEALVK 279
Cdd:PRK14101 579 SRILHLVMIDILAVGVA---IRRAAPNAELAEAVAR 611
|
|
| HTH_6 |
pfam01418 |
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ... |
1-76 |
1.93e-27 |
|
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best characterized member of this family is Swiss:P39266. RpiR is a regulator of the expression of rpiB gene.
Pssm-ID: 334531 [Multi-domain] Cd Length: 77 Bit Score: 101.25 E-value: 1.93e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996404 1 MNCLTRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALAS 76
Cdd:pfam01418 1 MGLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
|
|
| PRK11302 |
PRK11302 |
DNA-binding transcriptional regulator HexR; Provisional |
1-258 |
1.56e-26 |
|
DNA-binding transcriptional regulator HexR; Provisional
Pssm-ID: 183082 [Multi-domain] Cd Length: 284 Bit Score: 104.69 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 1 MNCLTRIRQRYPTLAASDKKLADFILAQPDQTRHLSSQQLAGEAGVSQSSVVKFAQKMGFKGFPALKLALSEALASApTP 80
Cdd:PRK11302 1 MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLANG-TP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 81 QsvpVHNQIRGDDPLRLVGEKLIKDNVAAM---HASLDVNTEEKlleAVTLLRHARRVIITGIGASGLVARNFSWKLMKI 157
Cdd:PRK11302 80 Y---VNRNVEEDDSVEAYTGKIFESAMASLdhaRQSLDPSAINR---AVDLLTQAKKISFFGLGASAAVAHDAQNKFFRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 158 GINAVSEQDMhallaTVQAMS-----PDDLLLAISYSGERREINMAAGEALRVGSQILAITgfNPNA-LQQQATLCLYTI 231
Cdd:PRK11302 154 NVPVVYFDDI-----VMQRMScmnssDGDVVVLISHTGRTKSLVELAQLARENGATVIAIT--SAGSpLAREATLALTLD 226
|
250 260
....*....|....*....|....*..
gi 503996404 232 AEEQATRSAAISSTSAQMMLTDLLFMG 258
Cdd:PRK11302 227 VPEDTDIYMPMVSRIAQLTVIDVLATG 253
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
128-257 |
1.92e-26 |
|
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: 100.45 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 128 LLRHARRVIITGIGASGLVARNFSWKLMKIGINAVSEQDMHALLATVQAM-SPDDLLLAISYSGERREINMAAGEALRVG 206
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALvDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 503996404 207 SQILAITGFNPNALQQQATLCLYTIAEEQaTRSAAISSTSAQMMLTDLLFM 257
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPE-TGVASTKSITAQLAALDALAV 130
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
110-229 |
1.03e-15 |
|
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: 73.38 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 110 MHASLDVNTEEKLLEAVTLLRHARRVIITGIGASGLVARNFSWKLMKIGINA--VSEqdmhallATVQAMSPDDLLLAIS 187
Cdd:cd05005 11 IENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVyvVGE-------TTTPAIGPGDLLIAIS 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 503996404 188 YSGERREINMAAGEALRVGSQILAITGFNPNALQQQATLCLY 229
Cdd:cd05005 84 GSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
107-259 |
1.76e-13 |
|
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: 69.23 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 107 VAAMHASLDvnteEKLLEAVTLLRHAR-RVIITGIGASGLVARNFSWKLMKIGINAVSeqdMHAL------LATVQamsP 179
Cdd:COG0794 22 LAALAERLD----ESFEKAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGTPAFF---LHPAeashgdLGMIT---P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 180 DDLLLAISYSGERREINMAAGEALRVGSQILAITGfNPN-ALQQQATLCLYTIAEEQATRS--AAISSTSAQMMLTDLLF 256
Cdd:COG0794 92 GDVVIAISNSGETEELLALLPLLKRLGVPLIAITG-NPDsTLARAADVVLDLPVEREACPLnlAPTTSTTATLALGDALA 170
|
...
gi 503996404 257 MGL 259
Cdd:COG0794 171 VAL 173
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
133-257 |
3.20e-13 |
|
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: 64.87 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 133 RRVIITGIGASGLVARNFSWKLMKIGINAVSEQDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAI 212
Cdd:cd05014 1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 503996404 213 TGFNPNALQQQATLCL-YTIAEEQATRS-AAISSTSAQMMLTDLLFM 257
Cdd:cd05014 81 TGNPNSTLAKLSDVVLdLPVEEEACPLGlAPTTSTTAMLALGDALAV 127
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
135-213 |
9.17e-09 |
|
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: 51.61 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 135 VIITGIGASGLVARNFSWKLMKI-GINAVSEQDMHALLA-TVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAI 212
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELtGIEVVALIATELEHAsLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 503996404 213 T 213
Cdd:cd04795 81 T 81
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
134-213 |
1.00e-06 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 46.87 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 134 RVIITGIGASGLVARNF-SWKLMKIGINAVSEQDMHaLLATVqamSPDDLLLAISYSGERREINMAAGEALRVGSQILAI 212
Cdd:cd05017 1 NIVILGMGGSGIGGDLLeSLLLDEAKIPVYVVKDYT-LPAFV---DRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAI 76
|
.
gi 503996404 213 T 213
Cdd:cd05017 77 T 77
|
|
| gutQ |
PRK11543 |
arabinose-5-phosphate isomerase GutQ; |
127-262 |
1.71e-06 |
|
arabinose-5-phosphate isomerase GutQ;
Pssm-ID: 183186 [Multi-domain] Cd Length: 321 Bit Score: 48.61 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 127 TLLRHARRVIITGIGASGLVARNFSWKLMKIGINAVSEQDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVG 206
Cdd:PRK11543 37 IILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKS 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 503996404 207 SQILAITGFNPNALQQQATLCLYTIAEEQA--TRSAAISSTSAQMMLTDLLFMGLVQQ 262
Cdd:PRK11543 117 IALLAMTGKPTSPLGLAAKAVLDISVEREAcpMHLAPTSSTVNTLMMGDALAMAVMQA 174
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
134-256 |
1.52e-05 |
|
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: 43.64 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 134 RVIITGIGAS---GLVARNFSWKLMKIGINAV--SEQDMHALLAtvqamSPDDLLLAISYSGERREINMAAGEALRVGSQ 208
Cdd:cd05008 1 RILIVGCGTSyhaALVAKYLLERLAGIPVEVEaaSEFRYRRPLL-----DEDTLVIAISQSGETADTLAALRLAKEKGAK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 503996404 209 ILAITGFNPNALQQQATLCLYTIA-EEQATRS--AAISSTSAQMMLTDLLF 256
Cdd:cd05008 76 TVAITNVVGSTLAREADYVLYLRAgPEISVAAtkAFTSQLLALLLLALALA 126
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
129-213 |
4.75e-05 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 44.20 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 129 LRHARRVIITGIGASGLV---ARNFSWKLMKIGINAVseQDMHaLLATVqamSPDDLLLAISYSGERREINMAAGEALRV 205
Cdd:PRK08674 31 LEKIDNIVISGMGGSGIGgdlLRILLFDELKVPVFVN--RDYT-LPAFV---DEKTLVIAVSYSGNTEETLSAVEQALKR 104
|
....*...
gi 503996404 206 GSQILAIT 213
Cdd:PRK08674 105 GAKIIAIT 112
|
|
| G6PI_arch |
TIGR02128 |
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ... |
134-213 |
4.26e-04 |
|
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member of the larger PGI superfamily and only distantly related to other glucose-6-phosphate isomerases. The family is limited to the archaea.
Pssm-ID: 273988 [Multi-domain] Cd Length: 308 Bit Score: 41.27 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 134 RVIITGIGASGLVARNFS-WKLMKIGINAVSEQDMHALLATVQAmspDDLLLAISYSGERREINMAAGEALRVGSQILAI 212
Cdd:TIGR02128 23 EIVICGMGGSGIAGRIISiLLLEKSFQGPVFVVKDYRLPRFVDG---KTLLIAVSYSGNTEETLSAVEEAKKKGAKVIAI 99
|
.
gi 503996404 213 T 213
Cdd:TIGR02128 100 T 100
|
|
| PRK10892 |
PRK10892 |
arabinose-5-phosphate isomerase KdsD; |
134-261 |
2.26e-03 |
|
arabinose-5-phosphate isomerase KdsD;
Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 38.94 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 134 RVIITGIGASGLVARNFSWKLMKIGINAVSEQDMHALLATVQAMSPDDLLLAISYSGERREINMAAGEALRVGSQILAIT 213
Cdd:PRK10892 49 KVVVMGMGKSGHIGRKMAATFASTGTPSFFVHPGEAAHGDLGMVTPQDVVIAISNSGESSEILALIPVLKRLHVPLICIT 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 503996404 214 GfNPNALQQQAT---LCLYTIAEEQATRSAAISSTSAQMMLTDLLFMGLVQ 261
Cdd:PRK10892 129 G-RPESSMARAAdihLCVKVPKEACPLGLAPTSSTTATLVMGDALAVALLK 178
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
130-256 |
2.28e-03 |
|
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: 39.11 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996404 130 RHARRVIITGIGASGLVARnfswkLMKIGINAVSEQDMHALLATVQAMSP------DDLLLAISYSGERREINMAAGEAL 203
Cdd:COG2222 32 KPPRRVVLVGAGSSDHAAQ-----AAAYLLERLLGIPVAALAPSELVVYPaylkleGTLVVAISRSGNSPEVVAALELAK 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 503996404 204 RVGSQILAITGFNPNALQQQATLCLYT-IAEEQATrsAAISSTSAQMMLTDLLF 256
Cdd:COG2222 107 ARGARTLAITNNPDSPLAEAADRVLPLpAGPEKSV--AATKSFTTMLLALLALL 158
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
179-229 |
3.59e-03 |
|
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).
Pssm-ID: 240139 [Multi-domain] Cd Length: 177 Bit Score: 37.49 E-value: 3.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503996404 179 PDDLLLAISYSGERREINMAAGEALRVGSQILAITGFNPNALQQQATLCLY 229
Cdd:cd05006 101 PGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIH 151
|
|
| |
